CRIM1_HUMAN - dbPTM
CRIM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRIM1_HUMAN
UniProt AC Q9NZV1
Protein Name Cysteine-rich motor neuron 1 protein
Gene Name CRIM1
Organism Homo sapiens (Human).
Sequence Length 1036
Subcellular Localization Processed cysteine-rich motor neuron 1 protein: Secreted.
Cell membrane
Single-pass type I membrane protein .
Protein 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..
Protein Sequence MYLVAGDRGLAGCGHLLVSLLGLLLLLARSGTRALVCLPCDESKCEEPRNCPGSIVQGVCGCCYTCASQRNESCGGTFGIYGTCDRGLRCVIRPPLNGDSLTEYEAGVCEDENWTDDQLLGFKPCNENLIAGCNIINGKCECNTIRTCSNPFEFPSQDMCLSALKRIEEEKPDCSKARCEVQFSPRCPEDSVLIEGYAPPGECCPLPSRCVCNPAGCLRKVCQPGNLNILVSKASGKPGECCDLYECKPVFGVDCRTVECPPVQQTACPPDSYETQVRLTADGCCTLPTRCECLSGLCGFPVCEVGSTPRIVSRGDGTPGKCCDVFECVNDTKPACVFNNVEYYDGDMFRMDNCRFCRCQGGVAICFTAQCGEINCERYYVPEGECCPVCEDPVYPFNNPAGCYANGLILAHGDRWREDDCTFCQCVNGERHCVATVCGQTCTNPVKVPGECCPVCEEPTIITVDPPACGELSNCTLTGKDCINGFKRDHNGCRTCQCINTEELCSERKQGCTLNCPFGFLTDAQNCEICECRPRPKKCRPIICDKYCPLGLLKNKHGCDICRCKKCPELSCSKICPLGFQQDSHGCLICKCREASASAGPPILSGTCLTVDGHHHKNEESWHDGCRECYCLNGREMCALITCPVPACGNPTIHPGQCCPSCADDFVVQKPELSTPSICHAPGGEYFVEGETWNIDSCTQCTCHSGRVLCETEVCPPLLCQNPSRTQDSCCPQCTDQPFRPSLSRNNSVPNYCKNDEGDIFLAAESWKPDVCTSCICIDSVISCFSESCPSVSCERPVLRKGQCCPYCIEDTIPKKVVCHFSGKAYADEERWDLDSCTHCYCLQGQTLCSTVSCPPLPCVEPINVEGSCCPMCPEMYVPEPTNIPIEKTNHRGEVDLEVPLWPTPSENDIVHLPRDMGHLQVDYRDNRLHPSEDSSLDSIASVVVPIIICLSIIIAFLFINQKKQWIPLLCWYRTPTKPSSLNNQLVSVDCKKGTRVQVDSSQRMLRIAEPDARFSGFYSMQKQNHLQADNFYQTV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
44UbiquitinationCLPCDESKCEEPRNC
EEECCHHHCCCCCCC		43.5533845483
54PhosphorylationEPRNCPGSIVQGVCG
CCCCCCCHHHCCCHH		12.53-
65PhosphorylationGVCGCCYTCASQRNE
CCHHHHHHHHHHCCC		6.4122468782
68PhosphorylationGCCYTCASQRNESCG
HHHHHHHHHCCCCCC		31.6422468782
71N-linked_GlycosylationYTCASQRNESCGGTF
HHHHHHCCCCCCCEE		37.59UniProtKB CARBOHYD
113N-linked_GlycosylationAGVCEDENWTDDQLL
ECCCCCCCCCCCCCC		60.31UniProtKB CARBOHYD
176UbiquitinationEEKPDCSKARCEVQF
HHCCCCCCCEEEEEE		46.3029967540
237UbiquitinationLVSKASGKPGECCDL
EEECCCCCCCCCCCC		47.5633845483
321UbiquitinationRGDGTPGKCCDVFEC
CCCCCCCCCCCEEEE		32.6633845483
330N-linked_GlycosylationCDVFECVNDTKPACV
CCEEEECCCCCCEEE		63.99UniProtKB CARBOHYD
474N-linked_GlycosylationPACGELSNCTLTGKD
CCCCCHHCCEECCCH		35.10UniProtKB CARBOHYD
596O-linked_GlycosylationICKCREASASAGPPI
EEECCHHHCCCCCCE		20.2950576185
596PhosphorylationICKCREASASAGPPI
EEECCHHHCCCCCCE		20.29-
598PhosphorylationKCREASASAGPPILS
ECCHHHCCCCCCEEE		31.12-
598O-linked_GlycosylationKCREASASAGPPILS
ECCHHHCCCCCCEEE		31.1250576191
630PhosphorylationHDGCRECYCLNGREM
CCCCCEEEEECCCEE		8.6725159151
656UbiquitinationGNPTIHPGQCCPSCA
CCCCCCCCCCCCCCC		20.9921890473
670UbiquitinationADDFVVQKPELSTPS
CCCEEEECCCCCCCC		28.9321963094
671UbiquitinationDDFVVQKPELSTPSI
CCEEEECCCCCCCCE		30.5722817900
701UbiquitinationNIDSCTQCTCHSGRV
EECCCCEEEECCCCE		2.0621963094
746N-linked_GlycosylationFRPSLSRNNSVPNYC
CCCCCCCCCCCCCCC		41.58UniProtKB CARBOHYD
807PhosphorylationRKGQCCPYCIEDTIP
CCCCCCCCEECCCCC		7.67-
816UbiquitinationIEDTIPKKVVCHFSG
ECCCCCCEEEEECCC		34.2529967540
826PhosphorylationCHFSGKAYADEERWD
EECCCCCCCCCCCCC		20.33-
897UbiquitinationNHRGEVDLEVPLWPT
CCCCCEEEECCCCCC		9.6221890473
904O-linked_GlycosylationLEVPLWPTPSENDIV
EECCCCCCCCCCCEE		28.06OGP
911UbiquitinationTPSENDIVHLPRDMG
CCCCCCEEECCCCCC		4.1821963094
912UbiquitinationPSENDIVHLPRDMGH
CCCCCEEECCCCCCC		30.3722817900
913UbiquitinationSENDIVHLPRDMGHL
CCCCEEECCCCCCCE		2.2921890473
920UbiquitinationLPRDMGHLQVDYRDN
CCCCCCCEEEECCCC		4.3821890473
927UbiquitinationLQVDYRDNRLHPSED
EEEECCCCCCCCCCC		39.1421963094
928UbiquitinationQVDYRDNRLHPSEDS
EEECCCCCCCCCCCC		38.3722817900
934UbiquitinationNRLHPSEDSSLDSIA
CCCCCCCCCCHHHHH		48.1121963094
935UbiquitinationRLHPSEDSSLDSIAS
CCCCCCCCCHHHHHH		28.8422817900
938UbiquitinationPSEDSSLDSIASVVV
CCCCCCHHHHHHHHH		39.6921890473
942UbiquitinationSSLDSIASVVVPIII
CCHHHHHHHHHHHHH		17.4921963094
945UbiquitinationDSIASVVVPIIICLS
HHHHHHHHHHHHHHH		2.3623000965
952UbiquitinationVPIIICLSIIIAFLF
HHHHHHHHHHHHHHH		13.8221963094
953UbiquitinationPIIICLSIIIAFLFI
HHHHHHHHHHHHHHH		1.3822817900
954UbiquitinationIIICLSIIIAFLFIN
HHHHHHHHHHHHHHH		1.3421890473
958UbiquitinationLSIIIAFLFINQKKQ
HHHHHHHHHHHCCCC		2.8921963094
959UbiquitinationSIIIAFLFINQKKQW
HHHHHHHHHHCCCCE		3.8821963094
960UbiquitinationIIIAFLFINQKKQWI
HHHHHHHHHCCCCEE		6.0922817900
965UbiquitinationLFINQKKQWIPLLCW
HHHHCCCCEEEEEEE		50.8221963094
968UbiquitinationNQKKQWIPLLCWYRT
HCCCCEEEEEEEECC		19.1321963094
969UbiquitinationQKKQWIPLLCWYRTP
CCCCEEEEEEEECCC		4.5322817900
975PhosphorylationPLLCWYRTPTKPSSL
EEEEEECCCCCCCHH		21.4425278378
977PhosphorylationLCWYRTPTKPSSLNN
EEEECCCCCCCHHCC		55.7825278378
978UbiquitinationCWYRTPTKPSSLNNQ
EEECCCCCCCHHCCE		44.0723000965
980PhosphorylationYRTPTKPSSLNNQLV
ECCCCCCCHHCCEEE		49.3525278378
981PhosphorylationRTPTKPSSLNNQLVS
CCCCCCCHHCCEEEE		43.5825278378
983UbiquitinationPTKPSSLNNQLVSVD
CCCCCHHCCEEEEEE		35.8321963094
988PhosphorylationSLNNQLVSVDCKKGT
HHCCEEEEEECCCCC		22.3425278378
990UbiquitinationNNQLVSVDCKKGTRV
CCEEEEEECCCCCEE		30.8921963094
992UbiquitinationQLVSVDCKKGTRVQV
EEEEEECCCCCEEEE		50.1821963094
993UbiquitinationLVSVDCKKGTRVQVD
EEEEECCCCCEEEEC		72.3722817900
995PhosphorylationSVDCKKGTRVQVDSS
EEECCCCCEEEECCH		36.22-
999UbiquitinationKKGTRVQVDSSQRML
CCCCEEEECCHHCEE		7.6321963094
1016PhosphorylationAEPDARFSGFYSMQK
HCCCHHHCCCCCCHH		23.5721945579
1019UbiquitinationDARFSGFYSMQKQNH
CHHHCCCCCCHHCCC		13.5223000965
1019PhosphorylationDARFSGFYSMQKQNH
CHHHCCCCCCHHCCC		13.5221945579
1020PhosphorylationARFSGFYSMQKQNHL
HHHCCCCCCHHCCCC		16.6921945579
1023UbiquitinationSGFYSMQKQNHLQAD
CCCCCCHHCCCCCCC		44.4121963094
1033PhosphorylationHLQADNFYQTV----
CCCCCCCCCCC----		14.9925159151
1033UbiquitinationHLQADNFYQTV----
CCCCCCCCCCC----		14.9921963094
1034UbiquitinationLQADNFYQTV-----
CCCCCCCCCC-----		31.4822817900
1035PhosphorylationQADNFYQTV------
CCCCCCCCC------		19.4625159151
1064Ubiquitination-----------------------------------
-----------------------------------		21963094
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CRIM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRIM1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CRIM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CRIM1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRIM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-1035, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1019, AND MASSSPECTROMETRY.

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