CD97_HUMAN - dbPTM
CD97_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD97_HUMAN
UniProt AC P48960
Protein Name CD97 antigen
Gene Name CD97
Organism Homo sapiens (Human).
Sequence Length 835
Subcellular Localization Cell membrane
Multi-pass membrane protein.
CD97 antigen subunit alpha: Secreted, extracellular space.
Protein Description Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration (By similarity)..
Protein Sequence MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSSFSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKFIPEDPKVCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSSAEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAKSLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAEDPGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLSAVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQELLCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVEDWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVGSTIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVRVFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFLWSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAIAQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKVREEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI
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
637 (in isoform 2)Ubiquitination-4.3921906983
681 (in isoform 3)Ubiquitination-27.5121906983
730 (in isoform 1)Ubiquitination-63.4321906983
802S-palmitoylationEEYRKWACLVAGGSK
HHHHHHHHEEECCCC
2.8229575903

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 CD97_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD97_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 CD97_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPST1_HUMANTPST1physical
28514442
AGRE2_HUMANEMR2physical
28514442
NNTM_HUMANNNTphysical
28514442
RED1_HUMANADARB1physical
28514442
ZDH21_HUMANZDHHC21physical
28514442
T120B_HUMANTMEM120Bphysical
28514442
MTCH2_HUMANMTCH2physical
28514442
GL8D1_HUMANGLT8D1physical
28514442
TSN15_HUMANTSPAN15physical
28514442
MFSD8_HUMANMFSD8physical
28514442
NU5M_HUMANND5physical
28514442
GPC5B_HUMANGPRC5Bphysical
28514442
JPH1_HUMANJPH1physical
28514442
B4GT7_HUMANB4GALT7physical
28514442
PIGG_HUMANPIGGphysical
28514442
NDUB8_HUMANNDUFB8physical
28514442
VDAC3_HUMANVDAC3physical
28514442
SERC1_HUMANSERINC1physical
28514442
TM223_HUMANTMEM223physical
28514442
ALG6_HUMANALG6physical
28514442
TMPPE_HUMANTMPPEphysical
28514442
SNG2_HUMANSYNGR2physical
28514442
GBB2_HUMANGNB2physical
28514442
RASN_HUMANNRASphysical
28514442
LEMD2_HUMANLEMD2physical
28514442
FDFT_HUMANFDFT1physical
28514442
BACE2_HUMANBACE2physical
28514442
BET1_HUMANBET1physical
28514442
YIPF6_HUMANYIPF6physical
28514442
POTEF_HUMANPOTEFphysical
28514442
S29A1_HUMANSLC29A1physical
28514442
NAGPA_HUMANNAGPAphysical
28514442
ZDH18_HUMANZDHHC18physical
28514442
EXTL3_HUMANEXTL3physical
28514442
HMOX1_HUMANHMOX1physical
28514442
YIPF3_HUMANYIPF3physical
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 CD97_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-371, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-453, AND MASSSPECTROMETRY.
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 SER-831 AND SER-833, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818 AND SER-831, ANDMASS SPECTROMETRY.

TOP