CD5_HUMAN - dbPTM
CD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD5_HUMAN
UniProt AC P06127
Protein Name T-cell surface glycoprotein CD5
Gene Name CD5
Organism Homo sapiens (Human).
Sequence Length 495
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description May act as a receptor in regulating T-cell proliferation..
Protein Sequence MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL
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
38PhosphorylationPDFQARLTRSNSKCQ
HHHHHHHCCCCCCCC
26.8829083192
40PhosphorylationFQARLTRSNSKCQGQ
HHHHHCCCCCCCCEE
39.9729083192
42PhosphorylationARLTRSNSKCQGQLE
HHHCCCCCCCCEEEE
35.7329083192
51PhosphorylationCQGQLEVYLKDGWHM
CCEEEEEEEECCEEE
9.9229083192
79UbiquitinationEDPSQASKVCQRLNC
CCHHHHHHHHHHCCC
50.47-
116N-linked_GlycosylationGQLGSFSNCSHSRND
EECCCCCCCCCCCCC
29.33UniProtKB CARBOHYD
142PhosphorylationPQKTTPPTTRPPPTT
CCCCCCCCCCCCCCC
36.3222210691
150PhosphorylationTRPPPTTTPEPTAPP
CCCCCCCCCCCCCCC
28.2922210691
184O-linked_GlycosylationYSGSLGGTISYEAQD
ECCCCCCEEEEECCC
12.64OGP
186PhosphorylationGSLGGTISYEAQDKT
CCCCCEEEEECCCCC
19.43-
208PhosphorylationCNNLQCGSFLKHLPE
HCCCCCCHHHHHCCC
34.7224719451
211UbiquitinationLQCGSFLKHLPETEA
CCCCHHHHHCCCCCC
40.8829967540
241N-linked_GlycosylationPIQWKIQNSSCTSLE
CCEEEEECCCCCCHH
39.09UniProtKB CARBOHYD
273UbiquitinationLCSGFQPKVQSRLVG
HHCCCCHHHCEEECC
41.97-
308PhosphorylationCDSSSARSSLRWEEV
CCCCCCHHHCCHHHH
33.1829083192
309PhosphorylationDSSSARSSLRWEEVC
CCCCCHHHCCHHHHH
19.1929083192
327PhosphorylationQCGSVNSYRVLDAGD
CCCCCCEEEEECCCC
10.2722210691
346UbiquitinationGLFCPHQKLSQCHEL
CCCCCCHHHHHHHHH
47.25-
361UbiquitinationWERNSYCKKVFVTCQ
HHHCCCCCEEEEEEC
43.6829967540
421PhosphorylationQRQWIGPTGMNQNMS
CCCCCCCCCCCCCCC
43.8023684312
428PhosphorylationTGMNQNMSFHRNHTA
CCCCCCCCEECCCCH
26.0023401153
434PhosphorylationMSFHRNHTATVRSHA
CCEECCCCHHHHHHC
27.8030576142
436PhosphorylationFHRNHTATVRSHAEN
EECCCCHHHHHHCCC
20.0130576142
439PhosphorylationNHTATVRSHAENPTA
CCCHHHHHHCCCCCC
23.7819605366
445PhosphorylationRSHAENPTASHVDNE
HHHCCCCCCCCCCCC
52.9928796482
447PhosphorylationHAENPTASHVDNEYS
HCCCCCCCCCCCCCC
26.9028796482
453PhosphorylationASHVDNEYSQPPRNS
CCCCCCCCCCCCCCC
20.8919605366
454PhosphorylationSHVDNEYSQPPRNSH
CCCCCCCCCCCCCCC
29.9928796482
460PhosphorylationYSQPPRNSHLSAYPA
CCCCCCCCCCCHHHH
27.3823401153
463PhosphorylationPPRNSHLSAYPALEG
CCCCCCCCHHHHHHH
21.9728122231
465PhosphorylationRNSHLSAYPALEGAL
CCCCCCHHHHHHHHH
5.9011751967
475PhosphorylationLEGALHRSSMQPDNS
HHHHHHHHCCCCCCC
21.2928796482
476PhosphorylationEGALHRSSMQPDNSS
HHHHHHHCCCCCCCC
22.7628796482
482PhosphorylationSSMQPDNSSDSDYDL
HCCCCCCCCCCCCCC
42.7923401153
483PhosphorylationSMQPDNSSDSDYDLH
CCCCCCCCCCCCCCC
47.6023401153
485PhosphorylationQPDNSSDSDYDLHGA
CCCCCCCCCCCCCCH
39.7628787133
487PhosphorylationDNSSDSDYDLHGAQR
CCCCCCCCCCCCHHC
25.1028787133

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
434TPhosphorylationKinasePRKCAP17252
GPS
434TPhosphorylationKinasePKCAP05696
PSP
434TPhosphorylationKinasePRKCBP68403
GPS
434TPhosphorylationKinasePRKCGP05129
GPS
436TPhosphorylationKinasePRKCGP05129
GPS
436TPhosphorylationKinasePRKCAP17252
GPS
436TPhosphorylationKinasePKCAP05696
PSP
436TPhosphorylationKinasePRKCBP68403
GPS
453YPhosphorylationKinaseLCKP06239
PSP
453YPhosphorylationKinaseFYNP06241
PSP
482SPhosphorylationKinaseCK2-FAMILY-GPS
482SPhosphorylationKinaseCK2_GROUP-PhosphoELM
482SPhosphorylationKinaseCSNK2A1P68400
GPS
483SPhosphorylationKinaseCK2_GROUP-PhosphoELM
483SPhosphorylationKinaseCSNK2A1P68400
GPS
483SPhosphorylationKinaseCK2-FAMILY-GPS
485SPhosphorylationKinaseCK2_GROUP-PhosphoELM
485SPhosphorylationKinaseCK2-FAMILY-GPS
485SPhosphorylationKinaseCSNK2A1P68400
GPS
487YPhosphorylationKinaseLCKP06239
PSP
487YPhosphorylationKinaseFYNP06241
PSP
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD5_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 CD5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD6_HUMANCD6physical
12473675
PTN6_HUMANPTPN6physical
10082557
CBL_HUMANCBLphysical
9603468
RASA1_HUMANRASA1physical
9603468
LCK_HUMANLCKphysical
21757751
FYN_HUMANFYNphysical
21757751
CD72_HUMANCD72physical
1711157

Drug and Disease Associations
Kegg Disease
H00002 Acute lymphoblastic leukemia (ALL) (precursor T lymphoblastic leukemia)
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D06381 Zolimomab aritox (USAN); Orthozyme CD5 plus (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; TYR-453; SER-482;SER-483 AND SER-485, AND MASS SPECTROMETRY.
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; TYR-453 ANDSER-460, AND MASS SPECTROMETRY.

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