CD27_HUMAN - dbPTM
CD27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD27_HUMAN
UniProt AC P26842
Protein Name CD27 antigen
Gene Name CD27
Organism Homo sapiens (Human).
Sequence Length 260
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor for CD70/CD27L. May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1..
Protein Sequence MARPHPWWLCVLGTLVGLSATPAPKSCPERHYWAQGKLCCQMCEPGTFLVKDCDQHRKAAQCDPCIPGVSFSPDHHTRPHCESCRHCNSGLLVRNCTITANAECACRNGWQCRDKECTECDPLPNPSLTARSSQALSPHPQPTHLPYVSEMLEARTAGHMQTLADFRQLPARTLSTHWPPQRSLCSSDFIRILVIFSGMFLVFTLAGALFLHQRRKYRSNKGESPVEPAEPCHYSCPREEEGSTIPIQEDYRKPEPACSP
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
95N-linked_GlycosylationNSGLLVRNCTITANA
CCCEEEECCEEECCC		21.58UniProtKB CARBOHYD
127O-linked_GlycosylationCDPLPNPSLTARSSQ
CCCCCCCCCCCCCCC		45.0222171320
147PhosphorylationPQPTHLPYVSEMLEA
CCCCCHHHHHHHHHH		23.9830576142
149O-linked_GlycosylationPTHLPYVSEMLEART
CCCHHHHHHHHHHHH		16.08OGP
149PhosphorylationPTHLPYVSEMLEART
CCCHHHHHHHHHHHH		16.0830576142
156PhosphorylationSEMLEARTAGHMQTL
HHHHHHHHHCCHHHH		44.0030576142
156O-linked_GlycosylationSEMLEARTAGHMQTL
HHHHHHHHHCCHHHH		44.00OGP
162O-linked_GlycosylationRTAGHMQTLADFRQL
HHHCCHHHHHHHHHC		19.15OGP
173PhosphorylationFRQLPARTLSTHWPP
HHHCCCHHHCCCCCC		27.4522210691
175PhosphorylationQLPARTLSTHWPPQR
HCCCHHHCCCCCCCH		20.0129632367
176PhosphorylationLPARTLSTHWPPQRS
CCCHHHCCCCCCCHH		30.9522210691
183PhosphorylationTHWPPQRSLCSSDFI
CCCCCCHHHCCCHHH		28.60-
219PhosphorylationHQRRKYRSNKGESPV
HHHHHHHCCCCCCCC		39.54-
221UbiquitinationRRKYRSNKGESPVEP
HHHHHCCCCCCCCCC		66.36-
243PhosphorylationCPREEEGSTIPIQED
CCCCCCCCCCCCCCC		26.8330108239
244PhosphorylationPREEEGSTIPIQEDY
CCCCCCCCCCCCCCC		41.4530108239
251PhosphorylationTIPIQEDYRKPEPAC
CCCCCCCCCCCCCCC		21.5630108239
253UbiquitinationPIQEDYRKPEPACSP
CCCCCCCCCCCCCCC		47.72-
259PhosphorylationRKPEPACSP------
CCCCCCCCC------		35.4323401153
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 CD27_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD27_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 CD27_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIVA_HUMANSIVA1physical
9177220
TRAF1_HUMANTRAF1physical
9794406
TRAF3_HUMANTRAF3physical
9794406
TRAF2_HUMANTRAF2physical
9794406
TRAF3_HUMANTRAF3physical
9582383
TRAF5_HUMANTRAF5physical
9582383
TRAF2_HUMANTRAF2physical
9582383
SIVA_HUMANSIVA1physical
16683188
TRAF2_HUMANTRAF2physical
9692890
C1GLT_HUMANC1GALT1physical
26186194
AT2B3_HUMANATP2B3physical
26186194
COQ8B_HUMANADCK4physical
26186194
BIRC2_HUMANBIRC2physical
26186194
CD59_HUMANCD59physical
26186194
CTNA2_HUMANCTNNA2physical
26186194
TCAF2_HUMANFAM115Cphysical
26186194
TTYH3_HUMANTTYH3physical
26186194
ADCY9_HUMANADCY9physical
26186194
SCAM1_HUMANSCAMP1physical
26186194
SEMG2_HUMANSEMG2physical
26186194
SEMG1_HUMANSEMG1physical
26186194
TRAF2_HUMANTRAF2physical
26186194
GOGA5_HUMANGOLGA5physical
26186194
CD032_HUMANC4orf32physical
26186194
MKS3_HUMANTMEM67physical
26186194
S2551_HUMANSLC25A51physical
26186194
SAAL1_HUMANSAAL1physical
26186194
S19A2_HUMANSLC19A2physical
26186194
GBB2_HUMANGNB2physical
26186194
RASH_HUMANHRASphysical
26186194
TM214_HUMANTMEM214physical
26186194
CREL1_HUMANCRELD1physical
26186194
EPCR_HUMANPROCRphysical
26186194
CD70_HUMANCD70physical
26186194
S2551_HUMANSLC25A51physical
28514442
C1GLT_HUMANC1GALT1physical
28514442
CD70_HUMANCD70physical
28514442
TCAF2_HUMANFAM115Cphysical
28514442
MKS3_HUMANTMEM67physical
28514442
SEMG2_HUMANSEMG2physical
28514442
SEMG1_HUMANSEMG1physical
28514442
AT2B3_HUMANATP2B3physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
S19A2_HUMANSLC19A2physical
28514442
CREL1_HUMANCRELD1physical
28514442
TRAF2_HUMANTRAF2physical
28514442
SCAM1_HUMANSCAMP1physical
28514442
ADCY9_HUMANADCY9physical
28514442
RASH_HUMANHRASphysical
28514442
COQ8B_HUMANADCK4physical
28514442
TTYH3_HUMANTTYH3physical
28514442
GBB2_HUMANGNB2physical
28514442
CTNA2_HUMANCTNNA2physical
28514442
CD032_HUMANC4orf32physical
28514442
BIRC2_HUMANBIRC2physical
28514442
CD59_HUMANCD59physical
28514442
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
OMIM Disease
615122Lymphoproliferative syndrome 2 (LPFS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD27_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT SER-127, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.

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