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P48467

- KINH_NEUCR

UniProt

P48467 - KINH_NEUCR

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 146Combined sources
Helixi19 – 224Combined sources
Turni23 – 253Combined sources
Beta strandi30 – 323Combined sources
Beta strandi37 – 404Combined sources
Beta strandi47 – 504Combined sources
Beta strandi52 – 554Combined sources
Helixi61 – 688Combined sources
Helixi70 – 767Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 876Combined sources
Helixi94 – 985Combined sources
Turni106 – 1083Combined sources
Helixi111 – 12414Combined sources
Beta strandi130 – 14213Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi159 – 1624Combined sources
Turni163 – 1653Combined sources
Beta strandi166 – 1694Combined sources
Helixi180 – 20021Combined sources
Helixi205 – 2073Combined sources
Beta strandi209 – 22012Combined sources
Turni221 – 2233Combined sources
Beta strandi226 – 23510Combined sources
Beta strandi245 – 2473Combined sources
Turni252 – 2554Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 27414Combined sources
Helixi282 – 2843Combined sources
Helixi286 – 2905Combined sources
Helixi292 – 2943Combined sources
Beta strandi300 – 3078Combined sources
Helixi311 – 3133Combined sources
Helixi314 – 32815Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi343 – 3453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP48467.
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

        10         20         30         40         50
MSSSANSIKV VARFRPQNRV EIESGGQPIV TFQGPDTCTV DSKEAQGSFT
60 70 80 90 100
FDRVFDMSCK QSDIFDFSIK PTVDDILNGY NGTVFAYGQT GAGKSYTMMG
110 120 130 140 150
TSIDDPDGRG VIPRIVEQIF TSILSSAANI EYTVRVSYME IYMERIRDLL
160 170 180 190 200
APQNDNLPVH EEKNRGVYVK GLLEIYVSSV QEVYEVMRRG GNARAVAATN
210 220 230 240 250
MNQESSRSHS IFVITITQKN VETGSAKSGQ LFLVDLAGSE KVGKTGASGQ
260 270 280 290 300
TLEEAKKINK SLSALGMVIN ALTDGKSSHV PYRDSKLTRI LQESLGGNSR
310 320 330 340 350
TTLIINCSPS SYNDAETLST LRFGMRAKSI KNKAKVNAEL SPAELKQMLA
360 370 380 390 400
KAKTQITSFE NYIVNLESEV QVWRGGETVP KEKWVPPLEL AITPSKSAST
410 420 430 440 450
TARPSTPSRL LPESRAETPA ISDRAGTPSL PLDKDEREEF LRRENELQDQ
460 470 480 490 500
IAEKESIAAA AERQLRETKE ELIALKDHDS KLGKENERLI SESNEFKMQL
510 520 530 540 550
ERLAFENKEA QITIDGLKDA NSELTAELDE VKQQMLDMKM SAKETSAVLD
560 570 580 590 600
EKEKKKAEKM AKMMAGFDLS GDVFSDNERA VADAIAQLDA LFEISSAGDA
610 620 630 640 650
IPPEDIKALR EKLVETQGFV RQAELSSFSA ASSDAEARKR AELEARLEAL
660 670 680 690 700
QQEHEELLSR NLTEADKEEV KALLAKSLSD KSAVQVELVE QLKADIALKN
710 720 730 740 750
SETEHLKALV DDLQRRVKAG GAGVAMANGK TVQQQLAEFD VMKKSLMRDL
760 770 780 790 800
QNRCERVVEL EISLDETREQ YNNVLRSSNN RAQQKKMAFL ERNLEQLTQV
810 820 830 840 850
QRQLVEQNSA LKKEVAIAER KLMARNERIQ SLESLLQESQ EKMAQANHKF
860 870 880 890 900
EVQLAAVKDR LEAAKAGSTR GLGTDAGLGG FSIGSRIAKP LRGGGDAVAG
910 920
ATATNPTIAT LQQNPPENKR SSWFFQKS
Length:928
Mass (Da):102,411
Last modified:July 15, 1999 - v2
Checksum:i2E2475195F674C02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P48467.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 100 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