XPR1_HUMAN - dbPTM
XPR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPR1_HUMAN
UniProt AC Q9UBH6
Protein Name Xenotropic and polytropic retrovirus receptor 1
Gene Name XPR1
Organism Homo sapiens (Human).
Sequence Length 696
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. [PubMed: 23791524]
Protein Sequence MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQKESTGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVAHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVLAAVFKLETDRSIWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFAPISVIPTYVYPLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSLELKWDESKGLLPNNSEESGICHKYTYGVRAIVQCIPAWLRFIQCLRRYRDTKRAFPHLVNAGKYSTTFFMVTFAALYSTHKERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQDDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT
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
48 (in isoform 2)Ubiquitination-43.4021890473
48 (in isoform 1)Ubiquitination-43.4021890473
48UbiquitinationVTDEDTVKRYFAKFE
CCCHHHHHHHHHHHH
43.4021906983
50PhosphorylationDEDTVKRYFAKFEEK
CHHHHHHHHHHHHHH
11.3718212344
57UbiquitinationYFAKFEEKFFQTCEK
HHHHHHHHHHHHHHH
44.26-
64UbiquitinationKFFQTCEKELAKINT
HHHHHHHHHHHHHHH
61.24-
76 (in isoform 2)Ubiquitination-47.2421890473
76 (in isoform 1)Ubiquitination-47.2421890473
76UbiquitinationINTFYSEKLAEAQRR
HHHHHHHHHHHHHHH
47.2421906983
99UbiquitinationQSSLDAQKESTGVTT
HHHHHHHHHHHCCCH
56.18-
99 (in isoform 2)Ubiquitination-56.18-
102PhosphorylationLDAQKESTGVTTLRQ
HHHHHHHHCCCHHHH
36.4429255136
105PhosphorylationQKESTGVTTLRQRRK
HHHHHCCCHHHHHCC
22.8129255136
106PhosphorylationKESTGVTTLRQRRKP
HHHHCCCHHHHHCCC
19.9629255136
162UbiquitinationGFRKILKKHDKILET
CHHHHHHHCHHHHHH
54.30-
165UbiquitinationKILKKHDKILETSRG
HHHHHCHHHHHHCCC
49.24-
273MethylationWPLIRIYRGGFLLIE
HHHHHHHHCCCHHHH
36.0724377067
273DimethylationWPLIRIYRGGFLLIE
HHHHHHHHCCCHHHH
36.07-
474 (in isoform 2)Ubiquitination-4.56-
483PhosphorylationHLVNAGKYSTTFFMV
HHHHCCCCCCHHHHH
15.44-
498PhosphorylationTFAALYSTHKERGHS
HHHHHHHHHHHCCCC
24.34-
539UbiquitinationMDWGLFDKNAGENTF
CCCCCCCCCCCCCCE
41.17-
574PhosphorylationVILRFAWTIQISITS
HHHHHHEEEEEEEEE
10.28-
594PhosphorylationHSGDIIATVFAPLEV
CCCCEEEEEECCHHH
13.02-
597 (in isoform 2)Ubiquitination-11.9321890473
619 (in isoform 2)Ubiquitination-41.3421890473
660PhosphorylationRNRQKNRSWKYNQSI
HHHHHHHCCCCCCCC
37.0019581576
662UbiquitinationRQKNRSWKYNQSISL
HHHHHCCCCCCCCCC
35.2521890473
662 (in isoform 1)Ubiquitination-35.2521890473
663PhosphorylationQKNRSWKYNQSISLR
HHHHCCCCCCCCCCC
16.5122167270
666PhosphorylationRSWKYNQSISLRRPR
HCCCCCCCCCCCCCC
15.5422167270
668PhosphorylationWKYNQSISLRRPRLA
CCCCCCCCCCCCCHH
22.5222167270
676PhosphorylationLRRPRLASQSKARDT
CCCCCHHCCCCCCCC
39.3126074081
678PhosphorylationRPRLASQSKARDTKV
CCCHHCCCCCCCCEE
26.2826074081
684UbiquitinationQSKARDTKVLIEDTD
CCCCCCCEEEEECCC
39.062190698
684 (in isoform 1)Ubiquitination-39.0621890473
690PhosphorylationTKVLIEDTDDEANT-
CEEEEECCCCCCCC-
32.3430266825
696PhosphorylationDTDDEANT-------
CCCCCCCC-------
47.2230266825

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 XPR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPR1_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 XPR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDIS_HUMANKIDINS220physical
28514442
B3A2_HUMANSLC4A2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616413Basal ganglia calcification, idiopathic, 6 (IBGC6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XPR1_HUMAN

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Related Literatures of Post-Translational Modification
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-668 AND THR-690, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-668 ANDTHR-690, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-690, AND MASSSPECTROMETRY.

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