KIRR1_HUMAN - dbPTM
KIRR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIRR1_HUMAN
UniProt AC Q96J84
Protein Name Kin of IRRE-like protein 1
Gene Name KIRREL1 {ECO:0000312|HGNC:HGNC:15734}
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Predominantly located at podocyte slit diaphragm.
Protein Description Plays a significant role in the normal development and function of the glomerular permeability. Signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity)..
Protein Sequence MLSLLVWILTLSDTFSQGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEDTRIDGGPVILLQAGTPHNLTCRAFNAKPAATIIWFRDGTQQEGAVASTELLKDGKRETTVSQLLINPTDLDIGRVFTCRSMNEAIPSGKETSIELDVHHPPTVTLSIEPQTVQEGERVVFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVHNKVGSTNVSTLVNVHFAPRIVVDPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQYAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGASILLIFFFIALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASVSTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPARFDGRPSSRLSHSSGYAQLNTYSRGPASDYGPEPTPPGPAAPAGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV
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
31PhosphorylationSQEPADQTVVAGQRA
CCCCCCCEEECCCCC		19.9320044836
46N-linked_GlycosylationVLPCVLLNYSGIVQW
HHEEEEECCCCCEEE		25.43UniProtKB CARBOHYD
140N-linked_GlycosylationLQAGTPHNLTCRAFN
EECCCCCCCEEECCC		37.94UniProtKB CARBOHYD
199PhosphorylationLDIGRVFTCRSMNEA
CCCCCEEEECCHHCC		12.2624702127
202PhosphorylationGRVFTCRSMNEAIPS
CCEEEECCHHCCCCC		28.2724702127
209PhosphorylationSMNEAIPSGKETSIE
CHHCCCCCCCEEEEE		57.2824719451
297N-linked_GlycosylationHNKVGSTNVSTLVNV
ECCCCCCCCEEEEEE		27.6919159218
351PhosphorylationKDSNMVLSNSNQLLL
CCCCEEECCCCCEEE		27.1429083192
359AcetylationNSNQLLLKSVTQADA
CCCCEEEEECHHHCC		42.7330589765
360PhosphorylationSNQLLLKSVTQADAG
CCCEEEEECHHHCCC		30.30-
369PhosphorylationTQADAGTYTCRAIVP
HHHCCCEEEEEEEEC		11.70-
370PhosphorylationQADAGTYTCRAIVPR
HHCCCEEEEEEEECC		8.71-
471N-linked_GlycosylationADFQTHYNCTAWNSF
ECCEEECCCCCCCCC		14.73UniProtKB CARBOHYD
532PhosphorylationKGSRKDVTLRKLDIK
CCCCCCCEEEECEEE		30.8624719451
539UbiquitinationTLRKLDIKVETVNRE
EEEECEEEEEEECCC		33.41-
542PhosphorylationKLDIKVETVNREPLT
ECEEEEEEECCCCCC		26.5223186163
549PhosphorylationTVNREPLTMHSDRED
EECCCCCCCCCCCCC		24.4530266825
552PhosphorylationREPLTMHSDREDDTA
CCCCCCCCCCCCCCC		27.7830266825
558PhosphorylationHSDREDDTASVSTAT
CCCCCCCCCCHHHHH		32.9029255136
560PhosphorylationDREDDTASVSTATRV
CCCCCCCCHHHHHHH		20.7729255136
562PhosphorylationEDDTASVSTATRVMK
CCCCCCHHHHHHHHH		15.1629255136
563PhosphorylationDDTASVSTATRVMKA
CCCCCHHHHHHHHHH		29.8729255136
565PhosphorylationTASVSTATRVMKAIY
CCCHHHHHHHHHHHH		24.7229255136
569UbiquitinationSTATRVMKAIYSSFK
HHHHHHHHHHHHHCC		28.86-
572PhosphorylationTRVMKAIYSSFKDDV
HHHHHHHHHHCCCCC		11.7927273156
573PhosphorylationRVMKAIYSSFKDDVD
HHHHHHHHHCCCCCC		24.1630266825
574PhosphorylationVMKAIYSSFKDDVDL
HHHHHHHHCCCCCCC		21.2430266825
576UbiquitinationKAIYSSFKDDVDLKQ
HHHHHHCCCCCCCCC		55.77-
582UbiquitinationFKDDVDLKQDLRCDT
CCCCCCCCCHHCCCC		36.98-
585 (in isoform 2)Ubiquitination-5.63-
588 (in isoform 2)Phosphorylation-40.0227642862
589 (in isoform 2)Phosphorylation-25.1227642862
590 (in isoform 2)Phosphorylation-3.0427642862
592PhosphorylationLRCDTIDTREEYEMK
HCCCCCCCCCCCCCC		35.81-
592 (in isoform 2)Ubiquitination-35.81-
596PhosphorylationTIDTREEYEMKDPTN
CCCCCCCCCCCCCCC		19.3028796482
598 (in isoform 2)Ubiquitination-6.13-
599UbiquitinationTREEYEMKDPTNGYY
CCCCCCCCCCCCCCE		48.92-
602PhosphorylationEYEMKDPTNGYYNVR
CCCCCCCCCCCEECE		51.9521945579
605PhosphorylationMKDPTNGYYNVRAHE
CCCCCCCCEECEECC		8.2421945579
606PhosphorylationKDPTNGYYNVRAHED
CCCCCCCEECEECCC		14.4721945579
608 (in isoform 2)Phosphorylation-3.1027642862
612 (in isoform 2)Phosphorylation-55.5227642862
615 (in isoform 2)Ubiquitination-49.32-
621PhosphorylationRPSSRAVLYADYRAP
CCCCCEEEEEEECCC		2.5917016520
621 (in isoform 2)Phosphorylation-2.5927642862
622PhosphorylationPSSRAVLYADYRAPG
CCCCEEEEEEECCCC		7.2821945579
622 (in isoform 2)Phosphorylation-7.2827642862
625PhosphorylationRAVLYADYRAPGPAR
CEEEEEEECCCCCCC		10.6621945579
626MethylationAVLYADYRAPGPARF
EEEEEEECCCCCCCC		34.5582954929
626 (in isoform 3)Ubiquitination-34.5521890473
638PhosphorylationARFDGRPSSRLSHSS
CCCCCCCCCCCCCCC		27.0828152594
638 (in isoform 2)Phosphorylation-27.0827642862
639PhosphorylationRFDGRPSSRLSHSSG
CCCCCCCCCCCCCCC		39.6728152594
641 (in isoform 2)Phosphorylation-6.1227642862
642PhosphorylationGRPSSRLSHSSGYAQ
CCCCCCCCCCCCCCC		21.8822167270
644PhosphorylationPSSRLSHSSGYAQLN
CCCCCCCCCCCCCCC		23.2922167270
645PhosphorylationSSRLSHSSGYAQLNT
CCCCCCCCCCCCCCC		30.3322167270
647PhosphorylationRLSHSSGYAQLNTYS
CCCCCCCCCCCCCCC		7.9720007894
652PhosphorylationSGYAQLNTYSRGPAS
CCCCCCCCCCCCCHH		31.3126356563
653PhosphorylationGYAQLNTYSRGPASD
CCCCCCCCCCCCHHH		8.6920007894
654PhosphorylationYAQLNTYSRGPASDY
CCCCCCCCCCCHHHC		28.8226356563
654 (in isoform 2)Phosphorylation-28.8227642862
658 (in isoform 2)Phosphorylation-20.1927642862
659PhosphorylationTYSRGPASDYGPEPT
CCCCCCHHHCCCCCC		34.2024114839
660 (in isoform 2)Phosphorylation-55.2927642862
661PhosphorylationSRGPASDYGPEPTPP
CCCCHHHCCCCCCCC		31.8926356563
661 (in isoform 2)Phosphorylation-31.8927642862
663 (in isoform 2)Phosphorylation-37.8627642862
668 (in isoform 2)Phosphorylation-64.9727642862
669 (in isoform 2)Phosphorylation-26.1927642862
670 (in isoform 2)Phosphorylation-30.9027642862
675 (in isoform 2)Phosphorylation-24.0627642862
676PhosphorylationGPAAPAGTDTTSQLS
CCCCCCCCCCCCCCC		32.0726852163
677 (in isoform 2)Phosphorylation-47.2527642862
678PhosphorylationAAPAGTDTTSQLSYE
CCCCCCCCCCCCCCC		28.3426356563
679PhosphorylationAPAGTDTTSQLSYEN
CCCCCCCCCCCCCCC		19.7926356563
680PhosphorylationPAGTDTTSQLSYENY
CCCCCCCCCCCCCCH		31.0826356563
683PhosphorylationTDTTSQLSYENYEKF
CCCCCCCCCCCHHHH		23.8219690332
684PhosphorylationDTTSQLSYENYEKFN
CCCCCCCCCCHHHHH		19.4526356563
687PhosphorylationSQLSYENYEKFNSHP
CCCCCCCHHHHHCCC		14.4627259358
689UbiquitinationLSYENYEKFNSHPFP
CCCCCHHHHHCCCCC		39.21-
692PhosphorylationENYEKFNSHPFPGAA
CCHHHHHCCCCCCCC		35.3521945579
692 (in isoform 2)Phosphorylation-35.3527642862
696 (in isoform 2)Phosphorylation-35.6427642862
699 (in isoform 2)Phosphorylation-24.7827642862
700 (in isoform 2)Phosphorylation-28.5527642862
701PhosphorylationPFPGAAGYPTYRLGY
CCCCCCCCCEEECCC		6.4121945579
703PhosphorylationPGAAGYPTYRLGYPQ
CCCCCCCEEECCCCC		16.8821945579
703 (in isoform 2)Phosphorylation-16.8827642862
704PhosphorylationGAAGYPTYRLGYPQA
CCCCCCEEECCCCCC		10.1921945579
708PhosphorylationYPTYRLGYPQAPPSG
CCEEECCCCCCCCCC		9.2125159151
717 (in isoform 2)Phosphorylation-59.0227642862
719PhosphorylationPPSGLERTPYEAYDP
CCCCCCCCCCCCCCC		22.3521945579
719 (in isoform 2)Phosphorylation-22.3527642862
720PhosphorylationPSGLERTPYEAYDPI
CCCCCCCCCCCCCCC		31.0517016520
720 (in isoform 2)Phosphorylation-31.0527642862
721PhosphorylationSGLERTPYEAYDPIG
CCCCCCCCCCCCCCC		16.7521945579
723PhosphorylationLERTPYEAYDPIGKY
CCCCCCCCCCCCCCC		14.2617016520
724PhosphorylationERTPYEAYDPIGKYA
CCCCCCCCCCCCCCE		15.4321945579
729UbiquitinationEAYDPIGKYATATRF
CCCCCCCCCEEEEEE		32.2221890473
729UbiquitinationEAYDPIGKYATATRF
CCCCCCCCCEEEEEE		32.222189047
729 (in isoform 1)Ubiquitination-32.2221890473
730PhosphorylationAYDPIGKYATATRFS
CCCCCCCCEEEEEEE		12.1727259358
730 (in isoform 2)Phosphorylation-12.1727642862
732PhosphorylationDPIGKYATATRFSYT
CCCCCCEEEEEEEEC		26.0223927012
734PhosphorylationIGKYATATRFSYTSQ
CCCCEEEEEEEECCC		28.0823927012
735 (in isoform 2)Phosphorylation-18.9527642862
737PhosphorylationYATATRFSYTSQHSD
CEEEEEEEECCCCCH		24.9826356563
737 (in isoform 2)Phosphorylation-24.9827642862
738PhosphorylationATATRFSYTSQHSDY
EEEEEEEECCCCCHH		14.0127259358
739O-linked_GlycosylationTATRFSYTSQHSDYG
EEEEEEECCCCCHHH		22.2555821515
739PhosphorylationTATRFSYTSQHSDYG
EEEEEEECCCCCHHH		22.2526356563
740O-linked_GlycosylationATRFSYTSQHSDYGQ
EEEEEECCCCCHHHH		20.0516173765
740PhosphorylationATRFSYTSQHSDYGQ
EEEEEECCCCCHHHH		20.0526356563
740 (in isoform 2)Phosphorylation-20.0527642862
743PhosphorylationFSYTSQHSDYGQRFQ
EEECCCCCHHHHHHH		25.5328152594
745PhosphorylationYTSQHSDYGQRFQQR
ECCCCCHHHHHHHHH		20.4125159151
745 (in isoform 2)Ubiquitination-20.4121890473
753 (in isoform 2)Phosphorylation-4.7227642862
754 (in isoform 2)Phosphorylation-30.5527642862
755 (in isoform 2)Phosphorylation-18.4427642862
756 (in isoform 2)Phosphorylation-13.3427642862
759 (in isoform 2)Phosphorylation-27642862
761 (in isoform 2)Phosphorylation-27642862
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
605YPhosphorylationKinaseFYNP06241
Uniprot
606YPhosphorylationKinaseFYNP06241
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIRR1_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 KIRR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPHN_HUMANNPHS1physical
12865409
ZO1_HUMANTJP1physical
12865409
KIRR1_HUMANKIRRELphysical
12660326
NPHN_HUMANNPHS1physical
12660326
ZO1_HUMANTJP1physical
12578837
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 KIRR1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-605; TYR-721 ANDTYR-724, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-622; TYR-625 ANDTYR-724, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory