P33176 (KINH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-1 heavy chain

Alternative name(s):
Conventional kinesin heavy chain
Ubiquitous kinesin heavy chain
Short name=UKHC

Gene names

Name:	KIF5B
Synonyms:	KNS, KNS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	963 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes By similarity.
Subunit structure	Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 By similarity. Interacts with SYBU. Interacts with JAKMIP1. Interacts with PLEKHM2. Interacts with ECM29. Ref.4 Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm › cytoskeleton By similarity. Note: Uniformly distributed between soma and neurites in hippocampal neurons By similarity.
Domain	Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.
Sequence similarities	Belongs to the kinesin-like protein family. Kinesin subfamily. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasm organization Inferred from electronic annotation. Source: Compara positive regulation of establishment of protein localization to plasma membrane Inferred from direct assay PubMed 19675065. Source: BHF-UCL positive regulation of potassium ion transport Inferred from direct assay PubMed 19675065. Source: BHF-UCL regulation of membrane potential Inferred from direct assay PubMed 19675065. Source: BHF-UCL stress granule disassembly Inferred from sequence or structural similarity. Source: BHF-UCL vesicle transport along microtubule Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	ciliary rootlet Inferred from electronic annotation. Source: Compara kinesin complex Traceable author statement Ref.1. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: HGNC vesicle Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from sequence or structural similarity. Source: HGNC microtubule motor activity Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 963

963

Kinesin-1 heavy chain

PRO_0000125351

Regions

Domain

2 – 328

327

Kinesin-motor

Nucleotide binding

85 – 92

8

ATP

Region

915 – 963

49

Globular

Coiled coil

329 – 914

586

Amino acid modifications

Modified residue

933

1

Phosphoserine Ref.9

Secondary structure

1

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963

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Helix

20 – 25

6

Beta strand

32 – 34

3

Turn

35 – 37

3

Beta strand

38 – 41

4

Beta strand

44 – 47

4

Beta strand

49 – 52

4

Helix

58 – 65

8

Helix

67 – 74

8

Beta strand

79 – 84

6

Helix

91 – 95

5

Turn

102 – 104

3

Helix

107 – 122

16

Beta strand

124 – 138

15

Beta strand

141 – 146

6

Beta strand

155 – 157

3

Beta strand

163 – 165

3

Beta strand

171 – 173

3

Helix

176 – 189

14

Turn

190 – 193

4

Helix

197 – 203

7

Beta strand

204 – 216

13

Turn

217 – 219

3

Beta strand

222 – 231

10

Beta strand

242 – 244

3

Helix

256 – 269

14

Helix

277 – 279

3

Helix

281 – 285

5

Helix

286 – 288

3

Beta strand

290 – 293

4

Beta strand

295 – 302

8

Helix

306 – 308

3

Helix

309 – 320

12

Beta strand

326 – 329

4

Helix

337 – 348

12

Sequences

	Sequence		Length	Mass (Da)
	P33176 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: A1FE5760C3250C8B	FASTA	963	109,685
	10 20 30 40 50 60 MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR VFQSSTSQEQ 70 80 90 100 110 120 VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH DPEGMGIIPR IVQDIFNYIY 130 140 150 160 170 180 SMDENLEFHI KVSYFEIYLD KIRDLLDVSK TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM 190 200 210 220 230 240 DTIDEGKSNR HVAVTNMNEH SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK 250 260 270 280 290 300 TGAEGAVLDE AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI 310 320 330 340 350 360 CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK NKILRNTIQW 370 380 390 400 410 420 LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN DKPATAIGVI GNFTDAERRK 430 440 450 460 470 480 CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK TQMLDQEELL ASTRRDQDNM QAELNRLQAE 490 500 510 520 530 540 NDASKEEVKE VLQALEELAV NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL 550 560 570 580 590 600 KEMTNHQKKR AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE 610 620 630 640 650 660 VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL QNVEQKKRQL 670 680 690 700 710 720 EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR 730 740 750 760 770 780 DEVEAKAKLI TDLQDQNQKM MLEQERLRVE HEKLKATDQE KSRKLHELTV MQDRREQARQ 790 800 810 820 830 840 DLKGLEETVA KELQTLHNLR KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE 850 860 870 880 890 900 QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD 910 920 930 940 950 960 RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS QPVAVRGGGG KQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells." Navone F., Niclas J., Hom-Booher N., Sparks L., Bernstein H.D., McCaffrey G., Vale R.D. J. Cell Biol. 117:1263-1275(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons." Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H. Nat. Cell Biol. 6:941-953(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYBU.
[5]	"The intracellular fate of Salmonella depends on the recruitment of kinesin." Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S. Science 308:1174-1178(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLEKHM2.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport." Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S., Couve A. Mol. Cell. Neurosci. 35:501-512(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JAKMIP1.
[8]	"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components." Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M. J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ECM29.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Crystal structure of the kinesin motor domain reveals a structural similarity to myosin." Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D. Nature 380:550-555(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
[12]	"Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy." Sindelar C.V., Budny M.J., Rice S., Naber N., Fletterick R., Cooke R. Nat. Struct. Biol. 9:844-848(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
[13]	"The beginning of kinesin's force-generating cycle visualized at 9-A resolution." Sindelar C.V., Downing K.H. J. Cell Biol. 177:377-385(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 1-325.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.

IPI

IPI00012837.

PIR

A41919.

RefSeq

NP_004512.1. NM_004521.2.

UniGene

Hs.327736.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BG2	X-ray	1.80	A	1-325	[»]
1MKJ	X-ray	2.70	A	1-349	[»]
2P4N	electron microscopy	9.00	K	1-325	[»]

ProteinModelPortal

P33176.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29244N.

IntAct

P33176. 16 interactions.

MINT

MINT-4999704.

STRING

9606.ENSP00000307078.

PTM databases

PhosphoSite

P33176.

Polymorphism databases

DMDM

417216.

Proteomic databases

PaxDb

P33176.

PRIDE

P33176.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302418; ENSP00000307078; ENSG00000170759.

GeneID

3799.

KEGG

hsa:3799.

UCSC

uc001iwe.4. human.

Organism-specific databases

CTD

3799.

GeneCards

GC10M032340.

HGNC

HGNC:6324. KIF5B.

HPA

CAB009846.

MIM

602809. gene.

neXtProt

NX_P33176.

PharmGKB

PA30108.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOVERGEN

HBG006210.

InParanoid

P33176.

KO

K10396.

OMA

LAECNIK.

OrthoDB

EOG405S0B.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P33176.

Bgee

P33176.

CleanEx

HS_KIF5B.

Genevestigator

P33176.

GermOnline

ENSG00000170759. Homo sapiens.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P33176.

ChEMBL

CHEMBL5864.

ChiTaRS

KIF5B. human.

EvolutionaryTrace

P33176.

GenomeRNAi

3799.

NextBio

14917.

SOURCE

Search...

Entry information

Entry name

KINH_HUMAN

Accession

Primary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.