CPLM-006515

Genbank Nucleotide ID

Protein Synonyms/Alias

5F7; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; Leukocyte activation antigen M6; OK blood group antigen; Tumor cell-derived collagenase stimulatory factor; TCSF; CD147

Homo sapiens (Human)

Position	Peptide	Type	References
173	VTGHRWLKGGVVLKE	ubiquitination	[1, 2, 3, 4, 5, 6]
179	LKGGVVLKEDALPGQ	ubiquitination	[1, 2, 3, 4, 5, 6]
187	EDALPGQKTEFKVDS	ubiquitination	[2, 5]
227	PPRVKAVKSSEHINE	ubiquitination	[2, 5]
243	ETAMLVCKSESVPPV	ubiquitination	[5]
257	VTDWAWYKITDSEDK	ubiquitination	[1, 2, 5, 6]
264	KITDSEDKALMNGSE	ubiquitination	[2, 4, 5]
307	RCNGTSSKGSDQAII	ubiquitination	[3, 4, 5, 7]
350	FIYEKRRKPEDVLDD	ubiquitination	[2, 7, 8, 9]
366	DAGSAPLKSSGQHQN	ubiquitination	[2, 7, 8, 10]
375	SGQHQNDKGKNVRQR	ubiquitination	[2]

[1] 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]
[2] 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]
[3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[5] 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]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[7] 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]
[8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[9] 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]
[10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]

Functional Description

Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). May target monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to plasma membranes of retinal pigment epithelium and neural retina. Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes (By similarity).

DOMAIN 138 219 Ig-like C2-type.
DOMAIN 221 315 Ig-like V-type.
MOD_RES 362 362 Phosphoserine.
CARBOHYD 160 160 N-linked (GlcNAc...).
CARBOHYD 268 268 N-linked (GlcNAc...).
CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
DISULFID 157 203
DISULFID 242 301

3D-structure; Alternative promoter usage; Alternative splicing; Blood group antigen; Cell membrane; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Immunoglobulin domain; Lectin; Mannose-binding; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0002080; C:acrosomal membrane; IEA:Compara.
GO:0000139; C:Golgi membrane; TAS:Reactome.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO:0045121; C:membrane raft; IEA:Compara.
GO:0005739; C:mitochondrion; IEA:Compara.
GO:0005886; C:plasma membrane; TAS:Reactome.
GO:0042383; C:sarcolemma; IEA:Compara.
GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
GO:0007596; P:blood coagulation; TAS:Reactome.
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO:0046697; P:decidualization; IEA:Compara.
GO:0007566; P:embryo implantation; IEA:Compara.
GO:0050900; P:leukocyte migration; TAS:Reactome.
GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO:0051591; P:response to cAMP; IEA:Compara.
GO:0046689; P:response to mercury ion; IEA:Compara.
GO:0043434; P:response to peptide hormone stimulus; IEA:Compara.

IPR009151; Basigin.
IPR007110; Ig-like_dom.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.

SM00409; IG
SM00408; IGc2