CDCP1_HUMAN - dbPTM
CDCP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDCP1_HUMAN
UniProt AC Q9H5V8
Protein Name CUB domain-containing protein 1
Gene Name CDCP1
Organism Homo sapiens (Human).
Sequence Length 836
Subcellular Localization Isoform 1: Cell membrane
Single-pass membrane protein . Shedding may also lead to a soluble peptide.
Isoform 3: Secreted.
Protein Description May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis..
Protein Sequence MAGLNCGVSIALLGVLLLGAARLPRGAEAFEIALPRESNITVLIKLGTPTLLAKPCYIVISKRHITMLSIKSGERIVFTFSCQSPENHFVIEIQKNIDCMSGPCPFGEVQLQPSTSLLPTLNRTFIWDVKAHKSIGLELQFSIPRLRQIGPGESCPDGVTHSISGRIDATVVRIGTFCSNGTVSRIKMQEGVKMALHLPWFHPRNVSGFSIANRSSIKRLCIIESVFEGEGSATLMSANYPEGFPEDELMTWQFVVPAHLRASVSFLNFNLSNCERKEERVEYYIPGSTTNPEVFKLEDKQPGNMAGNFNLSLQGCDQDAQSPGILRLQFQVLVQHPQNESNKIYVVDLSNERAMSLTIEPRPVKQSRKFVPGCFVCLESRTCSSNLTLTSGSKHKISFLCDDLTRLWMNVEKTISCTDHRYCQRKSYSLQVPSDILHLPVELHDFSWKLLVPKDRLSLVLVPAQKLQQHTHEKPCNTSFSYLVASAIPSQDLYFGSFCPGGSIKQIQVKQNISVTLRTFAPSFQQEASRQGLTVSFIPYFKEEGVFTVTPDTKSKVYLRTPNWDRGLPSLTSVSWNISVPRDQVACLTFFKERSGVVCQTGRAFMIIQEQRTRAEEIFSLDEDVLPKPSFHHHSFWVNISNCSPTSGKQLDLLFSVTLTPRTVDLTVILIAAVGGGVLLLSALGLIICCVKKKKKKTNKGPAVGIYNDNINTEMPRQPKKFQKGRKDNDSHVYAVIEDTMVYGHLLQDSSGSFLQPEVDTYRPFQGTMGVCPPSPPTICSRAPTAKLATEEPPPRSPPESESEPYTFSHPNNGDVSSKDTDIPLLNTQEPMEPAE
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
9PhosphorylationAGLNCGVSIALLGVL
CCCCHHHHHHHHHHH		6.3422817900
39N-linked_GlycosylationIALPRESNITVLIKL
EECCCCCCEEEEEEC		29.24UniProtKB CARBOHYD
70UbiquitinationRHITMLSIKSGERIV
CCEEEEEECCCCEEE		3.4722817900
71UbiquitinationHITMLSIKSGERIVF
CEEEEEECCCCEEEE		49.3722817900
71 (in isoform 1)Ubiquitination-49.3721906983
71 (in isoform 3)Ubiquitination-49.3721906983
109 (in isoform 2)Ubiquitination-7.6221906983
122N-linked_GlycosylationTSLLPTLNRTFIWDV
CCCCCCCCCEEEEEE		43.34UniProtKB CARBOHYD
142PhosphorylationIGLELQFSIPRLRQI
CCCEEEEECCCHHCC		20.7922817900
156 (in isoform 2)Ubiquitination-51.1521906983
164PhosphorylationDGVTHSISGRIDATV
CCCCCCCCCCEEEEE		25.6522817900
170PhosphorylationISGRIDATVVRIGTF
CCCCEEEEEEEEEEE		18.7822817900
180N-linked_GlycosylationRIGTFCSNGTVSRIK
EEEEECCCCEEEEEE		51.87UniProtKB CARBOHYD
184PhosphorylationFCSNGTVSRIKMQEG
ECCCCEEEEEEECCC		28.2922817900
186UbiquitinationSNGTVSRIKMQEGVK
CCCEEEEEEECCCCE		3.2027667366
187UbiquitinationNGTVSRIKMQEGVKM
CCEEEEEEECCCCEE		33.1627667366
205N-linked_GlycosylationLPWFHPRNVSGFSIA
CCCCCCCCCCCCCCC		36.44UniProtKB CARBOHYD
210PhosphorylationPRNVSGFSIANRSSI
CCCCCCCCCCCHHHC		25.0722817900
270N-linked_GlycosylationSVSFLNFNLSNCERK
EEEEEEEECCCCCCH		41.30UniProtKB CARBOHYD
283PhosphorylationRKEERVEYYIPGSTT
CHHHEEEEECCCCCC		12.11-
284PhosphorylationKEERVEYYIPGSTTN
HHHEEEEECCCCCCC		6.27-
295UbiquitinationSTTNPEVFKLEDKQP
CCCCHHEEECCCCCC		7.7322817900
296 (in isoform 3)Ubiquitination-57.0221906983
296 (in isoform 1)Ubiquitination-57.0221906983
296UbiquitinationTTNPEVFKLEDKQPG
CCCHHEEECCCCCCC		57.0221906983
299UbiquitinationPEVFKLEDKQPGNMA
HHEEECCCCCCCCCC		66.3822817900
300UbiquitinationEVFKLEDKQPGNMAG
HEEECCCCCCCCCCC		49.3622817900
310N-linked_GlycosylationGNMAGNFNLSLQGCD
CCCCCCEEEEEECCC		32.49UniProtKB CARBOHYD
341PhosphorylationVQHPQNESNKIYVVD
EECCCCCCCCEEEEE		51.4722210691
342UbiquitinationQHPQNESNKIYVVDL
ECCCCCCCCEEEEEC		28.6822817900
343UbiquitinationHPQNESNKIYVVDLS
CCCCCCCCEEEEECC		44.7022817900
343 (in isoform 1)Ubiquitination-44.7021906983
355 (in isoform 2)Ubiquitination-4.1721906983
367 (in isoform 2)Ubiquitination-31.5521906983
386N-linked_GlycosylationESRTCSSNLTLTSGS
ECCCCCCCEEEECCC		22.28UniProtKB CARBOHYD
458PhosphorylationLVPKDRLSLVLVPAQ
EEECCCEEEEEEEHH		19.82-
513 (in isoform 2)Ubiquitination-3.0421906983
516PhosphorylationVKQNISVTLRTFAPS
EECCEEEEEEECCHH		12.0624719451
541UbiquitinationTVSFIPYFKEEGVFT
EEEEEECCCCCCEEE		7.2422817900
542 (in isoform 1)Ubiquitination-49.3521906983
542UbiquitinationVSFIPYFKEEGVFTV
EEEEECCCCCCEEEE		49.3522817900
553UbiquitinationVFTVTPDTKSKVYLR
EEEECCCCCCCEEEE		38.1222817900
554 (in isoform 1)Ubiquitination-56.5121906983
554UbiquitinationFTVTPDTKSKVYLRT
EEECCCCCCCEEEEC		56.5121906983
555UbiquitinationTVTPDTKSKVYLRTP
EECCCCCCCEEEECC		29.4622817900
556UbiquitinationVTPDTKSKVYLRTPN
ECCCCCCCEEEECCC		36.1322817900
575PhosphorylationLPSLTSVSWNISVPR
CCCCCEEEEEECCCH		17.7422817900
579PhosphorylationTSVSWNISVPRDQVA
CEEEEEECCCHHHEE		23.9022817900
600 (in isoform 2)Ubiquitination-35.0721906983
660PhosphorylationLLFSVTLTPRTVDLT
EEEEEEECCCCCCEE		11.0224719451
694UbiquitinationIICCVKKKKKKTNKG
HHHHHHCCCCCCCCC		65.2022817900
695UbiquitinationICCVKKKKKKTNKGP
HHHHHCCCCCCCCCC		69.2722817900
696UbiquitinationCCVKKKKKKTNKGPA
HHHHCCCCCCCCCCC		73.9522817900
697UbiquitinationCVKKKKKKTNKGPAV
HHHCCCCCCCCCCCC		67.2322817900
699UbiquitinationKKKKKKTNKGPAVGI
HCCCCCCCCCCCCEE		57.0522817900
700 (in isoform 1)Ubiquitination-72.0721906983
700UbiquitinationKKKKKTNKGPAVGIY
CCCCCCCCCCCCEEE		72.0722817900
707PhosphorylationKGPAVGIYNDNINTE
CCCCCEEECCCCCCC		15.5518707149
713PhosphorylationIYNDNINTEMPRQPK
EECCCCCCCCCCCCC		29.8428442448
731PhosphorylationKGRKDNDSHVYAVIE
CCCCCCCCCEEEEEE		22.5526356563
734PhosphorylationKDNDSHVYAVIEDTM
CCCCCCEEEEEECCE		6.9620501830
740PhosphorylationVYAVIEDTMVYGHLL
EEEEEECCEEEEEEC		8.8526356563
743PhosphorylationVIEDTMVYGHLLQDS
EEECCEEEEEECCCC		6.4926356563
750PhosphorylationYGHLLQDSSGSFLQP
EEEECCCCCCCCCCC		24.5226356563
751PhosphorylationGHLLQDSSGSFLQPE
EEECCCCCCCCCCCC		46.9026356563
753PhosphorylationLLQDSSGSFLQPEVD
ECCCCCCCCCCCCCC		25.4026356563
761PhosphorylationFLQPEVDTYRPFQGT
CCCCCCCCCCCCCCC		26.9726356563
762PhosphorylationLQPEVDTYRPFQGTM
CCCCCCCCCCCCCCC		16.3026356563
775PhosphorylationTMGVCPPSPPTICSR
CCCCCCCCCCCCCCC		28.7527050516
786UbiquitinationICSRAPTAKLATEEP
CCCCCCCCCCCCCCC		12.1022817900
787 (in isoform 1)Ubiquitination-40.9321906983
787UbiquitinationCSRAPTAKLATEEPP
CCCCCCCCCCCCCCC		40.9322817900
790PhosphorylationAPTAKLATEEPPPRS
CCCCCCCCCCCCCCC		51.8528152594
797PhosphorylationTEEPPPRSPPESESE
CCCCCCCCCCCCCCC		51.0528355574
801PhosphorylationPPRSPPESESEPYTF
CCCCCCCCCCCCCCC		52.8028152594
803PhosphorylationRSPPESESEPYTFSH
CCCCCCCCCCCCCCC		53.8227794612
806PhosphorylationPESESEPYTFSHPNN
CCCCCCCCCCCCCCC		19.1627273156
807PhosphorylationESESEPYTFSHPNNG
CCCCCCCCCCCCCCC		29.4028152594
809PhosphorylationESEPYTFSHPNNGDV
CCCCCCCCCCCCCCC		30.1828152594
817PhosphorylationHPNNGDVSSKDTDIP
CCCCCCCCCCCCCCC		36.0928152594
818PhosphorylationPNNGDVSSKDTDIPL
CCCCCCCCCCCCCCC		34.1128152594
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
734YPhosphorylationKinasePTK2Q05397
GPS
734YPhosphorylationKinaseSRCP12931
PSP
743YPhosphorylationKinaseSRCP12931
PSP
762YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDCP1_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 CDCP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VWA1_HUMANVWA1physical
28514442
LEPR_HUMANLEPRphysical
28514442
MA1A1_HUMANMAN1A1physical
28514442
LRFN1_HUMANLRFN1physical
28514442
CSTN1_HUMANCLSTN1physical
28514442
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 CDCP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-707, AND MASSSPECTROMETRY.

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