K1143_HUMAN - dbPTM
K1143_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1143_HUMAN
UniProt AC Q96AT1
Protein Name Uncharacterized protein KIAA1143
Gene Name KIAA1143
Organism Homo sapiens (Human).
Sequence Length 154
Subcellular Localization
Protein Description
Protein Sequence MSKRNQVSYVRPAEPAFLARFKERVGYREGPTVETKRIQPQPPDEDGDHSDKEDEQPQVVVLKKGDLSVEEVMKIKAEIKAAKADEEPTPADGRIIYRKPVKHPSDEKYSGLTASSKKKKPNEDEVNQDSVKKNSQKQIKNSSLLSFDNEDENE
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
2Phosphorylation------MSKRNQVSY
------CCCCCCCCC
40.0826074081
4Methylation----MSKRNQVSYVR
----CCCCCCCCCCC
31.35115481029
8PhosphorylationMSKRNQVSYVRPAEP
CCCCCCCCCCCCCCH
14.2421945579
9PhosphorylationSKRNQVSYVRPAEPA
CCCCCCCCCCCCCHH
11.1321945579
11MethylationRNQVSYVRPAEPAFL
CCCCCCCCCCCHHHH
19.24115481013
20MethylationAEPAFLARFKERVGY
CCHHHHHHHHHHHCC
45.37115481021
32PhosphorylationVGYREGPTVETKRIQ
HCCCCCCCEEEEECC
41.6626074081
35PhosphorylationREGPTVETKRIQPQP
CCCCCEEEEECCCCC
22.6826074081
36AcetylationEGPTVETKRIQPQPP
CCCCEEEEECCCCCC
33.7223749302
36UbiquitinationEGPTVETKRIQPQPP
CCCCEEEEECCCCCC
33.72-
50PhosphorylationPDEDGDHSDKEDEQP
CCCCCCCCCCCCCCC
55.9329255136
68PhosphorylationVLKKGDLSVEEVMKI
EEECCCCCHHHHHHH
32.0221815630
73SulfoxidationDLSVEEVMKIKAEIK
CCCHHHHHHHHHHHH
4.1421406390
105PhosphorylationRKPVKHPSDEKYSGL
ECCCCCCCCCCCCCC
59.1126055452
108AcetylationVKHPSDEKYSGLTAS
CCCCCCCCCCCCCCC
50.1019608861
109PhosphorylationKHPSDEKYSGLTASS
CCCCCCCCCCCCCCC
13.1128796482
110PhosphorylationHPSDEKYSGLTASSK
CCCCCCCCCCCCCCC
38.0928796482
113PhosphorylationDEKYSGLTASSKKKK
CCCCCCCCCCCCCCC
28.1922199227
115PhosphorylationKYSGLTASSKKKKPN
CCCCCCCCCCCCCCC
37.1425159151
116PhosphorylationYSGLTASSKKKKPNE
CCCCCCCCCCCCCCC
46.1323401153
117AcetylationSGLTASSKKKKPNED
CCCCCCCCCCCCCCC
67.1425953088
119AcetylationLTASSKKKKPNEDEV
CCCCCCCCCCCCCCC
76.7530584283
120AcetylationTASSKKKKPNEDEVN
CCCCCCCCCCCCCCC
63.0530584289
130PhosphorylationEDEVNQDSVKKNSQK
CCCCCHHHHHHHHHH
26.5225159151
133AcetylationVNQDSVKKNSQKQIK
CCHHHHHHHHHHHHH
60.7330584295
135PhosphorylationQDSVKKNSQKQIKNS
HHHHHHHHHHHHHHH
47.8626074081
142PhosphorylationSQKQIKNSSLLSFDN
HHHHHHHHHCCCCCC
19.8430266825
143PhosphorylationQKQIKNSSLLSFDNE
HHHHHHHHCCCCCCC
42.6030266825
146PhosphorylationIKNSSLLSFDNEDEN
HHHHHCCCCCCCCCC
35.5325159151

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 K1143_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K1143_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 K1143_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CEP76_HUMANCEP76physical
25416956
CEP76_HUMANCEP76physical
21516116
AQR_HUMANAQRphysical
28514442
CRNL1_HUMANCRNKL1physical
28514442
SYF1_HUMANXAB2physical
28514442
WDR83_HUMANWDR83physical
28514442
ISY1_HUMANISY1physical
28514442
DHX35_HUMANDHX35physical
28514442
BUD31_HUMANBUD31physical
28514442
ECD_HUMANECDphysical
28514442
PRP17_HUMANCDC40physical
28514442
GPTC1_HUMANGPATCH1physical
28514442
U520_HUMANSNRNP200physical
28514442
EAPP_HUMANEAPPphysical
28514442
PPIE_HUMANPPIEphysical
28514442
PRP8_HUMANPRPF8physical
28514442
PAXB1_HUMANPAXBP1physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
RBM22_HUMANRBM22physical
28514442
CCD12_HUMANCCDC12physical
28514442
ZNHI2_HUMANZNHIT2physical
28514442
PRP6_HUMANPRPF6physical
28514442
SNW1_HUMANSNW1physical
28514442
AAR2_HUMANAAR2physical
28514442
BTBD9_HUMANBTBD9physical
28514442

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 K1143_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-146, AND MASSSPECTROMETRY.
"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 SER-143 AND SER-146, ANDMASS SPECTROMETRY.
"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-50 AND SER-146, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-130, 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-50 AND SER-146, AND MASSSPECTROMETRY.

TOP