KIF15_HUMAN - dbPTM
KIF15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF15_HUMAN
UniProt AC Q9NS87
Protein Name Kinesin-like protein KIF15
Gene Name KIF15
Organism Homo sapiens (Human).
Sequence Length 1388
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, spindle. Detected during the interphase in the cytoplasm as finely punctuate pattern and irregularly shaped dots. Detected during mitosis on the mitotic spindle. Colocalizes with TPX2 in mitosis. Localizes at the c
Protein Description Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly..
Protein Sequence MAPGCKTELRSVTNGQSNQPSNEGDAIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSES
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
116PhosphorylationGQTGSGKTFTMMGPS
EECCCCCEEEEECCC
28.0620068231
118PhosphorylationTGSGKTFTMMGPSES
CCCCCEEEEECCCCC
16.1020068231
123PhosphorylationTFTMMGPSESDNFSH
EEEEECCCCCCCCCH
43.9620068231
125PhosphorylationTMMGPSESDNFSHNL
EEECCCCCCCCCHHC
42.0420068231
129PhosphorylationPSESDNFSHNLRGVI
CCCCCCCCHHCCCCC
20.0920068231
139PhosphorylationLRGVIPRSFEYLFSL
CCCCCCHHHHHHHHH
19.6420068231
142PhosphorylationVIPRSFEYLFSLIDR
CCCHHHHHHHHHHHH
15.8420068231
145PhosphorylationRSFEYLFSLIDREKE
HHHHHHHHHHHHHHH
23.0920068231
226PhosphorylationWRNRRVASTSMNRES
CCCCCCCCCCCCCHH
20.39-
259PhosphorylationEIVNIRTSLLNLVDL
CEEEHHHHHHHHHHH
22.4728387310
283UbiquitinationHAEGMRLKEAGNINR
CHHHCCHHHHCCCHH
34.84-
291PhosphorylationEAGNINRSLSCLGQV
HHCCCHHHHHHHHHH
21.8328348404
293PhosphorylationGNINRSLSCLGQVIT
CCCHHHHHHHHHHHH
14.4528348404
309UbiquitinationLVDVGNGKQRHVCYR
HHCCCCCCEEEEEEE
48.43-
350PhosphorylationGSRCFGETLSTLNFA
CCCCCHHHHHHCCHH
26.79-
378PhosphorylationEDTQGNVSQLQAEVK
CCCCCCHHHHHHHHH
29.2227050516
385UbiquitinationSQLQAEVKRLKEQLA
HHHHHHHHHHHHHHH
43.44-
388UbiquitinationQAEVKRLKEQLAELA
HHHHHHHHHHHHHHH
47.66-
396PhosphorylationEQLAELASGQTPPES
HHHHHHHCCCCCCHH
44.0228464451
399PhosphorylationAELASGQTPPESFLT
HHHHCCCCCCHHHCC
44.3225159151
403PhosphorylationSGQTPPESFLTRDKK
CCCCCCHHHCCCCCC
31.1826074081
412PhosphorylationLTRDKKKTNYMEYFQ
CCCCCCCCCHHHHHH
40.2223401153
414PhosphorylationRDKKKTNYMEYFQEA
CCCCCCCHHHHHHHH
9.1423401153
434PhosphorylationKSEQEKKSLIEKVTQ
CCHHHHHHHHHHHHH
45.7224719451
438UbiquitinationEKKSLIEKVTQLEDL
HHHHHHHHHHHHHHH
43.52-
448UbiquitinationQLEDLTLKKEKFIQS
HHHHHHHCHHHHHHC
54.36-
449UbiquitinationLEDLTLKKEKFIQSN
HHHHHHCHHHHHHCC
70.06-
455PhosphorylationKKEKFIQSNKMIVKF
CHHHHHHCCCEEEEE
33.3318452278
512UbiquitinationEHHPRVAKYAMENHS
HHCHHHHHHHHHCCC
30.59-
513PhosphorylationHHPRVAKYAMENHSL
HCHHHHHHHHHCCCC
11.0525332170
534UbiquitinationLRLLEPVKRAQEMDA
HHHHHHHHHHHHHCH
53.37-
539SulfoxidationPVKRAQEMDAQTIAK
HHHHHHHHCHHHHHH
3.2621406390
546SumoylationMDAQTIAKLEKAFSE
HCHHHHHHHHHHHHH
54.02-
546UbiquitinationMDAQTIAKLEKAFSE
HCHHHHHHHHHHHHH
54.02-
546SumoylationMDAQTIAKLEKAFSE
HCHHHHHHHHHHHHH
54.02-
549UbiquitinationQTIAKLEKAFSEISG
HHHHHHHHHHHHHHC
66.23-
555PhosphorylationEKAFSEISGMEKSDK
HHHHHHHHCCCCCCC
28.2126074081
557SulfoxidationAFSEISGMEKSDKNQ
HHHHHHCCCCCCCCC
4.7121406390
560PhosphorylationEISGMEKSDKNQQGF
HHHCCCCCCCCCCCC
40.2826552605
562UbiquitinationSGMEKSDKNQQGFSP
HCCCCCCCCCCCCCH
64.84-
568PhosphorylationDKNQQGFSPKAQKEP
CCCCCCCCHHHCCCC
32.1122167270
570UbiquitinationNQQGFSPKAQKEPCL
CCCCCCHHHCCCCCC
63.35-
573UbiquitinationGFSPKAQKEPCLFAN
CCCHHHCCCCCCCCC
69.36-
581PhosphorylationEPCLFANTEKLKAQL
CCCCCCCHHHHHHHH
30.9426074081
638UbiquitinationENLLEATKACKRQEV
HHHHHHHHHHHHHHH
59.85-
646PhosphorylationACKRQEVSQLNKIHA
HHHHHHHHHHHHHHH
28.3529449344
650UbiquitinationQEVSQLNKIHAETLK
HHHHHHHHHHHHHHH
44.45-
655PhosphorylationLNKIHAETLKIITTP
HHHHHHHHHHEEECC
33.8526074081
660PhosphorylationAETLKIITTPTKAYQ
HHHHHEEECCCCHHH
30.1424719451
661PhosphorylationETLKIITTPTKAYQL
HHHHEEECCCCHHHC
20.6726074081
663PhosphorylationLKIITTPTKAYQLHS
HHEEECCCCHHHCCC
26.6426074081
664UbiquitinationKIITTPTKAYQLHSR
HEEECCCCHHHCCCC
46.42-
666PhosphorylationITTPTKAYQLHSRPV
EECCCCHHHCCCCCC
17.1126074081
670PhosphorylationTKAYQLHSRPVPKLS
CCHHHCCCCCCCCCC
47.0426074081
677PhosphorylationSRPVPKLSPEMGSFG
CCCCCCCCCCCCCCC
25.5826074081
692PhosphorylationSLYTQNSSILDNDIL
CCCCCCCCCCCCCCC
34.4217081983
721PhosphorylationAISEELRTVQEQMSA
HHHHHHHHHHHHHHH
38.8820068231
726SulfoxidationLRTVQEQMSALQAKL
HHHHHHHHHHHHHHC
2.2021406390
727PhosphorylationRTVQEQMSALQAKLD
HHHHHHHHHHHHHCC
26.0620068231
742UbiquitinationEEEHKNLKLQQHVDK
HHHHHHHHHHHHHHH
54.35-
763PhosphorylationQMQELFSSERIDWTK
HHHHHHHHHCCCCHH
24.45-
777PhosphorylationKQQEELLSQLNVLEK
HHHHHHHHHHHHHHH
45.29-
792UbiquitinationQLQETQTKNDFLKSE
HHHHHHCHHHHHHHH
44.71-
797AcetylationQTKNDFLKSEVHDLR
HCHHHHHHHHHHHHH
44.5619608861
812AcetylationVVLHSADKELSSVKL
HHHHHCCCCHHCCEE
61.3423749302
860UbiquitinationNEKLLESKACLQDSY
CHHHHCCHHHHCCCC
33.47-
962PhosphorylationKVQKLEESLLATEKV
HHHHHHHHHHHHHHH
21.2224719451
968UbiquitinationESLLATEKVISSLEK
HHHHHHHHHHHHHHH
40.28-
976PhosphorylationVISSLEKSRDSDKKV
HHHHHHHCCCCCHHH
31.7624719451
979PhosphorylationSLEKSRDSDKKVVAD
HHHHCCCCCHHHHHH
50.6624719451
1009UbiquitinationTETIDTLKQELKDIN
CCCHHHHHHHHHHCC
43.7619608861
1009AcetylationTETIDTLKQELKDIN
CCCHHHHHHHHHHCC
43.7619608861
1013AcetylationDTLKQELKDINCKYN
HHHHHHHHHCCCCCC
56.6725953088
1018AcetylationELKDINCKYNSALVD
HHHHCCCCCCCCCCC
42.8725953088
1044UbiquitinationEVDILDLKETLRLRI
CCCEECHHHHHHHHH
48.60-
1046PhosphorylationDILDLKETLRLRILS
CEECHHHHHHHHHCC
18.65-
1053PhosphorylationTLRLRILSEDIERDM
HHHHHHCCHHHHHHC
30.7423312004
1076PhosphorylationTEQLNMLTEASKKHS
HHHHHHHHHHHHHHH
20.80-
1081UbiquitinationMLTEASKKHSGLLQS
HHHHHHHHHHCHHHH
40.27-
1083PhosphorylationTEASKKHSGLLQSAQ
HHHHHHHHCHHHHHH
39.7623663014
1088PhosphorylationKHSGLLQSAQEELTK
HHHCHHHHHHHHHHH
31.7123312004
1094PhosphorylationQSAQEELTKKEALIQ
HHHHHHHHHHHHHHH
43.2629083192
1134PhosphorylationQLEHVMDSAAEDPQS
HHHHHHHHHCCCCCC
15.9820068231
1141PhosphorylationSAAEDPQSPKTPPHF
HHCCCCCCCCCCHHH
33.4823401153
1144PhosphorylationEDPQSPKTPPHFQTH
CCCCCCCCCHHHHHH
45.4923401153
1150PhosphorylationKTPPHFQTHLAKLLE
CCCHHHHHHHHHHHH
20.2220873877
1158PhosphorylationHLAKLLETQEQEIED
HHHHHHHHHHHHHHC
37.0629255136
1169PhosphorylationEIEDGRASKTSLEHL
HHHCCCCCHHHHHHH
34.8029255136
1170UbiquitinationIEDGRASKTSLEHLV
HHCCCCCHHHHHHHH
40.94-
1171PhosphorylationEDGRASKTSLEHLVT
HCCCCCHHHHHHHHH
35.7321712546
1172PhosphorylationDGRASKTSLEHLVTK
CCCCCHHHHHHHHHH
35.1825159151
1178PhosphorylationTSLEHLVTKLNEDRE
HHHHHHHHHCCCCCH
35.8524719451
1179UbiquitinationSLEHLVTKLNEDREV
HHHHHHHHCCCCCHH
41.66-
1187UbiquitinationLNEDREVKNAEILRM
CCCCCHHCHHHHHHH
45.76-
1280UbiquitinationVQSALYNKEMECLRM
HHHHHHHCHHHHHHC
44.90-
1355PhosphorylationNLHQKIQYVVRLKKE
HHHHHHHHHHHHHHH
12.37-

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
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF15_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 KIF15_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLP3A_HUMANMAP1LC3Aphysical
16169070
CHD3_HUMANCHD3physical
16169070
VIME_HUMANVIMphysical
16169070
CE126_HUMANKIAA1377physical
16169070
DMD_HUMANDMDphysical
26496610
FANCG_HUMANFANCGphysical
26496610
MED6_HUMANMED6physical
26496610
CD2AP_HUMANCD2APphysical
26496610
PISD_HUMANPISDphysical
26496610
RENT2_HUMANUPF2physical
26496610
KBP_HUMANKIAA1279physical
26496610
K1143_HUMANKIAA1143physical
26496610
RM44_HUMANMRPL44physical
26496610
ELMO3_HUMANELMO3physical
26496610
MTNA_HUMANMRI1physical
26496610

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 KIF15_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-797 AND LYS-1009, AND MASSSPECTROMETRY.
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-568, AND MASSSPECTROMETRY.

TOP