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Protein Page:
CIN85 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CIN85 Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit. May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Can self-associate and form homotetramers. Interacts with CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, MAGI2, CRK, BCAR1, SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with CBL and CBLB, but does not interact with CBLC. Two molecules of SH3KBP1 seem to bind through their respective SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is increased upon EGF stimulation. The interaction with CBL is attenuated by PDCD6IP. Interacts through its proline-rich region with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex seems to associate with a complex containing the phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably associates with ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion kinases PTK2 AND PTK2B, probably as a dimer. Interacts with DAB2 and probably associates with chathrin through its interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1 following growth factor treatment, enabling interaction with CBL. Interacts with DDN and probably associates with MAGI2 through its interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-associated complex upon stimulation with TNF-alpha seems to be mediated by SRC. Probably interacts with SH3KBP1. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Apoptosis; Adaptor/scaffold
Cellular Component: neuron projection; cytoplasmic vesicle membrane; focal adhesion; cytoskeleton; plasma membrane; synapse; cytosol
Molecular Function: protein binding; SH3 domain binding
Biological Process: negative regulation of epidermal growth factor receptor signaling pathway; epidermal growth factor receptor signaling pathway; regulation of cell shape; cell migration; cell-cell signaling; apoptosis; endocytosis; cytoskeleton organization and biogenesis
Reference #:  Q96B97 (UniProtKB)
Alt. Names/Synonyms: c-Cbl-interacting protein; Cbl-interacting protein of 85 kDa; CD2-binding protein 3; CD2BP3; GIG10; HSB-1; Human Src family kinase-binding protein 1; MIG18; migration-inducing gene 18 protein; SH3 domain-containing kinase-binding protein 1; SH3-domain kinase binding protein 1; SH3K1; SH3KBP1
Gene Symbols: SH3KBP1
Molecular weight: 73,126 Da
Basal Isoelectric point: 6.24  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CIN85

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S587‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 - gap
0 2 S79-p KPLHEVPsGNsLLSS
0 2 S82-p HEVPsGNsLLSSETI
0 17 S108-p RRCQVAFsyLPQNDD
0 2 Y109-p RCQVAFsyLPQNDDE
0 8 S156-p SNFIKELsGESDELG
0 3 S159 IKELsGESDELGIsQ
0 2 S165-p ESDELGIsQDEQLSK
0 3 T179-p KSSLRETtGsEsDGG
0 3 S181-p SLRETtGsEsDGGDS
0 3 S183-p RETtGsEsDGGDSSS
0 35 S230-p PIKLRPRsIEVENDF
0 4 T254-p KLPATTAtPDSSKTE
0 4 S410-p PRPPKTNsLSRPGAL
0 8 S436-p LTHTRGDsPKIDLAG
0 1 S468 IDLEGFDSVVSSTEK
0 1 S472 GFDSVVSSTEKLSHP
0 2 S498-p PPSQSLTsSSLssPD
0 1 S502-p SLTsSSLssPDIFds
0 2 S503-p LTsSSLssPDIFdsP
0 1 D508-ca LssPDIFdsPsPEED
0 8 S509-p ssPDIFdsPsPEEDK
0 9 S511-p PDIFdsPsPEEDKEE
0 3 S521-p EDKEEHIsLAHRGVD
0 2 K535-a DASKKTSktVtIsQV
0 2 T536-p ASKKTSktVtIsQVS
0 2 T538-p KKTSktVtIsQVSDN
0 3 S540-p TSktVtIsQVSDNKA
0 1 S572-p PLSSAAPsPLSSSLG
0 1 T580-p PLSSSLGtAGHRANs
0 1 N586 GtAGHRANsPsLFGT
1 27 S587-p tAGHRANsPsLFGTE
0 5 S589-p GHRANsPsLFGTEGK
1 0 K598-s FGTEGKPkMEPAASS
  mouse

► Hide Isoforms
 
- gap
S79 KPMHDVSSGNALLSS
A82 HDVSSGNALLSSETI
S108-p RRCQVAFsyLPQNDD
Y109-p RCQVAFsyLPQNDDE
S156-p SNFIKELsGEsDELG
S159-p IKELsGEsDELGISQ
S165 EsDELGISQDEQLSK
T223-p YYSLRETtGsEsDGG
S225-p SLRETtGsEsDGGDS
S227-p RETtGsEsDGGDSSS
S274-p PIKLRPRsIEVENDF
T298 KLPPATSTPDPSKTE
S454-p PRPPKTNsLNRPGAL
S480-p LTHTRGDsPKIDLAG
S512-p IDLEGFDsVISsTEK
S516-p GFDsVISsTEKLSHP
S542 PPSQSLTSSSLSsPD
S546 SLTSSSLSsPDIFDs
S547-p LTSSSLSsPDIFDsP
D552 LSsPDIFDsPsPEED
S553-p SsPDIFDsPsPEEDK
S555-p PDIFDsPsPEEDKEE
S565-p EDKEEHIsLAHRGID
K579-a DVSKKTSkTVTISQV
T580 VSKKTSkTVTISQVS
T582 KKTSkTVTISQVSDN
S584 TSkTVTISQVSDNKT
S616 SLSSVASSPMSSSLG
T624 PMSSSLGTAGQRAss
S630-p GTAGQRAssPsLFST
S631-p TAGQRAssPsLFSTE
S633-p GQRAssPsLFSTEGK
K642 FSTEGKPKMEPAVSS
  CIN85 iso3  
S10-p LSAAKAPsPTDLPES
S42 KPMHDVSSGNALLSS
A45 HDVSSGNALLSSETI
S71 RRCQVAFSYLPQNDD
Y72 RCQVAFSYLPQNDDE
S119 SNFIKELSGESDELG
S122 IKELSGESDELGISQ
S128 ESDELGISQDEQLSK
T142 KSSLRETTGsESDGG
S144-p SLRETTGsESDGGDS
S146 RETTGsESDGGDSSS
S193 PIKLRPRSIEVENDF
T217 KLPPATSTPDPSKTE
S373 PRPPKTNSLNRPGAL
S399 LTHTRGDSPKIDLAG
S431 IDLEGFDSVISSTEK
S435 GFDSVISSTEKLSHP
S461 PPSQSLTSSSLSSPD
S465 SLTSSSLSSPDIFDS
S466 LTSSSLSSPDIFDSP
D471 LSSPDIFDSPSPEED
S472 SSPDIFDSPSPEEDK
S474 PDIFDSPSPEEDKEE
S484 EDKEEHISLAHRGID
K498 DVSKKTSKTVTISQV
T499 VSKKTSKTVTISQVS
T501 KKTSKTVTISQVSDN
S503 TSKTVTISQVSDNKT
S535 SLSSVASSPMSSSLG
T543 PMSSSLGTAGQRASS
S549 GTAGQRASSPSLFST
S550 TAGQRASSPSLFSTE
S552 GQRASSPSLFSTEGK
K561 FSTEGKPKMEPAVSS
  rat

► Hide Isoforms
 
- gap
S79 KPMHDVSSGNSLLSS
S82 HDVSSGNSLLSSETI
S108 RRCQVAFSYLPQNDD
Y109 RCQVAFSYLPQNDDE
S156 SNFIKELSGESDELG
S159 IKELSGESDELGIsQ
S165-p ESDELGIsQDEQLSK
T223 YYSLRETTGSESDGG
S225 SLRETTGSESDGGDS
S227 RETTGSESDGGDSSS
S274-p PIKLRPRsIEVENDF
T298 KLPPATSTPDPSKTE
S454 PRPPKTNSLNRPGVL
S480-p LTHTRGDsSKIDLAG
S512 IDLEGFDSVISSTEK
S516 GFDSVISSTEKLSHP
S542 PPSQSLTSSSLSSPD
S546 SLTSSSLSSPDIFDS
S547 LTSSSLSSPDIFDSP
D552 LSSPDIFDSPSPEED
S553 SSPDIFDSPSPEEDK
S555 PDIFDSPSPEEDKEE
S565 EDKEEHISLAHRGID
R579 DVSKKTSRTVTISQV
T580 VSKKTSRTVTISQVS
T582 KKTSRTVTISQVSDN
S584 TSRTVTISQVSDNKA
S616 SLSSVASSPMSSSLG
T624 PMSSSLGTAGQRASs
S630 GTAGQRASsPSLFSA
S631-p TAGQRASsPSLFSAE
S633 GQRASsPSLFSAEGK
K642 FSAEGKAKTESAVSS
  CIN85 iso2  
- gap
S79 KPMHDVSSGNSLLSS
S82 HDVSSGNSLLSSETI
S108 RRCQVAFSYLPQNDD
Y109 RCQVAFSYLPQNDDE
S156 SNFIKELSGESDELG
S159 IKELSGESDELGISQ
S165 ESDELGISQDEQLSK
T179 KSSLRETTGSESDGG
S181 SLRETTGSESDGGDS
S183 RETTGSESDGGDSSS
S230 PIKLRPRSIEVENDF
T254 KLPPATSTPDPSKTE
S410 PRPPKTNSLNRPGVL
S436 LTHTRGDSSKIDLAG
S468 IDLEGFDSVISSTEK
S472 GFDSVISSTEKLSHP
S498 PPSQSLTSSSLSSPD
S502 SLTSSSLSSPDIFDS
S503 LTSSSLSSPDIFDSP
D508 LSSPDIFDSPSPEED
S509 SSPDIFDSPSPEEDK
S511 PDIFDSPSPEEDKEE
S521 EDKEEHISLAHRGID
R535 DVSKKTSRTVTISQV
T536 VSKKTSRTVTISQVS
T538 KKTSRTVTISQVSDN
S540 TSRTVTISQVSDNKA
S572 SLSSVASSPMSSSLG
T580 PMSSSLGTAGQRASS
S586 GTAGQRASSPSLFSA
S587 TAGQRASSPSLFSAE
S589 GQRASSPSLFSAEGK
K598 FSAEGKAKTESAVSS
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