Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  SHC SH2 domain-binding protein 1  

UniProtKB / Swiss-Prot ID :  SHCBP_HUMAN

Gene Name (Synonyms) : 
SHCBP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc (By similarity). 

Protein Sequence MADGSLTGGGLEAAAMAPERMGWAVEQELASLEKGLFQDEDSCSDCSYRDKPGSSLQSFMPEGKTFFPEI...
Predicted Secondary Structure CCCCCCCCCCCCHHHCCCCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCHHHHHHHHHHHHCCCCCCCHHH...
Protein Variant
LocationDescription
21M -> T (in dbSNP:rs6598679). VAR_051354
60M -> R (in dbSNP:rs11545690). VAR_051355
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
5PhosphoserineMADGSLTGG
CCCCCCCCC
24.25HPRD
Link-
5PhosphoserineMADGSLTGG
CCCCCCCCC
24.25Phosphositeplus
Link-
7PhosphothreonineDGSLTGGGL
CCCCCCCCC
35.16HPRD
Link-
7PhosphothreonineDGSLTGGGL
CCCCCCCCC
35.16Phosphositeplus
Link-
31PhosphoserineQELASLEKG
HHHHHHHHH
50.08HPRD
Link-
31PhosphoserineQELASLEKG
HHHHHHHHH
50.08PhosphoELM
Link-
31PhosphoserineQELASLEKG
HHHHHHHHH
50.08Phosphositeplus
Link-
31PhosphoserineQELASLEKG
HHHHHHHHH
50.08SysPTM
Link-
31Phosphoserine.QELASLEKG
HHHHHHHHH
50.08UniProtKB
Link-
42PhosphoserineQDEDSCSDC
CCCCCCCCC
17.30HPRD
Link-
42PhosphoserineQDEDSCSDC
CCCCCCCCC
17.30PhosphoELM
Link-
42PhosphoserineQDEDSCSDC
CCCCCCCCC
17.30Phosphositeplus
Link-
42PhosphoserineQDEDSCSDC
CCCCCCCCC
17.30SysPTM
Link-
42Phosphoserine.QDEDSCSDC
CCCCCCCCC
17.30UniProtKB
Link-
44PhosphoserineEDSCSDCSY
CCCCCCCCC
45.67HPRD
Link-
44PhosphoserineEDSCSDCSY
CCCCCCCCC
45.67PhosphoELM
Link-
44PhosphoserineEDSCSDCSY
CCCCCCCCC
45.67Phosphositeplus
Link-
44PhosphoserineEDSCSDCSY
CCCCCCCCC
45.67SysPTM
Link-
44Phosphoserine.EDSCSDCSY
CCCCCCCCC
45.67UniProtKB
Link-
47PhosphoserineCSDCSYRDK
CCCCCCHHH
28.35HPRD
Link-
47PhosphoserineCSDCSYRDK
CCCCCCHHH
28.35PhosphoELM
Link-
47PhosphoserineCSDCSYRDK
CCCCCCHHH
28.35Phosphositeplus
Link-
47PhosphoserineCSDCSYRDK
CCCCCCHHH
28.35SysPTM
Link-
47Phosphoserine.CSDCSYRDK
CCCCCCHHH
28.35UniProtKB
Link-
48PhosphotyrosineSDCSYRDKP
CCCCCHHHH
29.21HPRD
Link-
48PhosphotyrosineSDCSYRDKP
CCCCCHHHH
29.21PhosphoELM
Link-
48PhosphotyrosineSDCSYRDKP
CCCCCHHHH
29.21Phosphositeplus
Link-
51Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SYRDKPGSS
CCHHHHHHH
42.13Phosphositeplus
Link-
54PhosphoserineDKPGSSLQS
HHHHHHHHH
36.08HPRD
Link-
54PhosphoserineDKPGSSLQS
HHHHHHHHH
36.08PhosphoELM
Link-
55PhosphoserineKPGSSLQSF
HHHHHHHHH
36.02HPRD
Link-
55PhosphoserineKPGSSLQSF
HHHHHHHHH
36.02PhosphoELM
Link-
55PhosphoserineKPGSSLQSF
HHHHHHHHH
36.02Phosphositeplus
Link-
96PhosphoserineDCKASEVQE
CCCHHHHHH
24.64HPRD
Link-
96PhosphoserineDCKASEVQE
CCCHHHHHH
24.64Phosphositeplus
Link-
139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FAALKAVVR
CCCEEEEEE
34.11Phosphositeplus
Link-
217PhosphotyrosineEEDEYDYFV
CCHHHHHHH
28.41Phosphositeplus
Link-
219PhosphotyrosineDEYDYFVRC
HHHHHHHHH
11.76Phosphositeplus
Link-
269PhosphoserineRSSLSNCNS
HHHCCCCCC
41.08HPRD
Link-
269PhosphoserineRSSLSNCNS
HHHCCCCCC
41.08PhosphoELM
Link-
273PhosphoserineSNCNSDSEQ
CCCCCHHHH
44.72HPRD
Link-
273PhosphoserineSNCNSDSEQ
CCCCCHHHH
44.72PhosphoELM
Link-
273PhosphoserineSNCNSDSEQ
CCCCCHHHH
44.72Phosphositeplus
Link-
273PhosphoserineSNCNSDSEQ
CCCCCHHHH
44.72SysPTM
Link-
273Phosphoserine.SNCNSDSEQ
CCCCCHHHH
44.72UniProtKB
Link-
275PhosphoserineCNSDSEQEN
CCCHHHHHH
40.79PhosphoELM
Link-
275PhosphoserineCNSDSEQEN
CCCHHHHHH
40.79Phosphositeplus
Link-
296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MEQLKQKLK
HHHHHHHHH
45.11Phosphositeplus
Link-
300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KQKLKLIEN
HHHHHHHHC
55.22Phosphositeplus
Link-
315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FGYQKNSNI
CCCCCCCCC
54.59Phosphositeplus
Link-
406PhosphotyrosineELEGYGLPD
EEEEECCCC
13.20PhosphoELM
Link-
419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKRGKGDTF
EECCCCCCE
58.61Phosphositeplus
Link-
474PhosphoserineTVRTSAEFL
EEEECCEEE
18.42Phosphositeplus
Link-
474PhosphoserineTVRTSAEFL
EEEECCEEE
18.42SysPTM
Link-
573PhosphothreonineLKIQTSGEP
HHHHCCCCC
42.02HPRD
Link-
573PhosphothreonineLKIQTSGEP
HHHHCCCCC
42.02PhosphoELM
Link-
634PhosphoserineKKRLSELGI
HHHHHHCCC
34.50HPRD
Link-
634PhosphoserineKKRLSELGI
HHHHHHCCC
34.50PhosphoELM
Link-
634PhosphoserineKKRLSELGI
HHHHHHCCC
34.50Phosphositeplus
Link-
634PhosphoserineKKRLSELGI
HHHHHHCCC
34.50SysPTM
Link-
634Phosphoserine.KKRLSELGI
HHHHHHCCC
34.50UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433G_HUMANphysical interactionMINT-50847MINT15324660
CF113_HUMANphysical interactionEBI-754144
intact16189514
CF113_HUMANyeast 2-hybridHPRD:11557HPRD16189514
SHC1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:11557HPRD10086341
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-42; SER-44;SER-47; SER-273 AND SER-634, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-273, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures