KI16B_HUMAN - dbPTM
KI16B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KI16B_HUMAN
UniProt AC Q96L93
Protein Name Kinesin-like protein KIF16B
Gene Name KIF16B
Organism Homo sapiens (Human).
Sequence Length 1317
Subcellular Localization Cytoplasm, cytoskeleton . Early endosome membrane. It is unclear whether association with endosomes is mediated via phosphatidylinositol 3-phosphate (PtdIns(3)P)-binding or via its interaction with RAB14.
Protein Description Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development..
Protein Sequence MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAANTLAKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINEDANVKLIRELRAEIARLKTLLAQGNQIALLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTSADTMKDNEKLHNGTIQRKLKYERMVSRSLGANPDDLKDPIKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQSATSPLHINKVGLTLSKHTICEFSPFFKKGVFDYSSHGTG
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
31PhosphorylationFIIQMEKSKTTITNL
EEEEECCCCCEEEEE
23.17-
34PhosphorylationQMEKSKTTITNLKIP
EECCCCCEEEEEECC
29.55-
36PhosphorylationEKSKTTITNLKIPEG
CCCCCEEEEEECCCC
32.19-
45PhosphorylationLKIPEGGTGDSGRER
EECCCCCCCCCCCCE
48.9820068231
48PhosphorylationPEGGTGDSGRERTKT
CCCCCCCCCCCEEEE
40.8920068231
53PhosphorylationGDSGRERTKTFTYDF
CCCCCCEEEEEEEEE
29.6820068231
55PhosphorylationSGRERTKTFTYDFSF
CCCCEEEEEEEEEEE
22.1628270605
57PhosphorylationRERTKTFTYDFSFYS
CCEEEEEEEEEEEEE
27.6728270605
58PhosphorylationERTKTFTYDFSFYSA
CEEEEEEEEEEEEEC
15.7028270605
61PhosphorylationKTFTYDFSFYSADTK
EEEEEEEEEEECCCC
22.0028270605
72PhosphorylationADTKSPDYVSQEMVF
CCCCCCCCCCHHHHH
12.84-
84PhosphorylationMVFKTLGTDVVKSAF
HHHHHHCHHHHHHHH
28.8229396449
89PhosphorylationLGTDVVKSAFEGYNA
HCHHHHHHHHCCCCE
26.9530576142
106PhosphorylationFAYGQTGSGKSYTMM
EEECCCCCCCCEEEC
46.5730576142
109PhosphorylationGQTGSGKSYTMMGNS
CCCCCCCCEEECCCC
29.39-
110PhosphorylationQTGSGKSYTMMGNSG
CCCCCCCEEECCCCC
11.35-
111PhosphorylationTGSGKSYTMMGNSGD
CCCCCCEEECCCCCC
14.05-
119PhosphorylationMMGNSGDSGLIPRIC
ECCCCCCCCCHHHHH
38.7430576142
143PhosphorylationTTRWDEASFRTEVSY
CCCCCHHHCHHEEEH
17.1424719451
169PhosphorylationLRRKSSKTFNLRVRE
HHHCCCCCCCEEEEC
21.5028674151
211PhosphorylationAGNINRTTAATGMND
HCCCCCCCCCCCCCC
15.85-
220PhosphorylationATGMNDVSSRSHAIF
CCCCCCCCCCCEEEE
23.93-
240SulfoxidationQAKFDSEMPCETVSK
ECCCCCCCCCCEECE
5.5021406390
278PhosphorylationEGGNINKSLVTLGNV
CCCCCCHHHHHHHHH
24.4726434776
281PhosphorylationNINKSLVTLGNVISA
CCCHHHHHHHHHHHH
33.9526434776
287PhosphorylationVTLGNVISALADLSQ
HHHHHHHHHHHHCCH
16.9826434776
293PhosphorylationISALADLSQDAANTL
HHHHHHCCHHHHHHH
26.9326434776
299PhosphorylationLSQDAANTLAKKKQV
CCHHHHHHHHHCCCE
24.30-
316PhosphorylationPYRDSVLTWLLKDSL
ECHHHHHHHHHHHCC
16.35-
351PhosphorylationETLSTLRYANRAKNI
HHHHHHHHHHHHHCC
16.02-
398PhosphorylationNQIALLDSPTALSME
CEEEEECCHHHCCHH
24.9122199227
400PhosphorylationIALLDSPTALSMEEK
EEEECCHHHCCHHHH
44.1522199227
403PhosphorylationLDSPTALSMEEKLQQ
ECCHHHCCHHHHHHH
22.9922199227
420UbiquitinationARVQELTKEWTNKWN
HHHHHHHHHHHHHHH
64.97-
434AcetylationNETQNILKEQTLALR
HHHHHHHHHHHHHHH
43.937978727
442AcetylationEQTLALRKEGIGVVL
HHHHHHHHCCCEEEE
62.237978737
451PhosphorylationGIGVVLDSELPHLIG
CCEEEECCCCCHHCC
36.5530622161
465PhosphorylationGIDDDLLSTGIILYH
CCCHHHHCCCEEEEE
31.7030622161
466PhosphorylationIDDDLLSTGIILYHL
CCHHHHCCCEEEEEE
32.1630622161
471PhosphorylationLSTGIILYHLKEGQT
HCCCEEEEEECCCCE
8.4930622161
566PhosphorylationKLREKRKSGLLSSFS
HHHHHHHHCCHHHHC
38.4123403867
570PhosphorylationKRKSGLLSSFSLSMT
HHHHCCHHHHCCCCC
34.0923403867
571PhosphorylationRKSGLLSSFSLSMTD
HHHCCHHHHCCCCCC
20.8723403867
573PhosphorylationSGLLSSFSLSMTDLS
HCCHHHHCCCCCCHH
22.8326657352
575PhosphorylationLLSSFSLSMTDLSKS
CHHHHCCCCCCHHHC
20.5928102081
577PhosphorylationSSFSLSMTDLSKSRE
HHHCCCCCCHHHCCC
30.3422617229
580PhosphorylationSLSMTDLSKSRENLS
CCCCCCHHHCCCCCH
31.2523403867
582PhosphorylationSMTDLSKSRENLSAV
CCCCHHHCCCCCHHH
41.2630266825
587PhosphorylationSKSRENLSAVMLYNP
HHCCCCCHHHHHHCC
30.3330266825
592PhosphorylationNLSAVMLYNPGLEFE
CCHHHHHHCCCHHHH
10.9527732954
644PhosphorylationVETQRKETEIVQLQI
HHHHHHHHHHHHHHH
33.7628348404
657PhosphorylationQIRKQEESLKRRSFH
HHHHHHHHHHHHHHH
38.1427251275
662PhosphorylationEESLKRRSFHIENKL
HHHHHHHHHHHHHHH
25.8026657352
670TrimethylationFHIENKLKDLLAEKE
HHHHHHHHHHHHHHH
48.19-
670MethylationFHIENKLKDLLAEKE
HHHHHHHHHHHHHHH
48.19-
694UbiquitinationQQEIELQKKRQEEET
HHHHHHHHHHHHHHH
63.651720397
695UbiquitinationQEIELQKKRQEEETF
HHHHHHHHHHHHHHH
46.48-
713UbiquitinationQEELQRLKELNNNEK
HHHHHHHHHHCCCHH
63.44-
723UbiquitinationNNNEKAEKFQIFQEL
CCCHHHHHHHHHHHH
47.64-
749AcetylationAKLELEKKRLEEQEK
HHHHHHHHHHHHHHH
53.4911925873
772UbiquitinationLEEQLREKQEMIQLL
HHHHHHHHHHHHHHH
45.16-
800PhosphorylationDLEGIRESLLRVKEA
CCHHHHHHHHHHHHH
23.9023532336
820UbiquitinationEDGEELEKAQLRFFE
CCHHHHHHHHHHHHH
54.80-
847UbiquitinationEKDLVQQKDILKKEV
CHHHHHHHHHHHHHH
29.64-
852UbiquitinationQQKDILKKEVQEEQE
HHHHHHHHHHHHHHH
60.72-
881PhosphorylationLLEKHDESVTDVTEV
HHHHCCCCCCCCCCC
36.0525849741
883PhosphorylationEKHDESVTDVTEVPQ
HHCCCCCCCCCCCCC
33.7529396449
894UbiquitinationEVPQDFEKIKPVEYR
CCCCCHHHCCCCCHH
56.90-
924UbiquitinationLPTLLEEKQRAFEIL
HHHHHHHHHHHHHHH
35.39-
937PhosphorylationILDRGPLSLDNTLYQ
HHHCCCCCCCCHHHH
36.4926471730
941PhosphorylationGPLSLDNTLYQVEKE
CCCCCCCHHHHHHHH
26.8928509920
943PhosphorylationLSLDNTLYQVEKEME
CCCCCHHHHHHHHHH
14.4228509920
1017PhosphorylationARLERRHSALQRHST
HHHHHHHHHHHHHHH
28.9424732914
1023PhosphorylationHSALQRHSTLGMEIE
HHHHHHHHHHCCHHH
27.7628348404
1024PhosphorylationSALQRHSTLGMEIEE
HHHHHHHHHCCHHHH
22.6228348404
1035UbiquitinationEIEEQRQKLASLNSG
HHHHHHHHHHHCCCC
48.48-
1038PhosphorylationEQRQKLASLNSGSRE
HHHHHHHHCCCCCHH
38.2220068231
1041PhosphorylationQKLASLNSGSREQSG
HHHHHCCCCCHHHHH
43.3620068231
1043PhosphorylationLASLNSGSREQSGLQ
HHHCCCCCHHHHHHH
32.2520068231
1047PhosphorylationNSGSREQSGLQASLE
CCCCHHHHHHHHHHH
36.4025850435
1052PhosphorylationEQSGLQASLEAEQEA
HHHHHHHHHHHHHHH
17.4910997877
1062UbiquitinationAEQEALEKDQERLEY
HHHHHHHHHHHHHHH
66.61-
1069PhosphorylationKDQERLEYEIQQLKQ
HHHHHHHHHHHHHHH
23.9521945579
1075UbiquitinationEYEIQQLKQKIYEVD
HHHHHHHHHHHHEEC
45.25-
1079PhosphorylationQQLKQKIYEVDGVQK
HHHHHHHHEECCCCC
19.5525884760
1086UbiquitinationYEVDGVQKDHHGTLE
HEECCCCCCCCCCEE
57.53-
1095UbiquitinationHHGTLEGKVASSSLP
CCCCEEEEEECCCCC
25.83-
1098PhosphorylationTLEGKVASSSLPVSA
CEEEEEECCCCCCCC
24.3628348404
1099PhosphorylationLEGKVASSSLPVSAE
EEEEEECCCCCCCCC
26.5929255136
1100PhosphorylationEGKVASSSLPVSAEK
EEEEECCCCCCCCCH
33.9129255136
1104PhosphorylationASSSLPVSAEKSHLV
ECCCCCCCCCHHCCC
28.8629255136
1107UbiquitinationSLPVSAEKSHLVPLM
CCCCCCCHHCCCHHH
42.78-
1107 (in isoform 2)Ubiquitination-42.78-
1108PhosphorylationLPVSAEKSHLVPLMD
CCCCCCHHCCCHHHH
17.3521712546
1148SulfoxidationCSTSADTMKDNEKLH
CCCCCCCCCCCCHHC
5.4421406390
1149 (in isoform 2)Ubiquitination-60.54-
1172PhosphorylationYERMVSRSLGANPDD
HHHHHHHHCCCCHHH
24.5326657352
1181UbiquitinationGANPDDLKDPIKISI
CCCHHHCCCCCEEEC
69.33-
1187PhosphorylationLKDPIKISIPRYVLC
CCCCCEEECCCEEEE
22.8724719451
1191PhosphorylationIKISIPRYVLCGQGK
CEEECCCEEEECCCC
7.7529496907
1278PhosphorylationFFSVMLQSATSPLHI
HHHHHHHCCCCCCEE
29.56-
1280PhosphorylationSVMLQSATSPLHINK
HHHHHCCCCCCEECC
35.80-
1281PhosphorylationVMLQSATSPLHINKV
HHHHCCCCCCEECCC
25.77-
1291PhosphorylationHINKVGLTLSKHTIC
EECCCCEEECCCCCE
24.05-
1311PhosphorylationFKKGVFDYSSHGTG-
HCCCCCCCCCCCCC-
10.7027642862
1316PhosphorylationFDYSSHGTG------
CCCCCCCCC------
34.0027642862
1341 (in isoform 2)Phosphorylation-28348404

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 KI16B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KI16B_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 KI16B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MON1B_HUMANMON1Bphysical
28514442
CCZ1B_HUMANCCZ1physical
28514442
CCZ1_HUMANCCZ1physical
28514442
JIP4_HUMANSPAG9physical
28514442
CARM1_HUMANCARM1physical
28514442

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 KI16B_HUMAN

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Related Literatures of Post-Translational Modification

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