XCT_HUMAN - dbPTM
XCT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XCT_HUMAN
UniProt AC Q9UPY5
Protein Name Cystine/glutamate transporter
Gene Name SLC7A11
Organism Homo sapiens (Human).
Sequence Length 501
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate..
Protein Sequence MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGAGIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGPLPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLNSMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFYYGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLSNAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVRKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRPFKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGFVITLTGVPAYYLFIIWDKKPRWFRIMSEKITRTLQIILEVVPEEDKL
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
4Ubiquitination----MVRKPVVSTIS
----CCCCCEEEEEC
30.6521906983
8PhosphorylationMVRKPVVSTISKGGY
CCCCCEEEEECCCCC
21.9125159151
9PhosphorylationVRKPVVSTISKGGYL
CCCCEEEEECCCCCE
20.0525159151
11PhosphorylationKPVVSTISKGGYLQG
CCEEEEECCCCCEEC
25.9029514088
12UbiquitinationPVVSTISKGGYLQGN
CEEEEECCCCCEECC
53.1323000965
12UbiquitinationPVVSTISKGGYLQGN
CEEEEECCCCCEECC
53.1321890473
12SumoylationPVVSTISKGGYLQGN
CEEEEECCCCCEECC
53.13-
15PhosphorylationSTISKGGYLQGNVNG
EEECCCCCEECCCCC
12.4321945579
26PhosphorylationNVNGRLPSLGNKEPP
CCCCCCCCCCCCCCC
54.2022167270
30UbiquitinationRLPSLGNKEPPGQEK
CCCCCCCCCCCCCHH
70.5621906983
37UbiquitinationKEPPGQEKVQLKRKV
CCCCCCHHHHHHHHH
27.6521906983
41UbiquitinationGQEKVQLKRKVTLLR
CCHHHHHHHHHHHHH
32.8422817900
43UbiquitinationEKVQLKRKVTLLRGV
HHHHHHHHHHHHHCC
37.6723503661
51PhosphorylationVTLLRGVSIIIGTII
HHHHHCCHHHHHHHH
15.76-
222UbiquitinationKGQTQNFKDAFSGRD
CCCCCCHHHHHCCCC
56.5523000965
314N-linked_GlycosylationFSERLLGNFSLAVPI
CCHHHHCCCCCHHHH
24.25UniProtKB CARBOHYD
327S-palmitoylationPIFVALSCFGSMNGG
HHHHHHHCCCCCCCC
4.6929575903
481PhosphorylationPRWFRIMSEKITRTL
CCCHHHHCHHHHHHH
33.1122673903
483UbiquitinationWFRIMSEKITRTLQI
CHHHHCHHHHHHHHH
41.9121906983
500UbiquitinationEVVPEEDKL------
HCCCCCCCC------
60.4229901268

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
26SPhosphorylationKinaseAKT1P31749
PSP
26SPhosphorylationKinaseMTORP42345
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XCT_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 XCT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of XCT_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
DB06151Acetylcysteine
DB00138L-Cystine
DB00740Riluzole
DB01098Rosuvastatin
DB00795Sulfasalazine
DB08834Tauroursodeoxycholic acid
Regulatory Network of XCT_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.
"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-26, AND MASSSPECTROMETRY.
"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-26, AND MASSSPECTROMETRY.

TOP