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Protein

Kinesin-1 heavy chain

Gene

KIF5B

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

Functioni

Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (PubMed:20386726).By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 92ATP8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMotor protein
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-264876. Insulin processing.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiP33176.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000170759.10.
HGNCiHGNC:6324. KIF5B.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

DisGeNETi3799.
OpenTargetsiENSG00000170759.
PharmGKBiPA30108.

Chemistry databases

ChEMBLiCHEMBL5864.

Polymorphism and mutation databases

BioMutaiKIF5B.
DMDMi417216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001253512 – 963Kinesin-1 heavy chainAdd BLAST962

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei933PhosphoserineCombined sources1
Modified residuei956Omega-N-methylarginineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP33176.
PaxDbiP33176.
PeptideAtlasiP33176.
PRIDEiP33176.

PTM databases

iPTMnetiP33176.
PhosphoSitePlusiP33176.
SwissPalmiP33176.

Expressioni

Gene expression databases

BgeeiENSG00000170759.
CleanExiHS_KIF5B.
ExpressionAtlasiP33176. baseline and differential.
GenevisibleiP33176. HS.

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. Interacts with ZFYVE27 (By similarity).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • JUN kinase binding Source: Ensembl
  • microtubule binding Source: HGNC
  • microtubule lateral binding Source: Ensembl

Protein-protein interaction databases

BioGridi110000. 110 interactors.
CORUMiP33176.
DIPiDIP-29244N.
IntActiP33176. 68 interactors.
MINTiMINT-4999704.
STRINGi9606.ENSP00000307078.

Chemistry databases

BindingDBiP33176.

Structurei

Secondary structure

1963
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Helixi20 – 25Combined sources6
Beta strandi32 – 34Combined sources3
Turni35 – 37Combined sources3
Beta strandi38 – 41Combined sources4
Beta strandi44 – 47Combined sources4
Beta strandi49 – 52Combined sources4
Helixi58 – 65Combined sources8
Helixi67 – 74Combined sources8
Beta strandi79 – 84Combined sources6
Helixi91 – 95Combined sources5
Turni102 – 104Combined sources3
Helixi107 – 122Combined sources16
Beta strandi124 – 138Combined sources15
Beta strandi141 – 146Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi163 – 165Combined sources3
Beta strandi171 – 173Combined sources3
Helixi176 – 189Combined sources14
Turni190 – 193Combined sources4
Helixi197 – 203Combined sources7
Beta strandi204 – 216Combined sources13
Turni217 – 219Combined sources3
Beta strandi222 – 231Combined sources10
Helixi238 – 241Combined sources4
Beta strandi242 – 244Combined sources3
Helixi256 – 269Combined sources14
Helixi277 – 279Combined sources3
Helixi281 – 285Combined sources5
Helixi286 – 288Combined sources3
Beta strandi290 – 293Combined sources4
Beta strandi295 – 302Combined sources8
Helixi306 – 308Combined sources3
Helixi309 – 320Combined sources12
Beta strandi326 – 329Combined sources4
Helixi337 – 348Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
3J8Xelectron microscopy5.00K1-349[»]
3J8Yelectron microscopy5.00K1-349[»]
4HNAX-ray3.19K1-349[»]
4LNUX-ray2.19K1-325[»]
5LT0X-ray2.00A1-325[»]
5LT1X-ray1.95A/B1-325[»]
5LT2X-ray2.60A/B/C/D/E/K1-325[»]
5LT3X-ray2.59A/B/C/D/E/K1-325[»]
5LT4X-ray2.88A/B/C/D/E/K1-325[»]
ProteinModelPortaliP33176.
SMRiP33176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 325Kinesin motorPROSITE-ProRule annotationAdd BLAST318

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni915 – 963GlobularAdd BLAST49

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili329 – 914Add BLAST586

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00890000139323.
HOVERGENiHBG006210.
InParanoidiP33176.
KOiK10396.
OMAiNDCAKKI.
OrthoDBiEOG091G02A2.
PhylomeDBiP33176.
TreeFamiTF105225.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiView protein in InterPro
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF00225. Kinesin. 1 hit.
PRINTSiPR00380. KINESINHEAVY.
SMARTiView protein in SMART
SM00129. KISc. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.

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. No translation available.
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.

Similar proteinsi

Entry informationi

Entry nameiKINH_HUMAN
AccessioniPrimary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 27, 2017
This is version 179 of the entry and version 1 of the sequence. See 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