K0930_HUMAN - dbPTM
K0930_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K0930_HUMAN
UniProt AC Q6ICG6
Protein Name Uncharacterized protein KIAA0930
Gene Name KIAA0930
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization
Protein Description
Protein Sequence MLRAIAEERGRLSLRREVCGLGCFKDDRIVFWTWMFSTYFMEKWAPRQDDMLFYVRRKLAYSGSESGADGRKAAEPEVEVEVYRRDSKKLPGLGDPDIDWEESVCLNLILQKLDYMVTCAVCTRADGGDIHIHKKKSQQVFASPSKHPMDSKGEESKISYPNIFFMIDSFEEVFSDMTVGEGEMVCVELVASDKTNTFQGVIFQGSIRYEALKKVYDNRVSVAARMAQKMSFGFYKYSNMEFVRMKGPQGKGHAEMAVSRVSTGDTSPCGTEEDSSPASPMHERVTSFSTPPTPERNNRPAFFSPSLKRKVPRNRIAEMKKSHSANDSEEFFREDDGGADLHNATNLRSRSLSGTGRSLVGSWLKLNRADGNFLLYAHLTYVTLPLHRILTDILEVRQKPILMT
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
13PhosphorylationAEERGRLSLRREVCG
HHHHCCHHHCHHHHC		20.6123532336
33PhosphorylationDDRIVFWTWMFSTYF
CCCEEEEHHHHHHHH		8.7923401153
37PhosphorylationVFWTWMFSTYFMEKW
EEEHHHHHHHHHHHH		13.1923401153
38PhosphorylationFWTWMFSTYFMEKWA
EEHHHHHHHHHHHHC		14.9823401153
39PhosphorylationWTWMFSTYFMEKWAP
EHHHHHHHHHHHHCC		10.3423401153
61PhosphorylationYVRRKLAYSGSESGA
EHHHHHHHCCCCCCC		24.81-
62PhosphorylationVRRKLAYSGSESGAD
HHHHHHHCCCCCCCC		30.18-
143PhosphorylationKSQQVFASPSKHPMD
CCCCEECCCCCCCCC		20.4525627689
221PhosphorylationKVYDNRVSVAARMAQ
HHHCCHHHHHHHHHH		11.6429978859
231PhosphorylationARMAQKMSFGFYKYS
HHHHHHCCCEEEEEC		29.2928555341
259PhosphorylationGHAEMAVSRVSTGDT
CCCEEEEEEEECCCC		19.8926074081
262PhosphorylationEMAVSRVSTGDTSPC
EEEEEEEECCCCCCC		26.0923927012
263PhosphorylationMAVSRVSTGDTSPCG
EEEEEEECCCCCCCC		35.9023927012
266PhosphorylationSRVSTGDTSPCGTEE
EEEECCCCCCCCCCC		35.5923927012
267PhosphorylationRVSTGDTSPCGTEED
EEECCCCCCCCCCCC		23.9625159151
271PhosphorylationGDTSPCGTEEDSSPA
CCCCCCCCCCCCCCC		42.8123927012
272PhosphorylationDTSPCGTEEDSSPAS
CCCCCCCCCCCCCCC		45.1224719451
275PhosphorylationPCGTEEDSSPASPMH
CCCCCCCCCCCCCCC		41.3129255136
276PhosphorylationCGTEEDSSPASPMHE
CCCCCCCCCCCCCCH		36.4929255136
279PhosphorylationEEDSSPASPMHERVT
CCCCCCCCCCCHHHC		26.5823401153
284PhosphorylationPASPMHERVTSFSTP
CCCCCCHHHCCCCCC		23.4924719451
286PhosphorylationSPMHERVTSFSTPPT
CCCCHHHCCCCCCCC		30.2129255136
287PhosphorylationPMHERVTSFSTPPTP
CCCHHHCCCCCCCCC		17.8429255136
289PhosphorylationHERVTSFSTPPTPER
CHHHCCCCCCCCCCC		39.5123401153
290PhosphorylationERVTSFSTPPTPERN
HHHCCCCCCCCCCCC		31.1430266825
291PhosphorylationRVTSFSTPPTPERNN
HHCCCCCCCCCCCCC		29.5724719451
292PhosphorylationVTSFSTPPTPERNNR
HCCCCCCCCCCCCCC		61.7527251275
293PhosphorylationTSFSTPPTPERNNRP
CCCCCCCCCCCCCCC		38.7023401153
294PhosphorylationSFSTPPTPERNNRPA
CCCCCCCCCCCCCCC		44.3024719451
295PhosphorylationFSTPPTPERNNRPAF
CCCCCCCCCCCCCCC		71.2024719451
298PhosphorylationPPTPERNNRPAFFSP
CCCCCCCCCCCCCCH		58.4924719451
304PhosphorylationNNRPAFFSPSLKRKV
CCCCCCCCHHHHCCC		13.7119664994
304O-linked_GlycosylationNNRPAFFSPSLKRKV
CCCCCCCCHHHHCCC		13.7130379171
306PhosphorylationRPAFFSPSLKRKVPR
CCCCCCHHHHCCCCH		45.3729255136
309PhosphorylationFFSPSLKRKVPRNRI
CCCHHHHCCCCHHHH		50.9624719451
311PhosphorylationSPSLKRKVPRNRIAE
CHHHHCCCCHHHHHH		6.6424719451
322PhosphorylationRIAEMKKSHSANDSE
HHHHHHHHCCCCCHH		19.7030266825
324PhosphorylationAEMKKSHSANDSEEF
HHHHHHCCCCCHHHH		35.5429255136
328PhosphorylationKSHSANDSEEFFRED
HHCCCCCHHHHHCCC		38.5430266825
329PhosphorylationSHSANDSEEFFREDD
HCCCCCHHHHHCCCC		62.7824719451
331 (in isoform 3)Ubiquitination-6.5021890473
345PhosphorylationGADLHNATNLRSRSL
CCCCCCCCCCCCCCC		39.8520873877
349O-linked_GlycosylationHNATNLRSRSLSGTG
CCCCCCCCCCCCCCC		29.4130379171
349PhosphorylationHNATNLRSRSLSGTG
CCCCCCCCCCCCCCC		29.4120363803
351PhosphorylationATNLRSRSLSGTGRS
CCCCCCCCCCCCCHH		28.2928176443
353PhosphorylationNLRSRSLSGTGRSLV
CCCCCCCCCCCHHHH		35.2428176443
353O-linked_GlycosylationNLRSRSLSGTGRSLV
CCCCCCCCCCCHHHH		35.2430379171
355PhosphorylationRSRSLSGTGRSLVGS
CCCCCCCCCHHHHHH		26.5028176443
356PhosphorylationSRSLSGTGRSLVGSW
CCCCCCCCHHHHHHH		22.2427251275
358PhosphorylationSLSGTGRSLVGSWLK
CCCCCCHHHHHHHEE		28.8430266825
362PhosphorylationTGRSLVGSWLKLNRA
CCHHHHHHHEEEECC		23.0423401153
363PhosphorylationGRSLVGSWLKLNRAD
CHHHHHHHEEEECCC		7.5027251275
365UbiquitinationSLVGSWLKLNRADGN
HHHHHHEEEECCCCC		37.142189047
365 (in isoform 1)Ubiquitination-37.1421890473
367PhosphorylationVGSWLKLNRADGNFL
HHHHEEEECCCCCEE		35.1924719451
370 (in isoform 2)Ubiquitination-49.7021890473
376PhosphorylationADGNFLLYAHLTYVT
CCCCEEEEEEEEEEE		8.3024719451
381PhosphorylationLLYAHLTYVTLPLHR
EEEEEEEEEEHHHHH		9.5924719451
383PhosphorylationYAHLTYVTLPLHRIL
EEEEEEEEHHHHHHH		16.5524719451
388PhosphorylationYVTLPLHRILTDILE
EEEHHHHHHHHHHHH		33.0424719451
404PhosphorylationRQKPILMT-------
HCCCCCCC-------		31.8221712546
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 K0930_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K0930_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 K0930_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
1433T_HUMANYWHAQphysical
26186194
1433B_HUMANYWHABphysical
26186194
1433S_HUMANSFNphysical
26186194
1433G_HUMANYWHAGphysical
26186194
1433E_HUMANYWHAEphysical
26186194
1433Z_HUMANYWHAZphysical
26186194
1433F_HUMANYWHAHphysical
26186194
KLH11_HUMANKLHL11physical
26186194
FRYL_HUMANFRYLphysical
26186194
ATG7_HUMANATG7physical
26186194
WRN_HUMANWRNphysical
26186194
CK5P1_HUMANCDK5RAP1physical
28514442
KLH11_HUMANKLHL11physical
28514442
1433Z_HUMANYWHAZphysical
28514442
1433G_HUMANYWHAGphysical
28514442
1433E_HUMANYWHAEphysical
28514442
1433B_HUMANYWHABphysical
28514442
1433T_HUMANYWHAQphysical
28514442
1433F_HUMANYWHAHphysical
28514442
WRN_HUMANWRNphysical
28514442
1433S_HUMANSFNphysical
28514442
ATG7_HUMANATG7physical
28514442
FRYL_HUMANFRYLphysical
28514442
SIR2_HUMANSIRT2physical
28514442
RAB3I_HUMANRAB3IPphysical
27173435
CBY1_HUMANCBY1physical
27173435
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 K0930_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-279 AND THR-293, ANDMASS 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 SER-267; THR-271; SER-275;SER-289 AND THR-293, AND MASS 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 THR-290; THR-293 ANDSER-324, AND MASS SPECTROMETRY.

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