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1FBV

STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES

Functional Information from GO Data
ChainGOidnamespacecontents
A0001784molecular_functionphosphotyrosine residue binding
A0004842molecular_functionubiquitin-protein transferase activity
A0005509molecular_functioncalcium ion binding
A0007166biological_processcell surface receptor signaling pathway
A0023051biological_processregulation of signaling
A0046872molecular_functionmetal ion binding
C0000151cellular_componentubiquitin ligase complex
C0000166molecular_functionnucleotide binding
C0000209biological_processprotein polyubiquitination
C0003713molecular_functiontranscription coactivator activity
C0003723molecular_functionRNA binding
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006355biological_processregulation of DNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0008283biological_processcell population proliferation
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019787molecular_functionubiquitin-like protein transferase activity
C0019899molecular_functionenzyme binding
C0031398biological_processpositive regulation of protein ubiquitination
C0031625molecular_functionubiquitin protein ligase binding
C0032446biological_processprotein modification by small protein conjugation
C0036211biological_processprotein modification process
C0044770biological_processcell cycle phase transition
C0045893biological_processpositive regulation of DNA-templated transcription
C0051443biological_processpositive regulation of ubiquitin-protein transferase activity
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070979biological_processprotein K11-linked ubiquitination
C0071383biological_processcellular response to steroid hormone stimulus
C0071385biological_processcellular response to glucocorticoid stimulus
C0097027molecular_functionubiquitin-protein transferase activator activity
C0098793cellular_componentpresynapse
C1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS381
ACYS384
ACYS401
ACYS404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
ACYS396
AHIS398
ACYS416
ACYS419

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
AARG68
ALYS65

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AHIS213
ASER253
ALEU254
ALEU255
AARG256
AHIS360

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
AARG180
ALYS183
AARG246
AGLN249

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
AGLN146
AARG149
ALYS153
AMET374

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
ALYS382
CLYS1009
CLYS1100

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNIdek.GqVCLpvI
ChainResidueDetails
CTYR1075-ILE1090

site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL
ChainResidueDetails
ACYS396-LEU405

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15144186
ChainResidueDetails
BSER4

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
ChainResidueDetails
BPTR7
ATHR231
AASN233
ATYR235
AGLU240

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG294

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497
ChainResidueDetails
ATYR371

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 438
ChainResidueDetails
CCYS1086nucleofuge

218853

PDB entries from 2024-04-24

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