Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Kinesin-1 heavy chain  

UniProtKB / Swiss-Prot ID :  KINH_HUMAN

Gene Name (Synonyms) : 
KIF5B, KNS, KNS1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton (By similarity). Note=Uniformly distributed between soma and neurites in hippocampal neurons (By similarity). 

Protein Function :  Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity). 

Protein Sequence MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIV...
Predicted Secondary Structure CCCCCCCCEEEEEEECCCCHHHHHCCCCEEEEECCCCEEEECCCEEEECEEECCCCCHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADLAE
---CCCCCC
22.11UniProtKB
Link
28N6-acetyllysineNRGDKYIAK
HCCCCEEEE
41.18HPRD
Link
28N6-acetyllysineNRGDKYIAK
HCCCCEEEE
41.18Phosphositeplus
Link
166N6-acetyllysineVPYVKGCTE
CEEECCCEE
42.28HPRD
Link
166N6-acetyllysine.VPYVKGCTE
CEEECCCEE
42.28UniProtKB
Link
222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QTEQKLSGK
CCCCEEEEE
38.09Phosphositeplus
Link
649PhosphotyrosineSLTEYLQNV
HHHHHHHHH
14.35Phosphositeplus
Link-
761N6-acetyllysineTDQEKSRKL
HHHHHHHHH
50.34Phosphositeplus
Link-
764N6-acetyllysineEKSRKLHEL
HHHHHHHHH
62.38Phosphositeplus
Link-
783Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RQDLKGLEE
HHHCCHHHH
70.51Phosphositeplus
Link-
917PhosphoserineRRGHSAQIA
HCCCCCHHC
25.37HPRD
Link-
933PhosphoserineHPAASPTHP
CCCCCCCCC
32.22HPRD
Link-
933PhosphoserineHPAASPTHP
CCCCCCCCC
32.22PhosphoELM
Link-
933PhosphoserineHPAASPTHP
CCCCCCCCC
32.22Phosphositeplus
Link-
933PhosphoserineHPAASPTHP
CCCCCCCCC
32.22SysPTM
Link-
933Phosphoserine.HPAASPTHP
CCCCCCCCC
32.22UniProtKB
Link-
935PhosphothreonineAASPTHPSA
CCCCCCCCC
43.88HPRD
Link-
935PhosphothreonineAASPTHPSA
CCCCCCCCC
43.88PhosphoELM
Link-
935PhosphothreonineAASPTHPSA
CCCCCCCCC
43.88SysPTM
Link-
938PhosphoserinePTHPSAIRG
CCCCCCCCC
28.82HPRD
Link-
938PhosphoserinePTHPSAIRG
CCCCCCCCC
28.82Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-51009MINT15324660
1433Z_HUMANphysical interactionMINT-3297642MINT15161933
NEMO_HUMANphysical interactionMINT-48157MINT14743216
KINH_HUMANdirect interactionDIP:57268EDIP17013387
CDC5L_HUMANphysical interactionEBI-1105991
intact17043677
1433T_HUMANin vivoHPRD:07214HPRD15324660
KLC3_HUMANin vivoHPRD:07214HPRD10491391
SNP25_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07214HPRD12475239
KTN1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07214HPRD10913441
SNP23_HUMANin vitro
yeast 2-hybrid
HPRD:07214HPRD12475239
1433G_HUMANin vivoHPRD:07214HPRD15324660
EIF3A_HUMANin vitro
yeast 2-hybrid
HPRD:07214HPRD15184079
KIF5A_HUMANENSP00000307078STRING
KLC2_HUMANENSP00000307078STRING
KLC3_HUMANENSP00000307078STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-933, AND MASS SPECTROMETRY.
"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-166, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-933, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures