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6I2I

Refined 13pf Hela Cell Tubulin microtubule (EML4-NTD decorated)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003725molecular_functiondouble-stranded RNA binding
A0003924molecular_functionGTPase activity
A0005198molecular_functionstructural molecule activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0030705biological_processcytoskeleton-dependent intracellular transport
A0031625molecular_functionubiquitin protein ligase binding
A0051301biological_processcell division
A0071353biological_processcellular response to interleukin-4
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005198molecular_functionstructural molecule activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005641cellular_componentnuclear envelope lumen
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0019904molecular_functionprotein domain specific binding
B0030705biological_processcytoskeleton-dependent intracellular transport
B0031625molecular_functionubiquitin protein ligase binding
B0032794molecular_functionGTPase activating protein binding
B0032991cellular_componentprotein-containing complex
B0035578cellular_componentazurophil granule lumen
B0036464cellular_componentcytoplasmic ribonucleoprotein granule
B0042267biological_processnatural killer cell mediated cytotoxicity
B0042288molecular_functionMHC class I protein binding
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0045171cellular_componentintercellular bridge
B0046872molecular_functionmetal ion binding
B0050807biological_processregulation of synapse organization
B0051225biological_processspindle assembly
B0051301biological_processcell division
B0070062cellular_componentextracellular exosome
B0071895biological_processodontoblast differentiation
B0072686cellular_componentmitotic spindle
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
ATHR145
AGLY146
ATHR179
AGLU183
AASN206
ATYR224
ALEU227
AASN228
AMG502
AGLN11
AALA12
AGLN15
AASP98
AALA100
AASN101
AGLY143
AGLY144

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 502
ChainResidue
ATHR145
AGTP501

site_idAC3
Number of Residues16
Detailsbinding site for residue G2P B 501
ChainResidue
AGLU254
BGLY10
BGLN11
BCYS12
BGLN15
BALA99
BASN101
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BASN206
BTYR224
BASN228
BMG502

site_idAC4
Number of Residues1
Detailsbinding site for residue MG B 502
ChainResidue
BG2P501

site_idAC5
Number of Residues15
Detailsbinding site for residue TA1 B 503
ChainResidue
BVAL23
BASP26
BGLU27
BHIS229
BLEU230
BALA233
BSER236
BPRO274
BLEU275
BTHR276
BGLN281
BPRO360
BARG369
BGLY370
BLEU371

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLN11
BSER140
BGLY144
BTHR145
BGLY146
BASN206
BASN228

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU71
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER40

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR57
BTHR287
BTHR292

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS60
ASER232

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:16371510
ChainResidueDetails
BSER174

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000269|Ref.9
ChainResidueDetails
BARG320

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000269|PubMed:28576883
ChainResidueDetails
BGLU444
BGLU451

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000269|PubMed:32747782
ChainResidueDetails
BGLU448
BGLU449

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: 5-glutamyl glycine => ECO:0000269|PubMed:28576883
ChainResidueDetails
BGLU452
BGLU453

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
BLYS60

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
ALYS326
BLYS326
ALYS370

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PDB entries from 2024-07-17

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