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P48467

- KINH_NEUCR

UniProt

P48467 - KINH_NEUCR

Protein

Kinesin heavy chain

Gene

kin

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule's plus end.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 958ATP
    Nucleotide bindingi238 – 2458ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: InterPro

    GO - Biological processi

    1. microtubule-based movement Source: InterPro

    Keywords - Molecular functioni

    Motor protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin heavy chain
    Gene namesi
    Name:kin
    ORF Names:NCU09730
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 4, Linkage Group IV

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. kinesin complex Source: InterPro
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 928928Kinesin heavy chainPRO_0000125362Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5141.NCU09730.1.

    Structurei

    Secondary structure

    1
    928
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 146
    Helixi19 – 224
    Turni23 – 253
    Beta strandi30 – 323
    Beta strandi37 – 404
    Beta strandi47 – 504
    Beta strandi52 – 554
    Helixi61 – 688
    Helixi70 – 767
    Turni77 – 793
    Beta strandi82 – 876
    Helixi94 – 985
    Turni106 – 1083
    Helixi111 – 12414
    Beta strandi130 – 14213
    Beta strandi145 – 1484
    Beta strandi159 – 1624
    Turni163 – 1653
    Beta strandi166 – 1694
    Helixi180 – 20021
    Helixi205 – 2073
    Beta strandi209 – 22012
    Turni221 – 2233
    Beta strandi226 – 23510
    Beta strandi245 – 2473
    Turni252 – 2554
    Helixi256 – 2583
    Helixi261 – 27414
    Helixi282 – 2843
    Helixi286 – 2905
    Helixi292 – 2943
    Beta strandi300 – 3078
    Helixi311 – 3133
    Helixi314 – 32815
    Beta strandi338 – 3414
    Beta strandi343 – 3453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GOJX-ray2.30A1-355[»]
    ProteinModelPortaliP48467.
    SMRiP48467. Positions 2-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48467.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 330324Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili343 – 866524Sequence AnalysisAdd
    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.
    HOGENOMiHOG000216718.
    OMAiGTMRENE.
    OrthoDBiEOG7RRFGF.

    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.

    P48467-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSANSIKV VARFRPQNRV EIESGGQPIV TFQGPDTCTV DSKEAQGSFT    50
    FDRVFDMSCK QSDIFDFSIK PTVDDILNGY NGTVFAYGQT GAGKSYTMMG 100
    TSIDDPDGRG VIPRIVEQIF TSILSSAANI EYTVRVSYME IYMERIRDLL 150
    APQNDNLPVH EEKNRGVYVK GLLEIYVSSV QEVYEVMRRG GNARAVAATN 200
    MNQESSRSHS IFVITITQKN VETGSAKSGQ LFLVDLAGSE KVGKTGASGQ 250
    TLEEAKKINK SLSALGMVIN ALTDGKSSHV PYRDSKLTRI LQESLGGNSR 300
    TTLIINCSPS SYNDAETLST LRFGMRAKSI KNKAKVNAEL SPAELKQMLA 350
    KAKTQITSFE NYIVNLESEV QVWRGGETVP KEKWVPPLEL AITPSKSAST 400
    TARPSTPSRL LPESRAETPA ISDRAGTPSL PLDKDEREEF LRRENELQDQ 450
    IAEKESIAAA AERQLRETKE ELIALKDHDS KLGKENERLI SESNEFKMQL 500
    ERLAFENKEA QITIDGLKDA NSELTAELDE VKQQMLDMKM SAKETSAVLD 550
    EKEKKKAEKM AKMMAGFDLS GDVFSDNERA VADAIAQLDA LFEISSAGDA 600
    IPPEDIKALR EKLVETQGFV RQAELSSFSA ASSDAEARKR AELEARLEAL 650
    QQEHEELLSR NLTEADKEEV KALLAKSLSD KSAVQVELVE QLKADIALKN 700
    SETEHLKALV DDLQRRVKAG GAGVAMANGK TVQQQLAEFD VMKKSLMRDL 750
    QNRCERVVEL EISLDETREQ YNNVLRSSNN RAQQKKMAFL ERNLEQLTQV 800
    QRQLVEQNSA LKKEVAIAER KLMARNERIQ SLESLLQESQ EKMAQANHKF 850
    EVQLAAVKDR LEAAKAGSTR GLGTDAGLGG FSIGSRIAKP LRGGGDAVAG 900
    ATATNPTIAT LQQNPPENKR SSWFFQKS 928
    Length:928
    Mass (Da):102,411
    Last modified:July 15, 1999 - v2
    Checksum:i2E2475195F674C02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L47106 mRNA. Translation: AAB52961.1.
    CM002239 Genomic DNA. Translation: EAA35196.2.
    PIRiT10164.
    RefSeqiXP_964432.2. XM_959339.2.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000009500; EFNCRP00000009482; EFNCRG00000009481.
    GeneIDi3880594.
    KEGGincr:NCU09730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L47106 mRNA. Translation: AAB52961.1 .
    CM002239 Genomic DNA. Translation: EAA35196.2 .
    PIRi T10164.
    RefSeqi XP_964432.2. XM_959339.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GOJ X-ray 2.30 A 1-355 [» ]
    ProteinModelPortali P48467.
    SMRi P48467. Positions 2-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU09730.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000009500 ; EFNCRP00000009482 ; EFNCRG00000009481 .
    GeneIDi 3880594.
    KEGGi ncr:NCU09730.

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000216718.
    OMAi GTMRENE.
    OrthoDBi EOG7RRFGF.

    Miscellaneous databases

    EvolutionaryTracei P48467.

    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. "The Neurospora organelle motor: a distant relative of conventional kinesin with unconventional properties."
      Steinberg G., Schliwa M.
      Mol. Biol. Cell 6:1605-1618(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: 74A.
    2. Kirchner J.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    4. "Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules."
      Song Y.-H., Marx A., Muller J., Woehlke G., Schliwa M., Krebs A., Hoenger A., Mandelkow E.
      EMBO J. 20:6213-6225(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiKINH_NEUCR
    AccessioniPrimary (citable) accession number: P48467
    Secondary accession number(s): Q7RVK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3