KIF4B_HUMAN - dbPTM
KIF4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF4B_HUMAN
UniProt AC Q2VIQ3
Protein Name Chromosome-associated kinesin KIF4B
Gene Name KIF4B
Organism Homo sapiens (Human).
Sequence Length 1234
Subcellular Localization Nucleus matrix. Cytoplasm, cytoskeleton .
Protein Description Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity)..
Protein Sequence MKEEVKGIPVRVALRCRPLVPKEISEGCQMCLSFVPGETQVVVGTDKSFTYDFVFDPCTEQEEVFNKAVAPLIKGIFKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGIIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISIEQRKKSDKNCSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGSFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLSTLRYADRARKIKNKPIVNIDPHTAELNHLKQQVQQLQVLLLQAHGGTLPGSINAEPSENLQSLMEKNQSLVEENEKLSRCLSKAAGQTAQMLERIILTEQVNEKLNAKLEELRQHVACKLDLQKLVETLEDQELKENVEIICNLQQLITQLSDETVACTAAAIDTAVEEEAQVETSPETSRSSDAFTTQHALHQAQMSKEVVELNNALALKEALVRKMTQNDNQLQPIQFQYQDNIKNLELEVINLQKEKEELVRELQTAKKNVNQAKLSEHRHKLLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIWMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSSVLRRKTEEAAAANKRLKDALQKQREVTDKRKETQSHGKEGIAARVRNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVVQLKEKKESRENPPPKLRKCTFSLSEVHGQVLESEDCITKQIESLETEMELRSAQIADLQQKLLDAESEDRPKQCWENIATILEAKCALKYLIGELVSSKIHVTKLENSLRQSKASCADMQKMLFEEQNHFSEIETELQAELVRMEQQHQEKVLYLVSQLQESQMAEKQLEKSASEKEQQLVSTLQCQDEELEKMREVCEQNQQLLQENEIIKQKLILLQVASRQKHLPNDTLLSPDSSFEYIPPKPKPSRVKEKFLEQSMDIEDLKYCSEHSVNEHEDGDGDGDSDEGDDEEWKPTKLVKVSRKNIQGCSCKGWCGNKQCGCRKQKSDCGVDCSCDPTKCRNRQQGKDSLGTVEQTQDSEGSFKLEDPTEVTPGLSFFNPVCATPNSKILKEMCDMEQVLSKKTAPAPSPFDLPESKHGATEYQQNKPPGKKKKRALASNTSFFSGCSPIEEEAH
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
129UbiquitinationLFKEIDKKSDFEFTL
HHHHHCCCCCCEEEE
52.05-
158UbiquitinationLLCPSREKAQINIRE
HHCCCHHHHCCCCCC
44.47-
172UbiquitinationEDPKEGIKIVGLTEK
CCCCCCEEEEECCCC
42.04-
180PhosphorylationIVGLTEKTVLVALDT
EEECCCCEEEEEEEH
16.9130377224
187PhosphorylationTVLVALDTVSCLEQG
EEEEEEEHHHHHHCC
18.3730377224
189PhosphorylationLVALDTVSCLEQGNN
EEEEEHHHHHHCCCC
18.3130377224
197PhosphorylationCLEQGNNSRTVASTA
HHHCCCCCHHHHHHH
33.0730377224
199PhosphorylationEQGNNSRTVASTAMN
HCCCCCHHHHHHHCC
21.9030377224
203PhosphorylationNSRTVASTAMNSQSS
CCHHHHHHHCCCCCC
21.86-
207PhosphorylationVASTAMNSQSSRSHA
HHHHHCCCCCCCCCE
20.5327732954
209PhosphorylationSTAMNSQSSRSHAIF
HHHCCCCCCCCCEEE
27.7827732954
210PhosphorylationTAMNSQSSRSHAIFT
HHCCCCCCCCCEEEE
30.1127732954
234PhosphorylationDKNCSFRSKLHLVDL
CCCCCHHHHHHHHHH
37.2424719451
235UbiquitinationKNCSFRSKLHLVDLA
CCCCHHHHHHHHHHC
35.35-
244PhosphorylationHLVDLAGSERQKKTK
HHHHHCCCHHHHCHH
24.81-
250PhosphorylationGSERQKKTKAEGDRL
CCHHHHCHHCCCCHH
42.3923403867
251UbiquitinationSERQKKTKAEGDRLK
CHHHHCHHCCCCHHH
54.01-
258UbiquitinationKAEGDRLKEGININR
HCCCCHHHHCCCCCC
55.58-
269GlutathionylationNINRGLLCLGNVISA
CCCCHHHHHHHHHHH
5.7122555962
292UbiquitinationFVPYRDSKLTRLLQD
CCCCCCCHHHHHHHH
59.16-
294PhosphorylationPYRDSKLTRLLQDSL
CCCCCHHHHHHHHHC
24.0220068231
300PhosphorylationLTRLLQDSLGGNSHT
HHHHHHHHCCCCCEE
18.8924043423
305PhosphorylationQDSLGGNSHTLMIAC
HHHCCCCCEEEEEEE
22.5624043423
307PhosphorylationSLGGNSHTLMIACVS
HCCCCCEEEEEEEEC
20.1724043423
314PhosphorylationTLMIACVSPADSNLE
EEEEEEECCCCCCHH
17.7924043423
318PhosphorylationACVSPADSNLEETLS
EEECCCCCCHHHHHH
45.4824043423
323PhosphorylationADSNLEETLSTLRYA
CCCCHHHHHHHHHHH
19.3424043423
325PhosphorylationSNLEETLSTLRYADR
CCHHHHHHHHHHHHH
32.5824043423
326PhosphorylationNLEETLSTLRYADRA
CHHHHHHHHHHHHHH
20.5424043423
394PhosphorylationSLMEKNQSLVEENEK
HHHHHCHHHHHHHHH
43.7229255136
401UbiquitinationSLVEENEKLSRCLSK
HHHHHHHHHHHHHHH
64.44-
401SumoylationSLVEENEKLSRCLSK
HHHHHHHHHHHHHHH
64.44-
401SumoylationSLVEENEKLSRCLSK
HHHHHHHHHHHHHHH
64.44-
407PhosphorylationEKLSRCLSKAAGQTA
HHHHHHHHHHCHHHH
24.71-
449UbiquitinationACKLDLQKLVETLED
HHHHHHHHHHHHHCH
62.89-
460SumoylationTLEDQELKENVEIIC
HHCHHHHHHHHHHHH
46.63-
474PhosphorylationCNLQQLITQLSDETV
HHHHHHHHHCCCCHH
31.8617081983
507PhosphorylationTSPETSRSSDAFTTQ
CCCCCCCCCCCHHHH
32.1319691289
508PhosphorylationSPETSRSSDAFTTQH
CCCCCCCCCCHHHHH
31.6719691289
557PhosphorylationLQPIQFQYQDNIKNL
CCCCEEECHHHHCCC
21.08-
584PhosphorylationELVRELQTAKKNVNQ
HHHHHHHHHHHHHHH
53.7428258704
624AcetylationNEQSKLLKLKESTER
HHHHHHHHHHHHHHH
68.877266935
670UbiquitinationQWKQKKDKEVIQLKE
HHHHHCCHHHHHHHH
63.86-
676UbiquitinationDKEVIQLKERDRKRQ
CHHHHHHHHHHHHHH
34.04-
684PhosphorylationERDRKRQYELLKLER
HHHHHHHHHHHHHHH
16.7528152594
688UbiquitinationKRQYELLKLERNFQK
HHHHHHHHHHHHHHH
62.01-
715UbiquitinationAAANKRLKDALQKQR
HHHHHHHHHHHHHHH
45.01-
799PhosphorylationPPKLRKCTFSLSEVH
CCCHHHCEEEHHHHH
21.21-
801PhosphorylationKLRKCTFSLSEVHGQ
CHHHCEEEHHHHHCH
16.91-
840UbiquitinationQIADLQQKLLDAESE
HHHHHHHHHHHCCCC
37.7521890473
868AcetylationLEAKCALKYLIGELV
HHHHHHHHHHHHHHH
21.34-
869PhosphorylationEAKCALKYLIGELVS
HHHHHHHHHHHHHHH
12.3820068231
876PhosphorylationYLIGELVSSKIHVTK
HHHHHHHHCCCCHHH
38.2420068231
877PhosphorylationLIGELVSSKIHVTKL
HHHHHHHCCCCHHHH
28.3120068231
933PhosphorylationQHQEKVLYLVSQLQE
HHHHHHHHHHHHHHH
14.1929978859
936PhosphorylationEKVLYLVSQLQESQM
HHHHHHHHHHHHHHH
23.6829978859
941PhosphorylationLVSQLQESQMAEKQL
HHHHHHHHHHHHHHH
16.5829978859
951PhosphorylationAEKQLEKSASEKEQQ
HHHHHHHCHHHHHHH
27.87-
961PhosphorylationEKEQQLVSTLQCQDE
HHHHHHHHHHHCCHH
31.8024275569
1001PhosphorylationLILLQVASRQKHLPN
HHHHHHHHCCCCCCC
36.07-
1013PhosphorylationLPNDTLLSPDSSFEY
CCCCCCCCCCCCCCC
29.76-
1017PhosphorylationTLLSPDSSFEYIPPK
CCCCCCCCCCCCCCC
29.49-
1028PhosphorylationIPPKPKPSRVKEKFL
CCCCCCCCHHHHHHH
56.69-
1038PhosphorylationKEKFLEQSMDIEDLK
HHHHHHHCCCHHHHH
14.7329255136
1046PhosphorylationMDIEDLKYCSEHSVN
CCHHHHHHHHHCCCC
14.4317081983
1048PhosphorylationIEDLKYCSEHSVNEH
HHHHHHHHHCCCCCC
34.9428985074
1051PhosphorylationLKYCSEHSVNEHEDG
HHHHHHCCCCCCCCC
23.6828985074
1097UbiquitinationCKGWCGNKQCGCRKQ
CCCCCCCCCCCCCCC
32.05-
1106PhosphorylationCGCRKQKSDCGVDCS
CCCCCCCCCCCCCCC
35.32-
1113PhosphorylationSDCGVDCSCDPTKCR
CCCCCCCCCCCHHCC
19.66-
1117PhosphorylationVDCSCDPTKCRNRQQ
CCCCCCCHHCCCCCC
29.53-
1128PhosphorylationNRQQGKDSLGTVEQT
CCCCCCCCCCCCEEC
31.98-
1135PhosphorylationSLGTVEQTQDSEGSF
CCCCCEECCCCCCCE
22.3423663014
1138PhosphorylationTVEQTQDSEGSFKLE
CCEECCCCCCCEECC
33.7623663014
1141PhosphorylationQTQDSEGSFKLEDPT
ECCCCCCCEECCCCC
18.3723663014
1148PhosphorylationSFKLEDPTEVTPGLS
CEECCCCCCCCCCCC
56.2423663014
1151PhosphorylationLEDPTEVTPGLSFFN
CCCCCCCCCCCCCCC
12.8523663014
1155PhosphorylationTEVTPGLSFFNPVCA
CCCCCCCCCCCCCCC
33.4429255136
1163PhosphorylationFFNPVCATPNSKILK
CCCCCCCCCCHHHHH
20.2029255136
1166PhosphorylationPVCATPNSKILKEMC
CCCCCCCHHHHHHHC
23.4429255136
1183PhosphorylationEQVLSKKTAPAPSPF
HHHHCCCCCCCCCCC
41.4322461510
1188PhosphorylationKKTAPAPSPFDLPES
CCCCCCCCCCCCCCC
40.06-
1200PhosphorylationPESKHGATEYQQNKP
CCCCCCCCHHHCCCC
39.5622461510
1202PhosphorylationSKHGATEYQQNKPPG
CCCCCCHHHCCCCCC
15.8522461510
1218PhosphorylationKKKRALASNTSFFSG
HHHHHHHCCCCCCCC
41.3022167270
1220PhosphorylationKRALASNTSFFSGCS
HHHHHCCCCCCCCCC
25.1522167270
1221PhosphorylationRALASNTSFFSGCSP
HHHHCCCCCCCCCCC
28.6622167270
1224PhosphorylationASNTSFFSGCSPIEE
HCCCCCCCCCCCCCC
36.5622167270
1227PhosphorylationTSFFSGCSPIEEEAH
CCCCCCCCCCCCCCC
32.2222167270

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 KIF4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF4B_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 KIF4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KIF4B_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 KIF4B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-1038, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038 AND SER-1227, ANDMASS SPECTROMETRY.

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