K1958_HUMAN - dbPTM
K1958_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1958_HUMAN
UniProt AC Q8N8K9
Protein Name Uncharacterized protein KIAA1958
Gene Name KIAA1958
Organism Homo sapiens (Human).
Sequence Length 716
Subcellular Localization
Protein Description
Protein Sequence MEDCLHTSSENLSKLVSWAHSHGTICSLIPNLKHLLSEGSHGNLTAMWGCSAGHAYHWPLTATCRAGSQERVCFQDNRSFNSDSPSIIGVPSETQTSPVERYPGRPVKAKLDCNRTRDSCDFSYCSEPSELDETVEEYEDENTLFDMVCESSVTDEDSDFEPQTQRPQSIARKRPGVVPSSLHSSSQTQMVDECSNDVIIKKIKQEIPEDYYIVANAELTGGVDGPALSLTQMAKPKPQTHAGPSCVGSAKLIPHVTSAISTELDPHGMSASPSVISRPIVQKTARVSLASPNRGPPGTHGTNQQVAMQMPVSTSHPNKQISIPLSALQLPGQDEQVASEEFLSHLPSQVSSCEVALSPSVNTEPEVSSSQQQPPVAPAITTEATAQCIPAYSTKLNKFPVFNINDDLNDLCTSAVSPNTTKATRYALNVWRYWCMTNGLKDHTDITKIPAVKLNELLENFYVTVKKSDGSDFLATSLHAIRRGLDRILKNAGVGFSITSSTFSSSTKKLKEKLWVLSKAGMSGARSRNIVYFSLSDEEEMWQAGCLGDDSPITLLSTVVKYNSQYLNMRTLQEHADLMYGDIELLKDPQNQPYFARTDSVKRESRSGSTRVCHGKIYHEHSRGHKQCPYCLLYKYMYIHRPPTQMEAKSPFYLTARKEATDMGSVWYEEQRMGLRSLRGIVPNLAKKVKLENCENFTFVSFTQVSRRLGSHSCCQ
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
68PhosphorylationTATCRAGSQERVCFQ
EEEECCCCCCEEEEE		28.0820363803
79PhosphorylationVCFQDNRSFNSDSPS
EEEECCCCCCCCCCC		34.7326074081
82PhosphorylationQDNRSFNSDSPSIIG
ECCCCCCCCCCCEEC		37.1426074081
84PhosphorylationNRSFNSDSPSIIGVP
CCCCCCCCCCEECCC		21.9926074081
86PhosphorylationSFNSDSPSIIGVPSE
CCCCCCCCEECCCCC		30.6926074081
92PhosphorylationPSIIGVPSETQTSPV
CCEECCCCCCCCCCC		51.3625850435
94PhosphorylationIIGVPSETQTSPVER
EECCCCCCCCCCCCC		41.2923898821
96PhosphorylationGVPSETQTSPVERYP
CCCCCCCCCCCCCCC		42.2823898821
97PhosphorylationVPSETQTSPVERYPG
CCCCCCCCCCCCCCC		19.6821082442
102PhosphorylationQTSPVERYPGRPVKA
CCCCCCCCCCCCCEE		9.1323312004
173UbiquitinationRPQSIARKRPGVVPS
CCHHHHHHCCCCCCH		54.6529967540
180PhosphorylationKRPGVVPSSLHSSSQ
HCCCCCCHHCCCCCC		33.6429449344
181PhosphorylationRPGVVPSSLHSSSQT
CCCCCCHHCCCCCCC		24.8329449344
184PhosphorylationVVPSSLHSSSQTQMV
CCCHHCCCCCCCHHH		36.6629449344
185PhosphorylationVPSSLHSSSQTQMVD
CCHHCCCCCCCHHHH		18.7329449344
186PhosphorylationPSSLHSSSQTQMVDE
CHHCCCCCCCHHHHH		40.0229449344
188PhosphorylationSLHSSSQTQMVDECS
HCCCCCCCHHHHHCC		22.1529449344
195PhosphorylationTQMVDECSNDVIIKK
CHHHHHCCCCHHHHH		33.7329449344
201SumoylationCSNDVIIKKIKQEIP
CCCCHHHHHHHHHCC		37.0028112733
204SumoylationDVIIKKIKQEIPEDY
CHHHHHHHHHCCCCE		51.2428112733
237SumoylationLTQMAKPKPQTHAGP
HHHHCCCCCCCCCCC		49.3928112733
240PhosphorylationMAKPKPQTHAGPSCV
HCCCCCCCCCCCCCC		23.4028450419
245PhosphorylationPQTHAGPSCVGSAKL
CCCCCCCCCCCHHHH		22.1028122231
245 (in isoform 2)Phosphorylation-22.1021406692
249PhosphorylationAGPSCVGSAKLIPHV
CCCCCCCHHHHHHHH		11.2228450419
270PhosphorylationELDPHGMSASPSVIS
CCCCCCCCCCHHHHC		30.1325159151
272PhosphorylationDPHGMSASPSVISRP
CCCCCCCCHHHHCCH		15.4825159151
274PhosphorylationHGMSASPSVISRPIV
CCCCCCHHHHCCHHE		29.5926714015
283SumoylationISRPIVQKTARVSLA
HCCHHEECEEEEEEC		33.0028112733
283UbiquitinationISRPIVQKTARVSLA
HCCHHEECEEEEEEC		33.0029967540
288 (in isoform 2)Phosphorylation-16.8021406692
288PhosphorylationVQKTARVSLASPNRG
EECEEEEEECCCCCC		16.8025159151
291 (in isoform 2)Phosphorylation-28.1821406692
291PhosphorylationTARVSLASPNRGPPG
EEEEEECCCCCCCCC		28.1821815630
299PhosphorylationPNRGPPGTHGTNQQV
CCCCCCCCCCCCCCE		23.9428464451
302PhosphorylationGPPGTHGTNQQVAMQ
CCCCCCCCCCCEEEE		23.4221406692
313PhosphorylationVAMQMPVSTSHPNKQ
EEEECCCCCCCCCCE		20.5121406692
314 (in isoform 2)Phosphorylation-31.1521406692
314PhosphorylationAMQMPVSTSHPNKQI
EEECCCCCCCCCCEE		31.1521406692
315PhosphorylationMQMPVSTSHPNKQIS
EECCCCCCCCCCEEE		29.4621406692
398UbiquitinationAYSTKLNKFPVFNIN
CCCCCCCCCCCEECC		62.57-
422UbiquitinationAVSPNTTKATRYALN
CCCCCCHHHHHHHHH		45.80-
426UbiquitinationNTTKATRYALNVWRY
CCHHHHHHHHHHHHH		15.8729967540
426UbiquitinationNTTKATRYALNVWRY
CCHHHHHHHHHHHHH		15.87-
426PhosphorylationNTTKATRYALNVWRY
CCHHHHHHHHHHHHH		15.8730576142
437PhosphorylationVWRYWCMTNGLKDHT
HHHHHHHHCCCCCCC		24.0130576142
448UbiquitinationKDHTDITKIPAVKLN
CCCCCCCCCCCCCHH		47.2129967540
450UbiquitinationHTDITKIPAVKLNEL
CCCCCCCCCCCHHHH		32.34-
458 (in isoform 2)Phosphorylation-4.0522210691
460 (in isoform 2)Phosphorylation-33.2522210691
466UbiquitinationENFYVTVKKSDGSDF
HHEEEEEECCCCCCH		36.8729967540
475 (in isoform 2)Phosphorylation-8.6422210691
476UbiquitinationDGSDFLATSLHAIRR
CCCCHHHHHHHHHHH		33.6929967540
494UbiquitinationRILKNAGVGFSITSS
HHHHHCCCCEEEECC		6.9429967540
497PhosphorylationKNAGVGFSITSSTFS
HHCCCCEEEECCCCC		21.0126074081
499PhosphorylationAGVGFSITSSTFSSS
CCCCEEEECCCCCCC		18.5426074081
500PhosphorylationGVGFSITSSTFSSST
CCCEEEECCCCCCCC		26.2226074081
501PhosphorylationVGFSITSSTFSSSTK
CCEEEECCCCCCCCH		25.4826074081
502PhosphorylationGFSITSSTFSSSTKK
CEEEECCCCCCCCHH		27.5726074081
504PhosphorylationSITSSTFSSSTKKLK
EEECCCCCCCCHHHH		24.3826074081
505PhosphorylationITSSTFSSSTKKLKE
EECCCCCCCCHHHHH		37.5226074081
506PhosphorylationTSSTFSSSTKKLKEK
ECCCCCCCCHHHHHH		42.9426074081
507PhosphorylationSSTFSSSTKKLKEKL
CCCCCCCCHHHHHHH		33.8626074081
558PhosphorylationSPITLLSTVVKYNSQ
CCCHHHHHHHHHCHH		29.32-
587UbiquitinationYGDIELLKDPQNQPY
HCCHHHCCCCCCCCC		78.8429967540
615UbiquitinationGSTRVCHGKIYHEHS
CCCCEECCEECCCCC		16.9629967540
616UbiquitinationSTRVCHGKIYHEHSR
CCCEECCEECCCCCC		19.2029967540
621 (in isoform 2)Ubiquitination-14.96-
626SumoylationHEHSRGHKQCPYCLL
CCCCCCCCCCCHHHH		57.3228112733
644UbiquitinationMYIHRPPTQMEAKSP
HHCCCCCCCCCCCCC		43.1429967540
649UbiquitinationPPTQMEAKSPFYLTA
CCCCCCCCCCEEEEE		45.41-
658UbiquitinationPFYLTARKEATDMGS
CEEEEECCCCCCCCC		49.60-
665PhosphorylationKEATDMGSVWYEEQR
CCCCCCCCCHHHHHH		11.6628509920
677UbiquitinationEQRMGLRSLRGIVPN
HHHHCHHHHHCCCCC		27.71-
686UbiquitinationRGIVPNLAKKVKLEN
HCCCCCHHHHCCCCC		19.10-
716UbiquitinationLGSHSCCQ-------
HCCCCCCC-------		61.75-
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 K1958_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K1958_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 K1958_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1958_HUMANKIAA1958physical
25416956
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 K1958_HUMAN

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Related Literatures of Post-Translational Modification
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-97, 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-245, 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-68, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.

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