CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017673
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SHC SH2 domain-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
 SHCBP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51SDCSYRDKPGSSLQSubiquitination[1, 2]
94DYILADCKASEVQEFubiquitination[3]
139DVDFAALKAVVRLAEubiquitination[1]
296YSEMEQLKQKLKLIEubiquitination[1, 2, 3]
300EQLKQKLKLIENPLLubiquitination[1, 2, 3, 4]
315RYVFGYQKNSNIQAKubiquitination[1, 2, 5]
419IVIEKRGKGDTFVDCubiquitination[1, 2, 4]
454ILIVHRGKTTLENCVubiquitination[2]
480TSAEFLMKNSDLYGAubiquitination[2]
488NSDLYGAKGAGIEIYubiquitination[2]
517CKEGILIKDFLDEHYubiquitination[2]
664NQFKWNGKGSFGTFLubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 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. Acts as a positive regulator of FGF signaling in neural progenitor cells (By similarity). 
Sequence Annotation
 REPEAT 428 451 PbH1 1.
 REPEAT 452 473 PbH1 2.
 REPEAT 474 496 PbH1 3.
 REPEAT 497 518 PbH1 4.
 REPEAT 526 548 PbH1 5.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 7 7 Phosphothreonine.
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 42 42 Phosphoserine.
 MOD_RES 44 44 Phosphoserine.
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 273 273 Phosphoserine.
 MOD_RES 634 634 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 672 AA 
Protein Sequence
MADGSLTGGG LEAAAMAPER MGWAVEQELA SLEKGLFQDE DSCSDCSYRD KPGSSLQSFM 60
PEGKTFFPEI FQTNQLLFYE RFRAYQDYIL ADCKASEVQE FTAEFLEKVL EPSGWRAVWH 120
TNVFKVLVEI TDVDFAALKA VVRLAEPYLC DSQVSTFTME CMKELLDLKE HRLPLQELWV 180
VFDDSGVFDQ TALAIEHVRF FYQNIWRSWD EEEEDEYDYF VRCVEPRLRL HYDILEDRVP 240
SGLIVDYHNL LSQCEESYRK FLNLRSSLSN CNSDSEQENI SMVEGLKLYS EMEQLKQKLK 300
LIENPLLRYV FGYQKNSNIQ AKGVRSSGQK ITHVVSSTMM AGLLRSLLTD RLCQEPGEEE 360
REIQFHSDPL SAINACFEGD TVIVCPGHYV VHGTFSIADS IELEGYGLPD DIVIEKRGKG 420
DTFVDCTGAD IKISGIKFVQ HDAVEGILIV HRGKTTLENC VLQCETTGVT VRTSAEFLMK 480
NSDLYGAKGA GIEIYPGSQC TLSDNGIHHC KEGILIKDFL DEHYDIPKIS MVNNIIHNNE 540
GYGVVLVKPT IFSDLQENAE DGTEENKALK IQTSGEPDVA ERVDLEELIE CATGKMELCA 600
RTDPSEQVEG NCEIVNELIA ASTQKGQIKK KRLSELGITQ ADDNLMSQEM FVGIVGNQFK 660
WNGKGSFGTF LF 672 
Gene Ontology
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
 GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB. 
Interpro
 IPR006626; PbH1.
 IPR012334; Pectin_lyas_fold.
 IPR011050; Pectin_lyase_fold/virulence. 
Pfam
  
SMART
 SM00710; PbH1 
PROSITE
  
PRINTS