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P33176

- KINH_HUMAN

UniProt

P33176 - KINH_HUMAN

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Protein

Kinesin-1 heavy chain

Gene

KIF5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 928ATP

GO - Molecular functioni

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. microtubule binding Source: HGNC
  4. microtubule motor activity Source: HGNC
  5. plus-end-directed microtubule motor activity Source: RefGenome

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. axon guidance Source: RefGenome
  3. cellular protein metabolic process Source: Reactome
  4. cytoplasm organization Source: Ensembl
  5. cytoskeleton-dependent intracellular transport Source: RefGenome
  6. microtubule-based movement Source: RefGenome
  7. plus-end-directed vesicle transport along microtubule Source: Ensembl
  8. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  9. positive regulation of potassium ion transport Source: BHF-UCL
  10. regulation of membrane potential Source: BHF-UCL
  11. stress granule disassembly Source: BHF-UCL
  12. vesicle transport along microtubule Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_15550. Insulin processing.
REACT_25201. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-1 heavy chain
Alternative name(s):
Conventional kinesin heavy chain
Ubiquitous kinesin heavy chain
Short name:
UKHC
Gene namesi
Name:KIF5B
Synonyms:KNS, KNS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:6324. KIF5B.

Subcellular locationi

Cytoplasmcytoskeleton By similarity
Note: Uniformly distributed between soma and neurites in hippocampal neurons.By similarity

GO - Cellular componenti

  1. ciliary rootlet Source: Ensembl
  2. cytoplasm Source: HPA
  3. endocytic vesicle Source: Ensembl
  4. kinesin complex Source: RefGenome
  5. membrane Source: UniProtKB
  6. microtubule Source: UniProtKB-KW
  7. microtubule organizing center Source: HPA
  8. neuron projection Source: Ensembl
  9. perinuclear region of cytoplasm Source: HGNC
  10. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 963962Kinesin-1 heavy chainPRO_0000125351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei933 – 9331Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33176.
PaxDbiP33176.
PRIDEiP33176.

PTM databases

PhosphoSiteiP33176.

Expressioni

Gene expression databases

BgeeiP33176.
CleanExiHS_KIF5B.
ExpressionAtlasiP33176. baseline and differential.
GenevestigatoriP33176.

Organism-specific databases

HPAiCAB009846.
HPA037589.
HPA037590.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VACWR159P686193EBI-355878,EBI-7133540From a different organism.

Protein-protein interaction databases

BioGridi110000. 75 interactions.
DIPiDIP-29244N.
IntActiP33176. 22 interactions.
MINTiMINT-4999704.
STRINGi9606.ENSP00000307078.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Helixi20 – 256Combined sources
Beta strandi32 – 343Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 524Combined sources
Helixi58 – 658Combined sources
Helixi67 – 748Combined sources
Beta strandi79 – 846Combined sources
Helixi91 – 955Combined sources
Turni102 – 1043Combined sources
Helixi107 – 12216Combined sources
Beta strandi124 – 13815Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 18914Combined sources
Turni190 – 1934Combined sources
Helixi197 – 2037Combined sources
Beta strandi204 – 21613Combined sources
Turni217 – 2193Combined sources
Beta strandi222 – 23110Combined sources
Helixi238 – 2414Combined sources
Beta strandi242 – 2443Combined sources
Helixi256 – 26914Combined sources
Helixi277 – 2793Combined sources
Helixi281 – 2855Combined sources
Helixi286 – 2883Combined sources
Beta strandi290 – 2934Combined sources
Beta strandi295 – 3028Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 32012Combined sources
Beta strandi326 – 3294Combined sources
Helixi337 – 34812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
4HNAX-ray3.19K1-349[»]
ProteinModelPortaliP33176.
SMRiP33176. Positions 3-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 325318Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni915 – 96349GlobularAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili329 – 914586Add
BLAST

Domaini

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 similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG006210.
InParanoidiP33176.
KOiK10396.
OMAiLAECNIK.
OrthoDBiEOG7T4MJD.
PhylomeDBiP33176.
TreeFamiTF105225.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33176-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR
60 70 80 90 100
VFQSSTSQEQ VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH
110 120 130 140 150
DPEGMGIIPR IVQDIFNYIY SMDENLEFHI KVSYFEIYLD KIRDLLDVSK
160 170 180 190 200
TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM DTIDEGKSNR HVAVTNMNEH
210 220 230 240 250
SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK TGAEGAVLDE
260 270 280 290 300
AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI
310 320 330 340 350
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK
360 370 380 390 400
NKILRNTIQW LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN
410 420 430 440 450
DKPATAIGVI GNFTDAERRK CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK
460 470 480 490 500
TQMLDQEELL ASTRRDQDNM QAELNRLQAE NDASKEEVKE VLQALEELAV
510 520 530 540 550
NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL KEMTNHQKKR
560 570 580 590 600
AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE
610 620 630 640 650
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL
660 670 680 690 700
QNVEQKKRQL EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA
710 720 730 740 750
VEQQIQSHRE THQKQISSLR DEVEAKAKLI TDLQDQNQKM MLEQERLRVE
760 770 780 790 800
HEKLKATDQE KSRKLHELTV MQDRREQARQ DLKGLEETVA KELQTLHNLR
810 820 830 840 850
KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE QLTKVHKQLV
860 870 880 890 900
RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD
910 920 930 940 950
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS
960
QPVAVRGGGG KQV
Length:963
Mass (Da):109,685
Last modified:October 1, 1993 - v1
Checksum:iA1FE5760C3250C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.
CCDSiCCDS7171.1.
PIRiA41919.
RefSeqiNP_004512.1. NM_004521.2.
UniGeneiHs.327736.

Genome annotation databases

EnsembliENST00000302418; ENSP00000307078; ENSG00000170759.
GeneIDi3799.
KEGGihsa:3799.
UCSCiuc001iwe.4. human.

Polymorphism databases

DMDMi417216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65873 mRNA. Translation: CAA46703.1 .
AL161932 Genomic DNA. Translation: CAH71618.1 .
BC126279 mRNA. Translation: AAI26280.1 .
BC126281 mRNA. Translation: AAI26282.1 .
CCDSi CCDS7171.1.
PIRi A41919.
RefSeqi NP_004512.1. NM_004521.2.
UniGenei Hs.327736.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4HNA X-ray 3.19 K 1-349 [» ]
ProteinModelPortali P33176.
SMRi P33176. Positions 3-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110000. 75 interactions.
DIPi DIP-29244N.
IntActi P33176. 22 interactions.
MINTi MINT-4999704.
STRINGi 9606.ENSP00000307078.

Chemistry

BindingDBi P33176.
ChEMBLi CHEMBL5864.

PTM databases

PhosphoSitei P33176.

Polymorphism databases

DMDMi 417216.

Proteomic databases

MaxQBi P33176.
PaxDbi P33176.
PRIDEi P33176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302418 ; ENSP00000307078 ; ENSG00000170759 .
GeneIDi 3799.
KEGGi hsa:3799.
UCSCi uc001iwe.4. human.

Organism-specific databases

CTDi 3799.
GeneCardsi GC10M032340.
HGNCi HGNC:6324. KIF5B.
HPAi CAB009846.
HPA037589.
HPA037590.
MIMi 602809. gene.
neXtProti NX_P33176.
PharmGKBi PA30108.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
HOVERGENi HBG006210.
InParanoidi P33176.
KOi K10396.
OMAi LAECNIK.
OrthoDBi EOG7T4MJD.
PhylomeDBi P33176.
TreeFami TF105225.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_15550. Insulin processing.
REACT_25201. Kinesins.

Miscellaneous databases

ChiTaRSi KIF5B. human.
EvolutionaryTracei P33176.
GeneWikii KIF5B.
GenomeRNAii 3799.
NextBioi 14917.
PROi P33176.
SOURCEi Search...

Gene expression databases

Bgeei P33176.
CleanExi HS_KIF5B.
ExpressionAtlasi P33176. baseline and differential.
Genevestigatori P33176.

Family and domain databases

Gene3Di 3.40.850.10. 1 hit.
InterProi IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.
  15. "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.
  16. "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.

Entry informationi

Entry nameiKINH_HUMAN
AccessioniPrimary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3