dbPTM

ATRN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATRN_HUMAN
UniProt AC	O75882
Protein Name	Attractin
Gene Name	ATRN
Organism	Homo sapiens (Human).
Sequence Length	1429
Subcellular Localization	Isoform 1: Cell membrane Single-pass type I membrane protein . Isoform 2: Secreted . Isoform 3: Secreted .
Protein Description	Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines. May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system (By similarity)..
Protein Sequence	MVAAAAATEARLRRRTAATAALAGRSGGPHWDWDVTRAGRPGLGAGLRLPRLLSPPLRPRLLLLLLLLSPPLLLLLLPCEAEAAAAAAAVSGSAAAEAKECDRPCVNGGRCNPGTGQCVCPAGWVGEQCQHCGGRFRLTGSSGFVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATECSWDHLYVYDGDSIYAPLVAAFSGLIVPERDGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSFDMCPNNCSGRGECKISNSSDTVECECSENWKGEACDIPHCTDNCGFPHRGICNSSDVRGCSCFSDWQGPGCSVPVPANQSFWTREEYSNLKLPRASHKAVVNGNIMWVVGGYMFNHSDYNMVLAYDLASREWLPLNRSVNNVVVRYGHSLALYKDKIYMYGGKIDSTGNVTNELRVFHIHNESWVLLTPKAKEQYAVVGHSAHIVTLKNGRVVMLVIFGHCPLYGYISNVQEYDLDKNTWSILHTQGALVQGGYGHSSVYDHRTRALYVHGGYKAFSANKYRLADDLYRYDVDTQMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTSMSHGAKCFSSDFMAYDIACDRWSVLPRPDLHHDVNRFGHSAVLHNSTMYVFGGFNSLLLSDILVFTSEQCDAHRSEAACLAAGPGIRCVWNTGSSQCISWALATDEQEEKLKSECFSKRTLDHDRCDQHTDCYSCTANTNDCHWCNDHCVPRNHSCSEGQISIFRYENCPKDNPMYYCNKKTSCRSCALDQNCQWEPRNQECIALPENICGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSQSMSKLTLTPWVGLRKINVSYWCWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCERPANHSAKQCRTPCALRTACGDCTSGSSECMWCSNMKQCVDSNAYVASFPFGQCMEWYTMSTCPPENCSGYCTCSHCLEQPGCGWCTDPSNTGKGKCIEGSYKGPVKMPSQAPTGNFYPQPLLNSSMCLEDSRYNWSFIHCPACQCNGHSKCINQSICEKCENLTTGKHCETCISGFYGDPTNGGKCQPCKCNGHASLCNTNTGKCFCTTKGVKGDECQLCEVENRYQGNPLRGTCYYTLLIDYQFTFSLSQEDDRYYTAINFVATPDEQNRDLDMFINASKNFNLNITWAASFSAGTQAGEEMPVVSKTNIKEYKDSFSNEKFDFRNHPNITFFVYVSNFTWPIKIQIAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCWASRRREQLLREMQQMASRPFASVNVALETDEEPPDLIGGSIKTVPKPIALEPCFGNKAAVLSVFVRLPRGLGGIPPPGQSGLAVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	PHWDWDVTRAGRPGL CCCCCCCCCCCCCCC	16.60	-
141	Phosphorylation	GRFRLTGSSGFVTDG CCEEEECCCCEEECC	23.27	24667141
142	Phosphorylation	RFRLTGSSGFVTDGP CEEEECCCCEEECCC	37.28	24667141
154	Phosphorylation	DGPGNYKYKTKCTWL CCCCCEEEEEEEEEE	17.33	26657352
156	Phosphorylation	PGNYKYKTKCTWLIE CCCEEEEEEEEEEEC	28.41	26657352
159	Phosphorylation	YKYKTKCTWLIEGQP EEEEEEEEEEECCCC	25.51	26657352
213	N-linked_Glycosylation	IVPERDGNETVPEVV EECCCCCCCCCCHHH	46.16	UniProtKB CARBOHYD
237	N-linked_Glycosylation	FFSDAAYNLTGFNIT HHHCHHHCCCCCEEE	26.80	UniProtKB CARBOHYD
242	N-linked_Glycosylation	AYNLTGFNITYSFDM HHCCCCCEEEEEEEC	27.34	UniProtKB CARBOHYD
253	N-linked_Glycosylation	SFDMCPNNCSGRGEC EEECCCCCCCCCCEE	13.38	UniProtKB CARBOHYD
264 (in isoform 3)	Ubiquitination	-	49.35	21890473
264	N-linked_Glycosylation	RGECKISNSSDTVEC CCEEEECCCCCCEEE	49.35	18638581
264	N-linked_Glycosylation	RGECKISNSSDTVEC CCEEEECCCCCCEEE	49.35	16335952
300	N-linked_Glycosylation	FPHRGICNSSDVRGC CCCCCCCCCCCCCCC	42.50	16335952
325	N-linked_Glycosylation	CSVPVPANQSFWTRE CCCCCCCCCCCCCHH	31.77	UniProtKB CARBOHYD
338 (in isoform 2)	Ubiquitination	-	61.77	21890473
338 (in isoform 1)	Ubiquitination	-	61.77	21890473
338	Ubiquitination	REEYSNLKLPRASHK HHHHCCCCCCCCCCE	61.77	21890473
362	N-linked_Glycosylation	VVGGYMFNHSDYNMV EECCEECCCCCCCEE	19.75	UniProtKB CARBOHYD
383	N-linked_Glycosylation	SREWLPLNRSVNNVV CCCCCCCCCCCCCEE	32.04	19139490
383	N-linked_Glycosylation	SREWLPLNRSVNNVV CCCCCCCCCCCCCEE	32.04	16335952
405	Phosphorylation	ALYKDKIYMYGGKID EEECCEEEEECCEEC	7.04	29759185
407	Phosphorylation	YKDKIYMYGGKIDST ECCEEEEECCEECCC	13.02	29759185
416	N-linked_Glycosylation	GKIDSTGNVTNELRV CEECCCCCCCCEEEE	37.21	18638581
428	N-linked_Glycosylation	LRVFHIHNESWVLLT EEEEEEECCEEEEEC	44.38	16335952
492	Phosphorylation	NTWSILHTQGALVQG CCEEEEECCCCEECC	25.83	24114839
501	Phosphorylation	GALVQGGYGHSSVYD CCEECCCCCCCCHHC	20.63	24114839
505	Phosphorylation	QGGYGHSSVYDHRTR CCCCCCCCHHCCCCC	21.01	24114839
537	Phosphorylation	LADDLYRYDVDTQMW ECCCEECCCCCHHHH	13.53	22817900
555	Phosphorylation	KDSRFFRYLHTAVIV HCCHHHHHHCEEEEE	9.55	-
558	Phosphorylation	RFFRYLHTAVIVSGT HHHHHHCEEEEEECC	21.74	-
565	Phosphorylation	TAVIVSGTMLVFGGN EEEEEECCEEEECCC	10.38	-
575	N-linked_Glycosylation	VFGGNTHNDTSMSHG EECCCCCCCCCHHHC	52.82	16335952
623	N-linked_Glycosylation	GHSAVLHNSTMYVFG CCCEECCCCCEEEEC	34.71	16335952
731	N-linked_Glycosylation	NDHCVPRNHSCSEGQ CCCCCCCCCCCCCCC	25.92	17623646
731	N-linked_Glycosylation	NDHCVPRNHSCSEGQ CCCCCCCCCCCCCCC	25.92	17623646
749	Ubiquitination	FRYENCPKDNPMYYC EEEECCCCCCCCEEC	72.79	-
806	Ubiquitination	CLKITTAKENYDNAK EEEEEECHHHCCCCE	44.38	-
813	Ubiquitination	KENYDNAKLFCRNHN HHHCCCCEEEECCHH	48.64	-
825	Phosphorylation	NHNALLASLTTQKKV CHHHHHHHHCCHHHH	26.64	26074081
827	Phosphorylation	NALLASLTTQKKVEF HHHHHHHCCHHHHHH	25.37	26074081
828	Phosphorylation	ALLASLTTQKKVEFV HHHHHHCCHHHHHHH	43.62	26074081
849	Phosphorylation	MQSSQSMSKLTLTPW HHCCCCCCCCCCCCC	29.75	30576142
863	N-linked_Glycosylation	WVGLRKINVSYWCWE CCCCCCCEEEEEECC	21.51	UniProtKB CARBOHYD
908	Phosphorylation	TRGLKAATCINPLNG CCCCCHHHCCCCCCC	20.83	-
914	N-linked_Glycosylation	ATCINPLNGSVCERP HHCCCCCCCCCCCCC	41.78	18638581
914	N-linked_Glycosylation	ATCINPLNGSVCERP HHCCCCCCCCCCCCC	41.78	17623646
916	Phosphorylation	CINPLNGSVCERPAN CCCCCCCCCCCCCCC	23.63	-
923	N-linked_Glycosylation	SVCERPANHSAKQCR CCCCCCCCCCCCCCC	32.12	18638581
937	Phosphorylation	RTPCALRTACGDCTS CCCCHHHCCCCCCCC	27.44	24114839
944	Phosphorylation	TACGDCTSGSSECMW CCCCCCCCCCCCCCE	42.90	24114839
953	Phosphorylation	SSECMWCSNMKQCVD CCCCCEECCCHHHCC	25.17	24114839
986	N-linked_Glycosylation	MSTCPPENCSGYCTC CCCCCCCCCCCEECC	30.91	UniProtKB CARBOHYD
1043	N-linked_Glycosylation	FYPQPLLNSSMCLED CCCCCCCCCCCCCCC	39.46	16335952
1054	N-linked_Glycosylation	CLEDSRYNWSFIHCP CCCCCCCCEEEEECC	27.14	UniProtKB CARBOHYD
1073	N-linked_Glycosylation	NGHSKCINQSICEKC CCCHHHCCHHHHHHC	38.73	17623646
1073	N-linked_Glycosylation	NGHSKCINQSICEKC CCCHHHCCHHHHHHC	38.73	17623646
1082	N-linked_Glycosylation	SICEKCENLTTGKHC HHHHHCCCCCCCCCC	52.75	UniProtKB CARBOHYD
1146	Phosphorylation	LCEVENRYQGNPLRG EEEEEECCCCCCCCC	32.14	23879269
1154	Phosphorylation	QGNPLRGTCYYTLLI CCCCCCCCEEEEEEE	7.30	23879269
1185	Phosphorylation	TAINFVATPDEQNRD EEEEEEECCCCCCCC	26.43	18452278
1198	N-linked_Glycosylation	RDLDMFINASKNFNL CCHHEEEEECCCCCE	27.22	17623646
1198	N-linked_Glycosylation	RDLDMFINASKNFNL CCHHEEEEECCCCCE	27.22	16335952
1206	N-linked_Glycosylation	ASKNFNLNITWAASF ECCCCCEEEEEEEEE	30.65	UniProtKB CARBOHYD
1250	N-linked_Glycosylation	FDFRNHPNITFFVYV CCCCCCCCEEEEEEE	38.08	16335952
1259	N-linked_Glycosylation	TFFVYVSNFTWPIKI EEEEEEECCCCCEEE	28.46	16335952
1365	Methylation	LEPCFGNKAAVLSVF EEECCCCCHHHHHHE	37.79	-
1370	Phosphorylation	GNKAAVLSVFVRLPR CCCHHHHHHEEECCC	13.60	23403867
1418	Ubiquitination	SGAVRNRKQQPPAQP CCCCCCCCCCCCCCC	57.76	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO6	Q9NRD1	PMID:24658274

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ATRN_HUMAN !!

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 ATRN_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-416, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-264; ASN-300; ASN-383;ASN-416; ASN-428; ASN-575; ASN-623; ASN-1043; ASN-1198; ASN-1250 ANDASN-1259, AND MASS SPECTROMETRY.	16335952 [Abstract]
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-264; ASN-383 AND ASN-731,AND MASS SPECTROMETRY.	14760718 [Abstract]