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Protein

Kinesin heavy chain isoform 5A

Gene

Kif5a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 938ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • microtubule motor activity Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • microtubule-based movement Source: InterPro
  • microtubule-based process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin heavy chain isoform 5A
Alternative name(s):
Kinesin heavy chain neuron-specific 1
Neuronal kinesin heavy chain
Short name:
NKHC
Gene namesi
Name:Kif5aImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303035. Kif5a.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • kinesin complex Source: RGD
  • microtubule Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10271026Kinesin heavy chain isoform 5APRO_0000251143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei397 – 3971PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6QLM7.
PRIDEiQ6QLM7.

Expressioni

Tissue specificityi

Expressed in brain.1 Publication

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

DIPiDIP-46364N.
IntActiQ6QLM7. 1 interaction.
STRINGi10116.ENSRNOP00000007721.

Structurei

Secondary structure

1
1027
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi254 – 2563Combined sources
Helixi257 – 27115Combined sources
Helixi279 – 2813Combined sources
Helixi283 – 2875Combined sources
Helixi289 – 2935Combined sources
Beta strandi294 – 30411Combined sources
Helixi308 – 3103Combined sources
Helixi311 – 32515Combined sources
Beta strandi328 – 3314Combined sources
Beta strandi334 – 3363Combined sources
Helixi339 – 35012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KINX-ray2.00B252-351[»]
3KINX-ray3.10B/D256-372[»]
ProteinModelPortaliQ6QLM7.
SMRiQ6QLM7. Positions 7-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6QLM7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 327319Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 315142Microtubule-bindingSequence analysisAdd
BLAST
Regioni907 – 1027121GlobularSequence analysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili331 – 905575Sequence 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.Curated

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

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000216718.
HOVERGENiHBG006210.
InParanoidiQ6QLM7.
KOiK10396.
PhylomeDBiQ6QLM7.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
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.
PROSITEiPS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6QLM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD
60 70 80 90 100
RVFPPNTTQE QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL
110 120 130 140 150
HDPQLMGIIP RIARDIFNHI YSMDENLEFH IKVSYFEIYL DKIRDLLDVT
160 170 180 190 200
KTNLSVHEDK NRVPFVRGCT ERFVSSPEEI LDVIDEGKSN RHVAVTNMNE
210 220 230 240 250
HSSRSHSIFL INIKQENIET EQKLSGKLYL ADLAGSEKVS KTGAEGAVLD
260 270 280 290 300
EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
310 320 330 340 350
FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK
360 370 380 390 400
EKTKAQKETI AKLEAELSRW RNGENVPETE RLAGEDSALA AEICEETPVN
410 420 430 440 450
DNSSIVVRIA PEERQKYEEE IRRLYKQLDD KDDEINQQSQ LIEKLKQQML
460 470 480 490 500
DQEELLVSTR GDNEKVQREL SHLQSENDAA KEEVKEVLQA LEELAVNYDQ
510 520 530 540 550
KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SEPQRLQEVS GHQRKRIAEV
560 570 580 590 600
LNGLMKDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
610 620 630 640 650
VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV
660 670 680 690 700
ELKKRHLEES YDSLSDELAK LQAQETVHEV ALKDKEPDTQ DAEEVKKALE
710 720 730 740 750
LQMENHREAH HRQLARLRDE INEKQKTIDE LKDLDQKLQL ELEKLQADYE
760 770 780 790 800
RLKNEENEKS AKLQELTFLY ERHEQSKQDL KGLEETVARE LQTLHNLRKL
810 820 830 840 850
FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL TEVHKQLVRD
860 870 880 890 900
NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
910 920 930 940 950
KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL
960 970 980 990 1000
FQNYQNLHLQ AAPSSTSDVY FASNGATSVA PLASYQKANT DNGNATDIND
1010 1020
NRSDLPCGYE AEDPAKLFPL HQETAAS
Length:1,027
Mass (Da):116,916
Last modified:July 5, 2004 - v1
Checksum:i2068CCC4E05A24CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY535015 mRNA. Translation: AAS45402.1.
RefSeqiNP_997688.1. NM_212523.1.
UniGeneiRn.63144.

Genome annotation databases

GeneIDi314906.
KEGGirno:314906.
UCSCiRGD:1303035. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY535015 mRNA. Translation: AAS45402.1.
RefSeqiNP_997688.1. NM_212523.1.
UniGeneiRn.63144.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KINX-ray2.00B252-351[»]
3KINX-ray3.10B/D256-372[»]
ProteinModelPortaliQ6QLM7.
SMRiQ6QLM7. Positions 7-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46364N.
IntActiQ6QLM7. 1 interaction.
STRINGi10116.ENSRNOP00000007721.

Proteomic databases

PaxDbiQ6QLM7.
PRIDEiQ6QLM7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi314906.
KEGGirno:314906.
UCSCiRGD:1303035. rat.

Organism-specific databases

CTDi3798.
RGDi1303035. Kif5a.

Phylogenomic databases

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000216718.
HOVERGENiHBG006210.
InParanoidiQ6QLM7.
KOiK10396.
PhylomeDBiQ6QLM7.

Miscellaneous databases

EvolutionaryTraceiQ6QLM7.
PROiQ6QLM7.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
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.
PROSITEiPS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Taylor A.G., Miyashiro K., Eberwine J., Meaney D.F.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-DawleyImported.
  2. "Cloning and localization of a conventional kinesin motor expressed exclusively in neurons."
    Niclas J., Navone F., Hom-Booher N., Vale R.D.
    Neuron 12:1059-1072(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "X-ray structure of motor and neck domains from rat brain kinesin."
    Sack S., Mueller J., Marx A., Thormaehlen M., Mandelkow E.M., Brady S.T., Mandelkow E.
    Biochemistry 36:16155-16165(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 252-351 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiKIF5A_RAT
AccessioniPrimary (citable) accession number: Q6QLM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.