JKIP1_HUMAN - dbPTM
JKIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JKIP1_HUMAN
UniProt AC Q96N16
Protein Name Janus kinase and microtubule-interacting protein 1
Gene Name JAKMIP1
Organism Homo sapiens (Human).
Sequence Length 626
Subcellular Localization Cytoplasm, cytoskeleton. Membrane
Peripheral membrane protein. Colocalizes with the microtubule network. Localizes to the cell body and neurites of hippocampal neurons where it accumulates in granules. Localizes to the tail and to a lower extent to
Protein Description Associates with microtubules and may play a role in the microtubule-dependent transport of the GABA-B receptor. May play a role in JAK1 signaling and regulate microtubule cytoskeleton rearrangements..
Protein Sequence MSKKGRSKGEKPEMETDAVQMANEELRAKLTSIQIEFQQEKSKVGKLRERLQEAKLEREQEQRRHTAYISELKAKLHEEKTKELQALREGLIRQHEQEAARTAKIKEGELQRLQATLNVLRDGAADKVKTALLTEAREEARRAFDGERLRLQQEILELKAARKQAEEALSNCMQADKTKAADLRAAYQAHQDEVHRIKRECERDIRRLMDEIKGKDRVILALEKELGVQAGQTQKLLLQKEALDEQLVQVKEAERHHSSPKRELPPGIGDMVELMGVQDQHMDERDVRRFQLKIAELNSVIRKLEDRNTLLADERNELLKRSRETEVQLKPLVEKNKRMNKKNEDLLQSIQRMEEKIKNLTRENVEMKEKLSAQASLKRHTSLNDLSLTRDEQEIEFLRLQVLEQQHVIDDLSLERERLLRSKRHRGKSLKPPKKHVVETFFGFDEESVDSETLSETSYNTDRTDRTPATPEEDLDDATAREEADLRFCQLTREYQALQRAYALLQEQVGGTLDAEREARTREQLQADLLRCQAKIEDLEKLLVEKGQDSKWVEEKQLLIRTNQDLLEKIYRLEMEENQLKNEMQDAKDQNELLEFRVLELEVRDSICCKLSNGADILFEPKLKFM
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
7Phosphorylation-MSKKGRSKGEKPEM
-CCCCCCCCCCCCCC		54.39-
31PhosphorylationEELRAKLTSIQIEFQ
HHHHHHHHHHHHHHH		24.0724043423
32PhosphorylationELRAKLTSIQIEFQQ
HHHHHHHHHHHHHHH		23.9624043423
73UbiquitinationTAYISELKAKLHEEK
HHHHHHHHHHHCHHH		39.15-
86UbiquitinationEKTKELQALREGLIR
HHHHHHHHHHHHHHH		22.63-
213UbiquitinationRRLMDEIKGKDRVIL
HHHHHHHCCCHHEEH		58.84-
235UbiquitinationVQAGQTQKLLLQKEA
CCCCHHHHHHHHHHH		44.48-
251UbiquitinationDEQLVQVKEAERHHS
HHHHHHHHHHHHHCC		33.83-
293UbiquitinationDVRRFQLKIAELNSV
HHHHHHHHHHHHHHH		29.14-
376PhosphorylationEKLSAQASLKRHTSL
HHHHHHHHHHHCCCC		23.4927067055
378UbiquitinationLSAQASLKRHTSLND
HHHHHHHHHCCCCHH		39.37-
378AcetylationLSAQASLKRHTSLND
HHHHHHHHHCCCCHH		39.3725953088
381PhosphorylationQASLKRHTSLNDLSL
HHHHHHCCCCHHHCC		38.6528122231
381UbiquitinationQASLKRHTSLNDLSL
HHHHHHCCCCHHHCC		38.65-
382PhosphorylationASLKRHTSLNDLSLT
HHHHHCCCCHHHCCC		21.0323911959
386UbiquitinationRHTSLNDLSLTRDEQ
HCCCCHHHCCCCCHH		4.38-
387PhosphorylationHTSLNDLSLTRDEQE
CCCCHHHCCCCCHHH		30.4730576142
389PhosphorylationSLNDLSLTRDEQEIE
CCHHHCCCCCHHHHH		32.4726552605
391UbiquitinationNDLSLTRDEQEIEFL
HHHCCCCCHHHHHHH		57.61-
404UbiquitinationFLRLQVLEQQHVIDD
HHHHHHHHHCCCCCC		49.71-
424 (in isoform 3)Phosphorylation-26.4422210691
426 (in isoform 3)Phosphorylation-59.2622210691
445UbiquitinationVETFFGFDEESVDSE
HHEECCCCHHHCCCC		60.16-
464PhosphorylationTSYNTDRTDRTPATP
CCCCCCCCCCCCCCC		32.4230108239
467PhosphorylationNTDRTDRTPATPEED
CCCCCCCCCCCCHHH		21.7830108239
470PhosphorylationRTDRTPATPEEDLDD
CCCCCCCCCHHHCCC		32.2228122231
479PhosphorylationEEDLDDATAREEADL
HHHCCCCHHHHHHHH		32.9927732954
516 (in isoform 4)Phosphorylation-51.20-
541UbiquitinationAKIEDLEKLLVEKGQ
HHHHHHHHHHHHCCC		55.19-
546UbiquitinationLEKLLVEKGQDSKWV
HHHHHHHCCCCCCHH		55.16-
551UbiquitinationVEKGQDSKWVEEKQL
HHCCCCCCHHHHHHH		64.64-
556UbiquitinationDSKWVEEKQLLIRTN
CCCHHHHHHHHHHHC		32.51-
566 (in isoform 5)Phosphorylation-4.85-
569UbiquitinationTNQDLLEKIYRLEME
HCHHHHHHHHHHHHH		45.03-
588UbiquitinationKNEMQDAKDQNELLE
HHHHCHHHHHHHHHH		69.04-
593 (in isoform 5)Phosphorylation-7.92-
610UbiquitinationVRDSICCKLSNGADI
ECCCCEEECCCCCCE		51.00-
622UbiquitinationADILFEPKLKFM---
CCEEECCCCCCC---		58.05-
751 (in isoform 2)Phosphorylation--
778 (in isoform 2)Phosphorylation--
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 JKIP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JKIP1_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 JKIP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of JKIP1_HUMAN !!
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 JKIP1_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-382 AND THR-470, ANDMASS SPECTROMETRY.

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