eF-site ID 6msg-ABCDEFGHIJKLMNOPQRSTUVWXYZabcdeghijklmnopqrstuv
PDB Code 6msg
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, g, h, i, j, k, l, m, n, o, p, q, r, s, t, u, v
Title Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
Classification HYDROLASE
Compound 26S proteasome non-ATPase regulatory subunit 1
Source (PSB4_HUMAN)
Sequence A:  ESDTGLAPPALWDLAADKQTLQSEQPLQVARCTKIINADS
EDPKYIINVKQFAKFVVDLSDQVAPTDIEEGMRVGVDRNK
YQIHIPLPPKIDPTVTMMQVEEKPDVTYSDVGGCKEQIEK
LREVVETPLLHPERFVNLGIEPPKGVLLFGPPGTGKTLCA
RAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMART
KKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQL
DGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKIEFSLP
DLEGRTHIFKIHARSMSVERDIRFELLARLCPNSTGAEIR
SVCTEAGMFAIRARRKIATEKDFLEAVNKVIKSYAK
B:  EERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYV
SILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTV
MKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEE
MGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGS
ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTK
RYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNR
IETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMT
LADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMK
VTNEDFKKSKENVLYKKQEGTPEGLYL
C:  LEEGKAGSGLRQYYLSKIEELQLIVNDKSQNLRRLQAQRN
ELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVH
PEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNK
VDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVK
HPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCT
FIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDE
IDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIK
VIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILK
IHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYA
LRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
D:  DLYSRYKKLQQELEFLEVQEEYIKDEQKNLKKEFLHAQEE
VKRIQSIPLVIGQFLEAVDQNTAIVGSTTGSNYYVRILST
IDRELLKPNASVALHKHSNALVDVLPPEADSSIMMLTSDQ
KPDVMYADIGGMDIQKQEVREAVELPLTHFELYKQIGIDP
PRGVLMYGPPGCGKTMLAKAVAHHTTAAFIRVVGSEFVQK
YLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQ
TGADREVQRILLELLNQMDGFDQNVNVKVIMATNRADTLD
PALLRPGRLDRKIEFPLPDRRQKRLIFSTITSKMNLSEEV
DLEDYVARPDKISGADINSICQESGMLAVRENRYIVLAKD
FEKAYKTVIKKDEQEHEFYK
E:  MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQY
EKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYV
VGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVY
NMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQ
RVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVS
SSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGG
RRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATN
RPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPI
TKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHD
FVVQEDFMKAVRKVADSKKLESKLDYKPV
F:  EQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVLRVTH
ELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDVKCAVI
KTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETL
PTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVL
PMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQT
KATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIF
IDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNT
QVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEEARAR
IMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAG
MIALRRGATELTHEDYMEGILEVQAKKKANLQYYA
G:  SSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRG
KDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMT
ADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQV
YTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFK
ATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLST
VLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAE
H:  ERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAAN
GVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPD
YRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYT
QSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATA
MGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQ
MTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA
I:  SRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILAND
GVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITS
DANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAY
TQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKA
TCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTM
DVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHE
EEEAKAEREK
J:  SYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIV
VLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADAR
IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQS
NGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAI
GRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQS
GGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENE
K:  YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVC
LAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT
LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEED
SRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSA
SEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNAT
NIELATVQPGQNFHMFTKEELEEVIKDI
L:  NQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTH
AVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARL
LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRY
GRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGA
RSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQ
DLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQ
M:  TGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDG
VVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADA
RSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTL
YSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCA
IGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEV
KDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLK
N:  TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDR
IFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA
SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMM
VRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL
ALAMERDGSSGGVIRLAAIAESGVERQVLLG
O:  TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPN
IYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN
RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTD
KLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA
AGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLG
RYRCEKGTTAVLTEKITPLE
P:  SIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQK
IFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQ
IKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFI
CSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPD
HLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLK
ARMD
Q:  MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSE
KILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA
ANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDY
LAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELL
RKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQ
R:  TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPY
LLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS
KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNR
ISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI
YQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYS
G
S:  RFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDS
PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNN
KAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGA
VYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQN
VEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTK
EGIREETVSLRKD
T:  TQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNIS
RIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDG
HSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGES
FLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVL
SQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIE
GPLSTETNWDIAHMI
U:  GIISLLDEDEPQLKEFALHKLNAVVNDFWAEISESVDKIE
VLYEDEGFRSRQFAALVASKVFYHLGAFEESLNYALGAGD
LFNVNDNSEYVETIIAKCIDHYTKQCVENADLPEGEKKPI
DQRLEGIVNKMFQRCLDDHKYKQAIGIALETRRLDVFEKT
ILESNDVPGMLAYSLKLCMSLMQNKQFRNKVLRVLVKIYM
NLEKPDFINVCQCLIFLDDPQAVSDILEKLVKEDNLLMAY
QICFDLYESASQQFLSSVIQNLRTDQTLKMIKILSGEMAI
ELHLQFLIRNNNTDLMILKNTKDAVRNSVCHTATVIANSF
MHCGTTSDQFLRDNLEWLARATNWAKFTATASLGVIHKGH
EKEALQLMATYLPKDTSPGSAYQEGGGLYALGLIHANHGG
DIIDYLLNQLKNASNDIVRHGGSLGLGLAAMGTARQDVYD
LLKTNLYQDDAVTGEAAGLALGLVMLGSKNAQAIEDMVGY
AQETQHEKILRGLAVGIALVMYGRMEEADALIESLCRDKD
PILRRSGMYTVAMAYCGSGNNKAIRRLLHVAVSDVNDDVR
RAAVESLGFILFRTPEQCPSVVSLLSESYNPHVRYGAAMA
LGICCAGTGNKEAINLLEPMTNDPVNYVRQGALIASALIM
IQQTEITCPKVNQFRQLYSKVINDKHDDVMAKFGAILAQG
ILDAGGHNVTISLQSRTGHTHMPSVVGVLVFTQFWFWFPL
SHFLSLAYTPTCVIGLNKDLKMPKVQYKSNCKPSTFAYPA
PLEVPPEPNFQLLDNPARVMPAQLKVLTMPETCRYQPFKP
LSIGGIIILKDTSEDIEELVEP
V:  PPGGGEQEPPPPPAPQDVEMKEEAATGGGSTGEADGKTAA
AAAEHSQRELDTVTLEDIKEHVKQLEKAVSGKEPRFVLRA
LRMLPSTSRRLNHYVLYKAVQGFFTSNNATRDFLLPFLEE
PMDTEADLQFRPRTGKAASTPLLPEVEAYLQLLVVIFMMN
SKRYKEAQKISDDLMQKISTQNRRALDLVAAKCYYYHARV
YEFLDKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRN
YLHYSLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKA
IQLEYSEARRTMTNALRKAPQHTAVGFKQTVHKLLIVVEL
LLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQ
VLDQFGEKFQADGTYTLIIRLRHNVIKTGVRMISLSYSRI
SLADIAQKLQLDSPEDAEFIVAKAIRDGVIEASINHEKGY
VQSKEMIDIYSTREPQLAFHQRISFCLDIHNMSVKAMRFP
W:  MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRL
QEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEW
DLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPI
KLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVK
EAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYI
RTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSY
LSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFD
NEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTL
VEDYGMELRKGSLESPATDVFGSTEEGEKRWKDLKNRVVE
HNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNK
TIFAKVDRLAGIINFQRPKDPNNLLNDWSQKLNSLMSLVN
KTTHLIAKEEMIHNLQ
X:  VQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISK
AKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKR
TFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDD
KALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYC
PPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSI
DSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGR
QTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTH
LAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVE
RKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALE
TIQNMSKVVDSLYNKAKKLT
Y:  PKNPDLRIAQLRFLLSLPEHRGDAAVRDELMAAVRDNNMA
PYYEALCKSLDWQIDVDLLNKMKKANEDELKRLDEELEDA
EKNLGESEIRDAMMAKAEYLCRIGDKEGALTAFRKTYDKT
VALGHRLDIVFYLLRIGLFYMDNDLITRNTEKAKSLIEEG
GDWDRRNRLKVYQGLYCVAIRDFKQAAELFLDTVSTFTSY
ELMDYKTFVTYTVYVSMIALERPDLREKVIKGAEILEVLH
SLPAVRQYLFSLYECRYSVFFQSLAVVEQEMKKDWLFAPH
YRYYVREMRIHAYSQLLESYRSLTLGYMAEAFGVGVEFID
QELSRFIAAGRLHCKIDKVNEIVETNRPDSKNWQYQETIK
KGDLLLNRVQKLSRVINM
Z:  AVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQ
KKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKK
VNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVII
DVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGA
EEAEEVGVEHLLRDIKDTTVGTLSQRITNQVHGLKGLNSK
LLDIRSYLEKVATGKLPINHQIIYQLQDVFNLLPDVSLQE
FVKAFYLKTNDQMVVVYLASLIRSVVALHNLINNKIANRD
AEKKEG
a:  VPGFLQQSQNSGPGQPAVWHRLEELYTKKLWHQLTLQVLD
FVQDPCFAQGDGLIKLYENFISEFEHRVNPLSLVEIILHV
VRQMTDPNVALTFLEKTREKVKSSDEAVILCKTAIGALKL
NIGDLQVTKETIEDVEEMLNNLPGVTSVHSRFYDLSSKYY
QTIGNHASYYKDALRFLGCVDIKDLPVSEQQERAFTLGLA
GLLGEGVFNFGELLMHPVLESLRNTDRQWLIDTLYAFNSG
NVERFQTLKTAWGQQPDLAANEAQLLRKIQLLCLMEMTFT
RPANHRQLTFEEIAKSAKITVNEVELLVMKALSVGLVKGS
IDEVDKRVHMTWVQPRVLDLQQIKGMKDRLEFWCTDVKSM
EMLVEHQAHDILT
b:  MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSK
TRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQP
KGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDN
EKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTL
NGKDGTGSHLVTVPPGPSLADALISSPILAG
c:  AVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVD
DYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTG
RPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAV
VVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGH
LNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKK
SWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEED
KMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAM
LDTVVFK
d:  MYEQLKGEWNRKSPNLSKCGEELGRLKLVLLELNFLPTTG
TKLTKQQLILARDILEIGAQWSILRKDIPSFERYMAQLKC
YYFDYKEQLPESAYMHQLLGLNLLFLLSQNRVAEFHTELE
RLPAKDIQTNVYIKHPVSLEQYLMEGSYNKVFLAKGNIPA
ESYTFFIDILLDTIRDEIAGCIEKAYEKILFTEATRILFF
NTPKKMTDYAKKRGWVLGPNNYYSFASQQQKPEDTTIPST
ELAKQVIEYARQLEMIV
e:  MSEKKQPVDEDNWDDDNVEDDFSNQLRAELEKHGYKMETS
g:  SSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRG
KDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMT
ADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQV
YTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFK
ATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLST
VLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAE
h:  ERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAAN
GVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPD
YRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYT
QSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATA
MGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQ
MTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA
i:  SRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILAND
GVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITS
DANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAY
TQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKA
TCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTM
DVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHE
EEEAKAEREK
j:  SYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIV
VLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADAR
IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQS
NGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAI
GRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQS
GGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENE
k:  YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVC
LAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT
LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEED
SRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSA
SEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNAT
NIELATVQPGQNFHMFTKEELEEVIKDI
l:  NQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTH
AVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARL
LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRY
GRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGA
RSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQ
DLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQ
m:  TGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDG
VVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADA
RSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTL
YSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCA
IGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEV
KDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLK
n:  TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDR
IFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA
SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMM
VRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL
ALAMERDGSSGGVIRLAAIAESGVERQVLLG
o:  TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPN
IYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN
RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTD
KLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA
AGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLG
RYRCEKGTTAVLTEKITPLE
p:  SIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQK
IFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQ
IKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFI
CSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPD
HLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLK
ARMD
q:  MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSE
KILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA
ANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDY
LAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELL
RKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQ
r:  TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPY
LLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS
KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNR
ISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI
YQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYS
G
s:  RFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDS
PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNN
KAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGA
VYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQN
VEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTK
EGIREETVSLRKD
t:  TQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNIS
RIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDG
HSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGES
FLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVL
SQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIE
GPLSTETNWDIAHMI
u:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQRESTLHLVLRLRGG
v:  XXXXXXXXXXXXXXXXXXXXXXXX
Description (1)  26S proteasome


Functional site

1) chain c
residue 113
type
sequence H
description binding site for residue ZN c 401
source : AC1

2) chain c
residue 115
type
sequence H
description binding site for residue ZN c 401
source : AC1

3) chain c
residue 126
type
sequence D
description binding site for residue ZN c 401
source : AC1

4) chain u
residue 76
type
sequence G
description binding site for residue ZN c 401
source : AC1

5) chain A
residue 176
type
sequence D
description binding site for residue ADP A 501
source : AC2

6) chain A
residue 177
type
sequence V
description binding site for residue ADP A 501
source : AC2

7) chain A
residue 178
type
sequence G
description binding site for residue ADP A 501
source : AC2

8) chain A
residue 219
type
sequence G
description binding site for residue ADP A 501
source : AC2

9) chain A
residue 220
type
sequence T
description binding site for residue ADP A 501
source : AC2

10) chain A
residue 222
type
sequence K
description binding site for residue ADP A 501
source : AC2

11) chain A
residue 223
type
sequence T
description binding site for residue ADP A 501
source : AC2

12) chain A
residue 224
type
sequence L
description binding site for residue ADP A 501
source : AC2

13) chain A
residue 353
type
sequence H
description binding site for residue ADP A 501
source : AC2

14) chain A
residue 354
type
sequence I
description binding site for residue ADP A 501
source : AC2

15) chain A
residue 358
type
sequence H
description binding site for residue ADP A 501
source : AC2

16) chain A
residue 382
type
sequence G
description binding site for residue ADP A 501
source : AC2

17) chain C
residue 150
type
sequence M
description binding site for residue ATP C 501
source : AC3

18) chain C
residue 151
type
sequence I
description binding site for residue ATP C 501
source : AC3

19) chain C
residue 192
type
sequence P
description binding site for residue ATP C 501
source : AC3

20) chain C
residue 193
type
sequence G
description binding site for residue ATP C 501
source : AC3

21) chain C
residue 194
type
sequence T
description binding site for residue ATP C 501
source : AC3

22) chain C
residue 195
type
sequence G
description binding site for residue ATP C 501
source : AC3

23) chain C
residue 196
type
sequence K
description binding site for residue ATP C 501
source : AC3

24) chain C
residue 197
type
sequence T
description binding site for residue ATP C 501
source : AC3

25) chain C
residue 198
type
sequence L
description binding site for residue ATP C 501
source : AC3

26) chain C
residue 328
type
sequence I
description binding site for residue ATP C 501
source : AC3

27) chain C
residue 357
type
sequence A
description binding site for residue ATP C 501
source : AC3

28) chain C
residue 360
type
sequence K
description binding site for residue ATP C 501
source : AC3

29) chain D
residue 323
type
sequence R
description binding site for residue ATP C 501
source : AC3

30) chain C
residue 197
type
sequence T
description binding site for residue MG C 502
source : AC4

31) chain D
residue 168
type
sequence G
description binding site for residue ATP D 501
source : AC5

32) chain D
residue 208
type
sequence P
description binding site for residue ATP D 501
source : AC5

33) chain D
residue 209
type
sequence G
description binding site for residue ATP D 501
source : AC5

34) chain D
residue 211
type
sequence G
description binding site for residue ATP D 501
source : AC5

35) chain D
residue 212
type
sequence K
description binding site for residue ATP D 501
source : AC5

36) chain D
residue 213
type
sequence T
description binding site for residue ATP D 501
source : AC5

37) chain D
residue 214
type
sequence M
description binding site for residue ATP D 501
source : AC5

38) chain D
residue 372
type
sequence G
description binding site for residue ATP D 501
source : AC5

39) chain D
residue 373
type
sequence A
description binding site for residue ATP D 501
source : AC5

40) chain D
residue 376
type
sequence N
description binding site for residue ATP D 501
source : AC5

41) chain E
residue 265
type
sequence D
description binding site for residue ATP D 501
source : AC5

42) chain E
residue 291
type
sequence R
description binding site for residue ATP D 501
source : AC5

43) chain E
residue 294
type
sequence R
description binding site for residue ATP D 501
source : AC5

44) chain E
residue 134
type
sequence E
description binding site for residue ATP E 401
source : AC7

45) chain E
residue 135
type
sequence I
description binding site for residue ATP E 401
source : AC7

46) chain E
residue 176
type
sequence P
description binding site for residue ATP E 401
source : AC7

47) chain E
residue 177
type
sequence G
description binding site for residue ATP E 401
source : AC7

48) chain E
residue 178
type
sequence T
description binding site for residue ATP E 401
source : AC7

49) chain E
residue 179
type
sequence G
description binding site for residue ATP E 401
source : AC7

50) chain E
residue 180
type
sequence K
description binding site for residue ATP E 401
source : AC7

51) chain E
residue 181
type
sequence T
description binding site for residue ATP E 401
source : AC7

52) chain E
residue 182
type
sequence L
description binding site for residue ATP E 401
source : AC7

53) chain E
residue 312
type
sequence I
description binding site for residue ATP E 401
source : AC7

54) chain E
residue 316
type
sequence H
description binding site for residue ATP E 401
source : AC7

55) chain E
residue 340
type
sequence G
description binding site for residue ATP E 401
source : AC7

56) chain E
residue 341
type
sequence A
description binding site for residue ATP E 401
source : AC7

57) chain E
residue 344
type
sequence R
description binding site for residue ATP E 401
source : AC7

58) chain F
residue 344
type
sequence R
description binding site for residue ATP E 401
source : AC7

59) chain E
residue 181
type
sequence T
description binding site for residue MG E 402
source : AC8

60) chain E
residue 233
type
sequence D
description binding site for residue MG E 402
source : AC8

61) chain F
residue 187
type
sequence D
description binding site for residue ADP F 501
source : AC9

62) chain F
residue 188
type
sequence I
description binding site for residue ADP F 501
source : AC9

63) chain F
residue 189
type
sequence G
description binding site for residue ADP F 501
source : AC9

64) chain F
residue 230
type
sequence G
description binding site for residue ADP F 501
source : AC9

65) chain F
residue 231
type
sequence T
description binding site for residue ADP F 501
source : AC9

66) chain F
residue 233
type
sequence K
description binding site for residue ADP F 501
source : AC9

67) chain F
residue 234
type
sequence T
description binding site for residue ADP F 501
source : AC9

68) chain F
residue 235
type
sequence L
description binding site for residue ADP F 501
source : AC9

69) chain F
residue 365
type
sequence I
description binding site for residue ADP F 501
source : AC9

70) chain F
residue 369
type
sequence H
description binding site for residue ADP F 501
source : AC9

71) chain F
residue 393
type
sequence G
description binding site for residue ADP F 501
source : AC9

72) chain F
residue 394
type
sequence A
description binding site for residue ADP F 501
source : AC9

73) chain E
residue 174
type BINDING
sequence G
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

74) chain S
residue 134
type BINDING
sequence S
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

75) chain s
residue 34
type BINDING
sequence S
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

76) chain s
residue 40
type BINDING
sequence S
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

77) chain s
residue 134
type BINDING
sequence S
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

78) chain E
residue 72
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

79) chain E
residue 206
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

80) chain M
residue 229
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

81) chain m
residue 56
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

82) chain m
residue 205
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

83) chain m
residue 229
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

84) chain H
residue 76
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

85) chain h
residue 76
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

86) chain u
residue 63
type CROSSLNK
sequence R
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12

87) chain K
residue 198
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

88) chain k
residue 198
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

89) chain h
residue 70
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

90) chain h
residue 171
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

91) chain u
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

92) chain u
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

93) chain u
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

94) chain E
residue 244
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

95) chain s
residue 176
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

96) chain i
residue 127
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

97) chain i
residue 176
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

98) chain h
residue 14
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

99) chain h
residue 16
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

100) chain S
residue 30
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

101) chain S
residue 181
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

102) chain s
residue 30
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

103) chain s
residue 181
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

104) chain l
residue 202
type CARBOHYD
sequence E
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

105) chain H
residue 121
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P17220
source Swiss-Prot : SWS_FT_FI7

106) chain h
residue 121
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P17220
source Swiss-Prot : SWS_FT_FI7

107) chain u
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10

108) chain u
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11

109) chain u
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9

110) chain E
residue 273-291
type prosite
sequence VKMIMATNRPDTLDPALLR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

111) chain C
residue 289-307
type prosite
sequence IKVIMATNRIDILDSALLR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

112) chain D
residue 305-323
type prosite
sequence VKVIMATNRADTLDPALLR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

113) chain F
residue 326-344
type prosite
sequence VKVIAATNRVDILDPALLR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

114) chain A
residue 315-333
type prosite
sequence IKVLMATNRPDTLDPALMR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

115) chain B
residue 325-343
type prosite
sequence VKVIMATNRIETLDPALIR
description AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
source prosite : PS00674

116) chain l
residue 6-28
type prosite
sequence YDNDVTVWSPQGRIHQIEYAMEA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

117) chain k
residue 8-30
type prosite
sequence YDRGVNTFSPEGRLFQVEYAIEA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

118) chain j
residue 3-25
type prosite
sequence YDRAITVFSPDGHLFQVEYAQEA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

119) chain i
residue 5-27
type prosite
sequence YDSRTTIFSPEGRLYQVEYAMEA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

120) chain h
residue 6-28
type prosite
sequence YSFSLTTFSPSGKLVQIEYALAA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

121) chain M
residue 7-29
type prosite
sequence YDLSASTFSPDGRVFQVEYAMKA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

122) chain g
residue 9-31
type prosite
sequence FDRHITIFSPEGRLYQVEYAFKA
description PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
source prosite : PS00388

123) chain R
residue 4-51
type prosite
sequence LAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLG
TMAGGAAD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

124) chain P
residue 12-59
type prosite
sequence MAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYI
GLAGLATD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

125) chain O
residue 4-51
type prosite
sequence AGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYC
CGAGTAAD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

126) chain S
residue 13-60
type prosite
sequence LAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVI
GCSGFHGD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

127) chain N
residue 4-51
type prosite
sequence MAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFC
CRSGSAAD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

128) chain i
residue 35-82
type prosite
sequence LGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMAC
SVAGITSD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

129) chain T
residue 12-59
type prosite
sequence LGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTML
GASGDYAD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854

130) chain Q
residue 5-52
type prosite
sequence IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILL
LCVGEAGD
description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
source prosite : PS00854


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