KI20B_MOUSE - dbPTM
KI20B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KI20B_MOUSE
UniProt AC Q80WE4
Protein Name Kinesin-like protein KIF20B {ECO:0000305}
Gene Name Kif20b {ECO:0000312|MGI:MGI:2444576}
Organism Mus musculus (Mouse).
Sequence Length 1774
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . Midbody . Cell projection, axon
Protein Description Plus-end-directed motor enzyme that is required for completion of cytokinesis (By similarity). Required for proper midbody organization and abscission in polarized cortical stem cells. [PubMed: 24173802 Plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. Participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner]
Protein Sequence MESHLNPDGVPRPSYVFSADPIARPLEINFDGVKLDLSHEFSLVASNPAANSLGSKNYLQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMSFKPHRCREYLKLSSDQEKEESANKNTLLRQIKEVTIHNDSYDVLCGHLTNSLTIPEFEESVNSCDQSSLNVDNIKYSVWVSFFEIYNESIYDLFVPVSSKFQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFSTTAQRVYVPDTLSSSQEKSFASNKSLQDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDLVEDLEENEETQNMETELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDEPTNRICDIELETEEAHNYVGVEDIFHSLQDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTPLQPNKMAVKHPGCPTPVTIKIPKARKRKSGEVEEDLVKCENKKNSTPRSNVKFPVSEHRNSPVKKEQKVSVGPSSKKTYSLRSQASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETMSSPKLSTVEVSKENVSQPKKAKRKLYRNEISSPINISGQVILMEQKVKETDHQILKRRLRTRTAK
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
38PhosphorylationDGVKLDLSHEFSLVA
CCEEEECCCCEEEEE		22.1926643407
42PhosphorylationLDLSHEFSLVASNPA
EECCCCEEEEECCCC		20.9626643407
302PhosphorylationKRKMLRLSQDIKGYS
HHHHHHHCCCCCCCH		21.2617525332
348PhosphorylationTKLNNASSRSHSIFT
EECCCCCCCCCEEEE		35.0828059163
482PhosphorylationQRVYVPDTLSSSQEK
CEEECCCCCCCHHHH		23.5926643407
484PhosphorylationVYVPDTLSSSQEKSF
EECCCCCCCHHHHCC		30.0026643407
485PhosphorylationYVPDTLSSSQEKSFA
ECCCCCCCHHHHCCC		38.8726643407
486PhosphorylationVPDTLSSSQEKSFAS
CCCCCCCHHHHCCCC		38.7026643407
548PhosphorylationEETQNMETELTDEDS
HHHHCHHCCCCCCCC		26.06-
551PhosphorylationQNMETELTDEDSDKS
HCHHCCCCCCCCCCC		30.98-
649PhosphorylationDLVGKCDSQDEPTNR
HHHCCCCCCCCCCCC		49.3427149854
725PhosphorylationVKAELAETKEELIKA
HHHHHHHHHHHHHHH		37.8429514104
741PhosphorylationEELKNRESNSLVQAL
HHHHCCCCHHHHHHH		28.6026643407
743PhosphorylationLKNRESNSLVQALKT
HHCCCCHHHHHHHHH		38.9128066266
806PhosphorylationKKGLILVSPPITEEQ
CCCEEEECCCCCHHH		22.8626824392
810PhosphorylationILVSPPITEEQNKMG
EEECCCCCHHHHHHC		38.9628066266
947PhosphorylationTKIDELRSLDSPSHI
HHHHHHHCCCCCCCC		49.5026643407
950PhosphorylationDELRSLDSPSHISKI
HHHHCCCCCCCCCCE		33.3326824392
952PhosphorylationLRSLDSPSHISKIDL
HHCCCCCCCCCCEEE		37.0925159016
955PhosphorylationLDSPSHISKIDLLNL
CCCCCCCCCEEECCH		20.3826643407
966PhosphorylationLLNLQDLSSGAKGDN
ECCHHHCCCCCCCCC		34.7128066266
967PhosphorylationLNLQDLSSGAKGDNC
CCHHHCCCCCCCCCC		50.4928066266
977PhosphorylationKGDNCLNTSQQLPGG
CCCCCCCCCCCCCCC		18.2426643407
978PhosphorylationGDNCLNTSQQLPGGD
CCCCCCCCCCCCCCC		18.1726643407
1086PhosphorylationREELQEKSVSLRVQV
HHHHHHCCCHHHHHH		19.0430387612
1088PhosphorylationELQEKSVSLRVQVQL
HHHHCCCHHHHHHHH		19.9722802335
1107PhosphorylationEQALSELSQDVTCYK
HHHHHHHHCCCCCCH		21.9317525332
1260PhosphorylationEQVQREVSVMRDEEK
HHHHHHHHCCCCHHH		12.8720495213
1374PhosphorylationEKFKDLETRSNQRLN
HHHHCHHHHHCCCCC		46.8520139300
1457PhosphorylationKLQNEVETLTAQLAE
HHHHHHHHHHHHHHH		34.2922802335
1542PhosphorylationETEPQSTSLEISRNT
CCCCCCCEEEEECCC		29.29-
1598PhosphorylationVKHPGCPTPVTIKIP
CCCCCCCCCEEEECC		34.1728066266
1612PhosphorylationPKARKRKSGEVEEDL
CCCCCCCCCCCHHHH		44.1926824392
1629PhosphorylationCENKKNSTPRSNVKF
CCCCCCCCCCCCCCC		31.9220139300
1639PhosphorylationSNVKFPVSEHRNSPV
CCCCCCCCCCCCCCC		28.1125266776
1644PhosphorylationPVSEHRNSPVKKEQK
CCCCCCCCCCCCCCC		30.9025263469
1669PhosphorylationYSLRSQASTVSANIA
EEHHHHHHCHHHHHH		23.0029514104
1694PhosphorylationFGDFLQHSPTILQSK
HHHHHHCCHHHHHHH		15.6926824392
1696PhosphorylationDFLQHSPTILQSKAK
HHHHCCHHHHHHHHH		37.0225168779
1700PhosphorylationHSPTILQSKAKKIIE
CCHHHHHHHHHHHHH		31.0025159016
1708PhosphorylationKAKKIIETMSSPKLS
HHHHHHHHCCCCCCC		16.3725159016
1710PhosphorylationKKIIETMSSPKLSTV
HHHHHHCCCCCCCEE		51.4026824392
1711PhosphorylationKIIETMSSPKLSTVE
HHHHHCCCCCCCEEE		18.4126824392
1716PhosphorylationMSSPKLSTVEVSKEN
CCCCCCCEEECCHHH		30.9922942356
1720PhosphorylationKLSTVEVSKENVSQP
CCCEEECCHHHCCCC		22.2723140645
1735PhosphorylationKKAKRKLYRNEISSP
HHHHHHHHHCCCCCC		17.9023984901
1740PhosphorylationKLYRNEISSPINISG
HHHHCCCCCCEECCC		24.7123984901
1741PhosphorylationLYRNEISSPINISGQ
HHHCCCCCCEECCCE		35.1523984901
1746PhosphorylationISSPINISGQVILME
CCCCEECCCEEEEEE		20.7726745281
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
1598TPhosphorylationKinaseCDK1P11440
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KI20B_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 KI20B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DIAP2_HUMANDIAPH2physical
26496610
DNLI3_HUMANLIG3physical
26496610
KI67_HUMANMKI67physical
26496610
LIS1_HUMANPAFAH1B1physical
26496610
HM20A_HUMANHMG20Aphysical
26496610
SF3B2_HUMANSF3B2physical
26496610
ICE1_HUMANICE1physical
26496610
TB10B_HUMANTBC1D10Bphysical
26496610
TDIF2_HUMANDNTTIP2physical
26496610
NDE1_HUMANNDE1physical
26496610
XPO5_HUMANXPO5physical
26496610
SHOT1_HUMANKIAA1598physical
26496610
TGS1_HUMANTGS1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KI20B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-1107, ANDMASS SPECTROMETRY.

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