CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022468
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cysteine-rich motor neuron 1 protein 
Protein Synonyms/Alias
 CRIM-1; Cysteine-rich repeat-containing protein S52; Processed cysteine-rich motor neuron 1 protein 
Gene Name
 CRIM1 
Gene Synonyms/Alias
 S52; UNQ1886/PRO4330 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
978CWYRTPTKPSSLNNQubiquitination[1, 2, 3, 4]
992QLVSVDCKKGTRVQVubiquitination[2]
1023SGFYSMQKQNHLQADubiquitination[2, 5, 6]
Reference
 [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] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface. 
Sequence Annotation
 DOMAIN 35 112 IGFBP N-terminal.
 DOMAIN 334 391 VWFC 1.
 DOMAIN 401 457 VWFC 2.
 DOMAIN 469 498 Antistasin-like 1.
 DOMAIN 505 532 Antistasin-like 2.
 DOMAIN 539 564 Antistasin-like 3.
 DOMAIN 567 592 Antistasin-like 4.
 DOMAIN 606 663 VWFC 3.
 DOMAIN 677 735 VWFC 4.
 DOMAIN 751 809 VWFC 5.
 DOMAIN 817 874 VWFC 6.
 MOTIF 314 316 Cell attachment site (Potential).
 MOD_RES 1035 1035 Phosphothreonine.
 CARBOHYD 71 71 N-linked (GlcNAc...) (Potential).
 CARBOHYD 113 113 N-linked (GlcNAc...) (Potential).
 CARBOHYD 330 330 N-linked (GlcNAc...) (Potential).
 CARBOHYD 474 474 N-linked (GlcNAc...) (Potential).
 CARBOHYD 746 746 N-linked (GlcNAc...) (Potential).  
Keyword
 Cell membrane; Complete proteome; Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1036 AA 
Protein Sequence
MYLVAGDRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN CPGSIVQGVC 60
GCCYTCASQR NESCGGTFGI YGTCDRGLRC VIRPPLNGDS LTEYEAGVCE DENWTDDQLL 120
GFKPCNENLI AGCNIINGKC ECNTIRTCSN PFEFPSQDMC LSALKRIEEE KPDCSKARCE 180
VQFSPRCPED SVLIEGYAPP GECCPLPSRC VCNPAGCLRK VCQPGNLNIL VSKASGKPGE 240
CCDLYECKPV FGVDCRTVEC PPVQQTACPP DSYETQVRLT ADGCCTLPTR CECLSGLCGF 300
PVCEVGSTPR IVSRGDGTPG KCCDVFECVN DTKPACVFNN VEYYDGDMFR MDNCRFCRCQ 360
GGVAICFTAQ CGEINCERYY VPEGECCPVC EDPVYPFNNP AGCYANGLIL AHGDRWREDD 420
CTFCQCVNGE RHCVATVCGQ TCTNPVKVPG ECCPVCEEPT IITVDPPACG ELSNCTLTGK 480
DCINGFKRDH NGCRTCQCIN TEELCSERKQ GCTLNCPFGF LTDAQNCEIC ECRPRPKKCR 540
PIICDKYCPL GLLKNKHGCD ICRCKKCPEL SCSKICPLGF QQDSHGCLIC KCREASASAG 600
PPILSGTCLT VDGHHHKNEE SWHDGCRECY CLNGREMCAL ITCPVPACGN PTIHPGQCCP 660
SCADDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVLC ETEVCPPLLC 720
QNPSRTQDSC CPQCTDQPFR PSLSRNNSVP NYCKNDEGDI FLAAESWKPD VCTSCICIDS 780
VISCFSESCP SVSCERPVLR KGQCCPYCIE DTIPKKVVCH FSGKAYADEE RWDLDSCTHC 840
YCLQGQTLCS TVSCPPLPCV EPINVEGSCC PMCPEMYVPE PTNIPIEKTN HRGEVDLEVP 900
LWPTPSENDI VHLPRDMGHL QVDYRDNRLH PSEDSSLDSI ASVVVPIIIC LSIIIAFLFI 960
NQKKQWIPLL CWYRTPTKPS SLNNQLVSVD CKKGTRVQVD SSQRMLRIAE PDARFSGFYS 1020
MQKQNHLQAD NFYQTV 1036 
Gene Ontology
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; TAS:ProtInc.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005010; F:insulin-like growth factor-activated receptor activity; TAS:ProtInc.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
 GO:0043086; P:negative regulation of catalytic activity; IEA:GOC.
 GO:0007399; P:nervous system development; TAS:ProtInc.
 GO:0001558; P:regulation of cell growth; IEA:InterPro. 
Interpro
 IPR000867; IGFBP-like.
 IPR011061; Prot_inh_I14/15_hirudin/antisn.
 IPR018112; Prot_inh_I15_antistasin.
 IPR004094; Prot_inh_I15_antistasin-like.
 IPR001007; VWF_C. 
Pfam
 PF02822; Antistasin
 PF00093; VWC 
SMART
 SM00121; IB
 SM00214; VWC 
PROSITE
 PS51252; ANTISTASIN
 PS51323; IGFBP_N_2
 PS01208; VWFC_1
 PS50184; VWFC_2 
PRINTS