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P33176

- KINH_HUMAN

UniProt

P33176 - KINH_HUMAN

Protein

Kinesin-1 heavy chain

Gene

KIF5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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. ATP binding Source: UniProtKB-KW
    2. microtubule binding Source: HGNC
    3. microtubule motor activity Source: HGNC
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cytoplasm organization Source: Ensembl
    3. microtubule-based movement Source: ProtInc
    4. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    5. positive regulation of potassium ion transport Source: BHF-UCL
    6. regulation of membrane potential Source: BHF-UCL
    7. stress granule disassembly Source: BHF-UCL
    8. vesicle transport along microtubule Source: HGNC

    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. kinesin complex Source: ProtInc
    4. membrane Source: UniProtKB
    5. microtubule Source: UniProtKB-KW
    6. microtubule organizing center Source: HPA
    7. neuron projection Source: Ensembl
    8. perinuclear region of cytoplasm Source: HGNC
    9. vesicle Source: UniProtKB

    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

    ArrayExpressiP33176.
    BgeeiP33176.
    CleanExiHS_KIF5B.
    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. 64 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 – 158
    Helixi20 – 256
    Beta strandi32 – 343
    Turni35 – 373
    Beta strandi38 – 414
    Beta strandi44 – 474
    Beta strandi49 – 524
    Helixi58 – 658
    Helixi67 – 748
    Beta strandi79 – 846
    Helixi91 – 955
    Turni102 – 1043
    Helixi107 – 12216
    Beta strandi124 – 13815
    Beta strandi141 – 1466
    Beta strandi155 – 1573
    Beta strandi163 – 1653
    Beta strandi171 – 1733
    Helixi176 – 18914
    Turni190 – 1934
    Helixi197 – 2037
    Beta strandi204 – 21613
    Turni217 – 2193
    Beta strandi222 – 23110
    Helixi238 – 2414
    Beta strandi242 – 2443
    Helixi256 – 26914
    Helixi277 – 2793
    Helixi281 – 2855
    Helixi286 – 2883
    Beta strandi290 – 2934
    Beta strandi295 – 3028
    Helixi306 – 3083
    Helixi309 – 32012
    Beta strandi326 – 3294
    Helixi337 – 34812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR    50
    VFQSSTSQEQ VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH 100
    DPEGMGIIPR IVQDIFNYIY SMDENLEFHI KVSYFEIYLD KIRDLLDVSK 150
    TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM DTIDEGKSNR HVAVTNMNEH 200
    SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK TGAEGAVLDE 250
    AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI 300
    CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK 350
    NKILRNTIQW LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN 400
    DKPATAIGVI GNFTDAERRK CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK 450
    TQMLDQEELL ASTRRDQDNM QAELNRLQAE NDASKEEVKE VLQALEELAV 500
    NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL KEMTNHQKKR 550
    AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE 600
    VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL 650
    QNVEQKKRQL EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA 700
    VEQQIQSHRE THQKQISSLR DEVEAKAKLI TDLQDQNQKM MLEQERLRVE 750
    HEKLKATDQE KSRKLHELTV MQDRREQARQ DLKGLEETVA KELQTLHNLR 800
    KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE QLTKVHKQLV 850
    RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD 900
    RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS 950
    QPVAVRGGGG KQV 963
    Length:963
    Mass (Da):109,685
    Last modified:October 1, 1993 - v1
    Checksum:iA1FE5760C3250C8B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 64 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

    ArrayExpressi P33176.
    Bgeei P33176.
    CleanExi HS_KIF5B.
    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

    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: October 1, 2014
    This is version 146 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