dbPTM

CR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CR2_HUMAN
UniProt AC	P20023
Protein Name	Complement receptor type 2
Gene Name	CR2
Organism	Homo sapiens (Human).
Sequence Length	1033
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Receptor for complement C3Dd, for the Epstein-Barr virus on human B-cells and T-cells and for HNRNPU. [PubMed: 7753047 Participates in B lymphocytes activation]
Protein Sequence	MGAAGLLGVFLALVAPGVLGISCGSPPPILNGRISYYSTPIAVGTVIRYSCSGTFRLIGEKSLLCITKDKVDGTWDKPAPKCEYFNKYSSCPEPIVPGGYKIRGSTPYRHGDSVTFACKTNFSMNGNKSVWCQANNMWGPTRLPTCVSVFPLECPALPMIHNGHHTSENVGSIAPGLSVTYSCESGYLLVGEKIINCLSSGKWSAVPPTCEEARCKSLGRFPNGKVKEPPILRVGVTANFFCDEGYRLQGPPSSRCVIAGQGVAWTKMPVCEEIFCPSPPPILNGRHIGNSLANVSYGSIVTYTCDPDPEEGVNFILIGESTLRCTVDSQKTGTWSGPAPRCELSTSAVQCPHPQILRGRMVSGQKDRYTYNDTVIFACMFGFTLKGSKQIRCNAQGTWEPSAPVCEKECQAPPNILNGQKEDRHMVRFDPGTSIKYSCNPGYVLVGEESIQCTSEGVWTPPVPQCKVAACEATGRQLLTKPQHQFVRPDVNSSCGEGYKLSGSVYQECQGTIPWFMEIRLCKEITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTCNPGPERGVEFSLIGESTIRCTSNDQERGTWSGPAPLCKLSLLAVQCSHVHIANGYKISGKEAPYFYNDTVTFKCYSGFTLKGSSQIRCKADNTWDPEIPVCEKETCQHVRQSLQELPAGSRVELVNTSCQDGYQLTGHAYQMCQDAENGIWFKKIPLCKVIHCHPPPVIVNGKHTGMMAENFLYGNEVSYECDQGFYLLGEKKLQCRSDSKGHGSWSGPSPQCLRSPPVTRCPNPEVKHGYKLNKTHSAYSHNDIVYVDCNPGFIMNGSRVIRCHTDNTWVPGVPTCIKKAFIGCPPPPKTPNGNHTGGNIARFSPGMSILYSCDQGYLLVGEALLLCTHEGTWSQPAPHCKEVNCSSPADMDGIQKGLEPRKMYQYGAVVTLECEDGYMLEGSPQSQCQSDHQWNPPLAVCRSRSLAPVLCGIAAGLILLTFLIVITLYVISKHRARNYYTDTSQKEAFHLEAREVYSVDPYNPAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Phosphorylation	LNGRISYYSTPIAVG CCCEEEEECCCEEEE	10.16	24719451
39	Phosphorylation	GRISYYSTPIAVGTV CEEEEECCCEEEEEE	11.55	24719451
45	Phosphorylation	STPIAVGTVIRYSCS CCCEEEEEEEEEECC	13.22	22468782
84	Phosphorylation	KPAPKCEYFNKYSSC CCCCCCCCCCCCCCC	23.17	24719451
88	Phosphorylation	KCEYFNKYSSCPEPI CCCCCCCCCCCCCCC	13.61	24719451
100	Phosphorylation	EPIVPGGYKIRGSTP CCCCCCCEEEECCCC	14.79	24719451
121	N-linked_Glycosylation	VTFACKTNFSMNGNK EEEEEEECCCCCCCE	16.70	12122212
127	N-linked_Glycosylation	TNFSMNGNKSVWCQA ECCCCCCCEEEEEEE	28.55	12122212
141	Phosphorylation	ANNMWGPTRLPTCVS ECCCCCCCCCCCEEE	40.68	-
145	Phosphorylation	WGPTRLPTCVSVFPL CCCCCCCCEEEEEEE	30.08	-
148	Phosphorylation	TRLPTCVSVFPLECP CCCCCEEEEEEECCC	21.86	-
204	Phosphorylation	CLSSGKWSAVPPTCE HHHCCCCCCCCCCCH	23.91	-
209	Phosphorylation	KWSAVPPTCEEARCK CCCCCCCCCHHHHHH	26.86	-
216	Acetylation	TCEEARCKSLGRFPN CCHHHHHHHCCCCCC	43.07	19829819
225	Acetylation	LGRFPNGKVKEPPIL CCCCCCCCCCCCCEE	57.69	19829827
294	N-linked_Glycosylation	HIGNSLANVSYGSIV CCCCCCCCCCCCEEE	28.67	UniProtKB CARBOHYD
363	Phosphorylation	ILRGRMVSGQKDRYT HHCCCCCCCCCCCCE	26.60	30622161
372	N-linked_Glycosylation	QKDRYTYNDTVIFAC CCCCCEECCCEEEEE	30.58	UniProtKB CARBOHYD
492	N-linked_Glycosylation	QFVRPDVNSSCGEGY HCCCCCCCCCCCCCC	35.27	UniProtKB CARBOHYD
506	Phosphorylation	YKLSGSVYQECQGTI CCCCCHHHHHCCCCC	10.57	-
623	N-linked_Glycosylation	KEAPYFYNDTVTFKC CCCCCEECCCEEEEE	28.69	19349973
631	Phosphorylation	DTVTFKCYSGFTLKG CCEEEEEECCEEEEC	16.66	29759185
632	Phosphorylation	TVTFKCYSGFTLKGS CEEEEEECCEEEECC	36.58	29759185
635	Phosphorylation	FKCYSGFTLKGSSQI EEEECCEEEECCCEE	30.96	29759185
682	N-linked_Glycosylation	GSRVELVNTSCQDGY CCCEEEEECCCCCCC	38.61	UniProtKB CARBOHYD
782	Phosphorylation	PSPQCLRSPPVTRCP CCCHHHCCCCCCCCC	22.17	20363803
800	N-linked_Glycosylation	VKHGYKLNKTHSAYS CCCCEECCCCCCCCC	42.92	UniProtKB CARBOHYD
823	N-linked_Glycosylation	CNPGFIMNGSRVIRC CCCCCEECCCEEEEE	40.24	UniProtKB CARBOHYD
841	Phosphorylation	NTWVPGVPTCIKKAF CCCCCCCCCEEEHHH	27.71	24719451
861	N-linked_Glycosylation	PPKTPNGNHTGGNIA CCCCCCCCCCCCCCC	35.87	UniProtKB CARBOHYD
911	N-linked_Glycosylation	APHCKEVNCSSPADM CCCCCCCCCCCCCCC	22.50	UniProtKB CARBOHYD
994	Phosphorylation	LTFLIVITLYVISKH HHHHHHHHHHHHHHH	10.92	-
1007	Phosphorylation	KHRARNYYTDTSQKE HHHHHHCCCCCCHHH	11.16	30108239
1008	Phosphorylation	HRARNYYTDTSQKEA HHHHHCCCCCCHHHE	23.57	30108239
1010	Phosphorylation	ARNYYTDTSQKEAFH HHHCCCCCCHHHEEE	25.84	30108239
1011	Phosphorylation	RNYYTDTSQKEAFHL HHCCCCCCHHHEEEE	41.90	30108239
1024	Phosphorylation	HLEAREVYSVDPYNP EECEEEEEECCCCCC	9.75	19060867
1025	Phosphorylation	LEAREVYSVDPYNPA ECEEEEEECCCCCCC	25.81	30108239
1029	Phosphorylation	EVYSVDPYNPAS--- EEEECCCCCCCC---	29.34	21253578
1088	Phosphorylation	-------------------------------------------------------------- --------------------------------------------------------------		27642862

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 CR2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CR2_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 CR2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD81_HUMAN	CD81	physical	1383329
IFM1_HUMAN	IFITM1	physical	1383329
FCER2_HUMAN	FCER2	physical	7515913
ANXA6_HUMAN	ANXA6	physical	1831222

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610927	Systemic lupus erythematosus 9 (SLEB9)
614699	Immunodeficiency, common variable, 7 (CVID7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CR2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The crystal structure of human CD21: Implications for Epstein-Barrvirus and C3d binding."; Prota A.E., Sage D.R., Stehle T., Fingeroth J.D.; Proc. Natl. Acad. Sci. U.S.A. 99:10641-10646(2002). Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-148, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-121 AND ASN-127.	12122212 [Abstract]
"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-623, AND MASSSPECTROMETRY.	19349973 [Abstract]
Phosphorylation
Reference	PubMed
"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-1029, AND MASSSPECTROMETRY.	18083107 [Abstract]