CD47_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD47_HUMAN
• UniProt AC: Q08722
• Protein Name: Leukocyte surface antigen CD47
• Gene Name: CD47
• Organism: Homo sapiens (Human).
• Sequence Length: 323
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection..
• Protein Sequence: MWPLVAALLLGSACCGSAQLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTFDGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTELTREGETIIELKYRVVSWFSPNENILIVIFPIFAILLFWGQFGIKTLKYRSGGMDEKTIALLVAGLVITVIVIVGAILFVPGEYSLKNATGLGLIVTSTGILILLHYYVFSTAIGLTSFVIAILVIQVIAYILAVVGLSLCIAACIPMHGPLLISGLSILALAQLLGLVYMKFVASNQKTIQPPRKAVEEPLNAFKESKGMMNDE

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
19	Pyrrolidone_carboxylic_acid	SACCGSAQLLFNKTK HHHHHHHHHHCCCCC	40.16	-
19	Pyrrolidone_carboxylic_acid	SACCGSAQLLFNKTK HHHHHHHHHHCCCCC	40.16	18657508
19	Pyrrolidone_carboxylic_acid	SACCGSAQLLFNKTK HHHHHHHHHHCCCCC	40.16	18657508
23	N-linked_Glycosylation	GSAQLLFNKTKSVEF HHHHHHCCCCCEEEE	51.56	18657508
34	N-linked_Glycosylation	SVEFTFCNDTVVIPC EEEEEECCCEEEEEE	43.74	UniProtKB CARBOHYD
50	N-linked_Glycosylation	VTNMEAQNTTEVYVK EEECCCCCCEEEEEE	56.89	18657508
73	N-linked_Glycosylation	YTFDGALNKSTVPTD EEEECCCCCCCCCCC	35.38	18657508
74 (in isoform 4)	Ubiquitination	-	48.64	21906983
74 (in isoform 3)	Ubiquitination	-	48.64	21906983
74 (in isoform 2)	Ubiquitination	-	48.64	21906983
74 (in isoform 1)	Ubiquitination	-	48.64	21906983
74	Ubiquitination	TFDGALNKSTVPTDF EEECCCCCCCCCCCC	48.64	21906983
85	Ubiquitination	PTDFSSAKIEVSQLL CCCCCCCEEEHHHHH	41.15	-
89	Phosphorylation	SSAKIEVSQLLKGDA CCCEEEHHHHHCCCC	11.43	-
93	Ubiquitination	IEVSQLLKGDASLKM EEHHHHHCCCCCCCC	64.44	-
99	Ubiquitination	LKGDASLKMDKSDAV HCCCCCCCCCHHHHC	42.42	-
102	Ubiquitination	DASLKMDKSDAVSHT CCCCCCCHHHHCCCC	46.89	-
111	N-linked_Glycosylation	DAVSHTGNYTCEVTE HHCCCCCCEEEEEEE	30.05	18657508
203	Phosphorylation	LFVPGEYSLKNATGL HCCCCCCCCCCCCCC	28.68	24719451
206	N-linked_Glycosylation	PGEYSLKNATGLGLI CCCCCCCCCCCCCEE	48.29	UniProtKB CARBOHYD
288	Phosphorylation	AQLLGLVYMKFVASN HHHHHHHHHHHHHCC	10.30	-
304	Ubiquitination	KTIQPPRKAVEEPLN CCCCCCHHHHHHHHH	63.66	-
314	Ubiquitination	EEPLNAFKESKGMMN HHHHHHHHHHHCCCC	59.68	21906983
314 (in isoform 1)	Ubiquitination	-	59.68	21906983
316	Phosphorylation	PLNAFKESKGMMNDE HHHHHHHHHCCCCCC	34.79	28355574
317	Ubiquitination	LNAFKESKGMMNDE- HHHHHHHHCCCCCC-	52.49	2190698
317 (in isoform 1)	Ubiquitination	-	52.49	21906983

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CD47_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD47_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CD47_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BNIP3_HUMAN	BNIP3	physical	12690108
ITB1_HUMAN	ITGB1	physical	10397731
SYNE4_HUMAN	SYNE4	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	21125662
GBB3_HUMAN	GNB3	physical	21125662
GNAQ_HUMAN	GNAQ	physical	21125662
GNAS3_HUMAN	GNAS	physical	21125662
GNAS2_HUMAN	GNAS	physical	21125662
ALEX_HUMAN	GNAS	physical	21125662
GNAS1_HUMAN	GNAS	physical	21125662

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Paired receptor specificity explained by structures of signalregulatory proteins alone and complexed with CD47.";
Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I.,Barclay A.N.;
Mol. Cell 31:266-277(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-136 IN COMPLEX WITHSIRPA, DISULFIDE BOND, GLYCOSYLATION AT ASN-23; ASN-50; ASN-73 ANDASN-111, AND PYROGLUTAMATE FORMATION AT GLN-19.
PubMed: 18657508

"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-50 AND ASN-73, AND MASSSPECTROMETRY.
PubMed: 19349973

"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-73 AND ASN-111, AND MASSSPECTROMETRY.
PubMed: 19159218