KIRR1_MOUSE - dbPTM
KIRR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIRR1_MOUSE
UniProt AC Q80W68
Protein Name Kin of IRRE-like protein 1
Gene Name Kirrel1
Organism Mus musculus (Mouse).
Sequence Length 789
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. Is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1..
Protein Sequence MTLESPSTRLMTCQSSLLPEKPRFLSQKMWAPHLVVAYLIFVTLALALPGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGAGILVVFSFAALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASISTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV
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
43PhosphorylationVAYLIFVTLALALPG
HHHHHHHHHHHHCCC		8.79-
78N-linked_GlycosylationVLPCVLLNYSGIVQW
HHEEEEECCCCCEEE		25.43-
172N-linked_GlycosylationLQAGTPYNLTCRAFN
EECCCCCEEEEECCC		30.03-
329N-linked_GlycosylationYNKVGSTNVSTLVNV
EECCCCCCCHHEEEE		27.6919349973
503N-linked_GlycosylationADFQTHYNCTAWNSF
ECCEEECCCCCCCCC		14.73-
584PhosphorylationREPLTMHSDREDDTA
CCCCCCCCCCCCCCC		27.7826824392
590PhosphorylationHSDREDDTASISTAT
CCCCCCCCCHHHHHH		34.3329233185
592PhosphorylationDREDDTASISTATRV
CCCCCCCHHHHHHHH		21.1126824392
594PhosphorylationEDDTASISTATRVMK
CCCCCHHHHHHHHHH		14.9729233185
595PhosphorylationDDTASISTATRVMKA
CCCCHHHHHHHHHHH		30.3126824392
604PhosphorylationTRVMKAIYSSFKDDV
HHHHHHHHHHCCCCC		11.7920116462
605PhosphorylationRVMKAIYSSFKDDVD
HHHHHHHHHCCCCCC		24.1622499769
606PhosphorylationVMKAIYSSFKDDVDL
HHHHHHHHCCCCCCC		21.2422499769
614UbiquitinationFKDDVDLKQDLRCDT
CCCCCCCCCHHCCCC		36.9822790023
624PhosphorylationLRCDTIDTREEYEMK
HCCCCCCCCCCCCCC		35.8122817900
628PhosphorylationTIDTREEYEMKDPTN
CCCCCCCCCCCCCCC		19.3022817900
631UbiquitinationTREEYEMKDPTNGYY
CCCCCCCCCCCCCCE		48.9222790023
634PhosphorylationEYEMKDPTNGYYNVR
CCCCCCCCCCCEECE		51.9522499769
637PhosphorylationMKDPTNGYYNVRAHE
CCCCCCCCEECEECC		8.2422499769
638PhosphorylationKDPTNGYYNVRAHED
CCCCCCCEECEECCC		14.4722499769
648PhosphorylationRAHEDRPSSRAVLYA
EECCCCCCCCEEEEE		33.0927717184
649PhosphorylationAHEDRPSSRAVLYAD
ECCCCCCCCEEEEEE		27.2626824392
654PhosphorylationPSSRAVLYADYRAPG
CCCCEEEEEEECCCC		7.2822499769
657PhosphorylationRAVLYADYRAPGPTR
CEEEEEEECCCCCCC		10.6622499769
663PhosphorylationDYRAPGPTRFDGRPS
EECCCCCCCCCCCCC		50.3022499769
670PhosphorylationTRFDGRPSSRLSHSS
CCCCCCCCCCCCCCC		27.0825168779
671PhosphorylationRFDGRPSSRLSHSSG
CCCCCCCCCCCCCCC		39.6724899341
674PhosphorylationGRPSSRLSHSSGYAQ
CCCCCCCCCCCCCEE		21.8822499769
676PhosphorylationPSSRLSHSSGYAQLN
CCCCCCCCCCCEECC		23.2922499769
677PhosphorylationSSRLSHSSGYAQLNT
CCCCCCCCCCEECCC		30.3322499769
679PhosphorylationRLSHSSGYAQLNTYS
CCCCCCCCEECCCCC		7.9720116462
684PhosphorylationSGYAQLNTYSRAPAS
CCCEECCCCCCCCHH		31.3122499769
685PhosphorylationGYAQLNTYSRAPASD
CCEECCCCCCCCHHH		8.6220116462
686PhosphorylationYAQLNTYSRAPASDY
CEECCCCCCCCHHHC		21.6722499769
691PhosphorylationTYSRAPASDYGTEPT
CCCCCCHHHCCCCCC		30.2429514104
710PhosphorylationSAPGGTDTTSQLSYE
CCCCCCCCCCCCCCC		28.3421082442
711PhosphorylationAPGGTDTTSQLSYEN
CCCCCCCCCCCCCCC		19.7921082442
712PhosphorylationPGGTDTTSQLSYENY
CCCCCCCCCCCCCCH		31.0821183079
715PhosphorylationTDTTSQLSYENYEKF
CCCCCCCCCCCHHHH		23.8229514104
716PhosphorylationDTTSQLSYENYEKFN
CCCCCCCCCCHHHHH		19.45-
719PhosphorylationSQLSYENYEKFNSHP
CCCCCCCHHHHHCCC		14.4622817900
724PhosphorylationENYEKFNSHPFPGAA
CCHHHHHCCCCCCCC		35.3522499769
733PhosphorylationPFPGAAGYPTYRLGY
CCCCCCCCCEEECCC		6.4122499769
735PhosphorylationPGAAGYPTYRLGYPQ
CCCCCCCEEECCCCC		16.8822499769
736PhosphorylationGAAGYPTYRLGYPQA
CCCCCCEEECCCCCC		10.1922499769
740PhosphorylationYPTYRLGYPQAPPSG
CCEEECCCCCCCCCC		9.2129514104
751PhosphorylationPPSGLERTPYEAYDP
CCCCCCCCCCCCCCC		22.3522499769
753PhosphorylationSGLERTPYEAYDPIG
CCCCCCCCCCCCCCC		16.7520116462
756PhosphorylationERTPYEAYDPIGKYA
CCCCCCCCCCCCCCE		15.4320116462
762PhosphorylationAYDPIGKYATATRFS
CCCCCCCCEEEEEEE		12.1720116462
764PhosphorylationDPIGKYATATRFSYT
CCCCCCEEEEEEEEC		26.0222499769
766PhosphorylationIGKYATATRFSYTSQ
CCCCEEEEEEEECCC		28.0822499769
769PhosphorylationYATATRFSYTSQHSD
CEEEEEEEECCCCCH		24.9822499769
770PhosphorylationATATRFSYTSQHSDY
EEEEEEEECCCCCHH		14.0122499769
771PhosphorylationTATRFSYTSQHSDYG
EEEEEEECCCCCHHH		22.2529514104
772PhosphorylationATRFSYTSQHSDYGQ
EEEEEECCCCCHHHH		20.0522499769
775PhosphorylationFSYTSQHSDYGQRFQ
EEECCCCCHHHHHHH		25.5322499769
777PhosphorylationYTSQHSDYGQRFQQR
ECCCCCHHHHHHHHH		20.4122499769
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
637YPhosphorylationKinaseFYNP06241
PSP
637YPhosphorylationKinaseFYNP39688
Uniprot
638YPhosphorylationKinaseFYNP06241
PSP
638YPhosphorylationKinaseFYNP39688
Uniprot
716YPhosphorylationKinaseFYNP06241
PSP
716YPhosphorylationKinaseFYNP39688
PSP
719YPhosphorylationKinaseFYNP06241
PSP
719YPhosphorylationKinaseFYNP39688
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIRR1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KIRR1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIRR1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-329, AND MASSSPECTROMETRY.

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