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Kinesin-like protein KIF1A (Axonal transporter of synaptic vesicles) (Microtubule-based motor KIF1A) (Unc-104- and KIF1A-related protein) (hUnc-104)

 KIF1A_HUMAN             Reviewed;        1690 AA.
Q12756; B0I1S5; F5H045; O95068; Q13355; Q14752; Q2NKJ6; Q4LE42;
Q53T78; Q59GH1; Q63Z40; Q6P1R9; Q7KZ57;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
10-OCT-2018, entry version 172.
RecName: Full=Kinesin-like protein KIF1A;
AltName: Full=Axonal transporter of synaptic vesicles;
AltName: Full=Microtubule-based motor KIF1A;
AltName: Full=Unc-104- and KIF1A-related protein;
Short=hUnc-104;
Name=KIF1A; Synonyms=ATSV, C2orf20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8661001; DOI=10.1006/geno.1996.0217;
Furlong R.A., Zhou C.Y., Ferguson-Smith M.A., Affara N.A.;
"Characterization of a kinesin-related gene ATSV, within the tuberous
sclerosis locus (TSC1) candidate region on chromosome 9q34.";
Genomics 33:421-429(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
recombination: preparation of full-length cDNA clones encoding motor
proteins.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1362 (ISOFORM 2).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 102-251.
TISSUE=Retina;
Bost-Usinger L., Hoang E.H.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 882-1690 (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1690 (ISOFORM 1).
TISSUE=Brain;
Campagna S.E., Otsuka A.J.;
"A putative human kinesin family member with sequence similarity to
unc-104 and KIF1A.";
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1275-1690 (ISOFORM 1).
TISSUE=Brain;
Yu W., Sarginson J., Gibbs R.A.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1318-1690 (ISOFORM 1).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
INVOLVEMENT IN HSN2C.
PubMed=21820098; DOI=10.1016/j.ajhg.2011.06.013;
Riviere J.B., Ramalingam S., Lavastre V., Shekarabi M., Holbert S.,
Lafontaine J., Srour M., Merner N., Rochefort D., Hince P., Gaudet R.,
Mes-Masson A.M., Baets J., Houlden H., Brais B., Nicholson G.A.,
Van Esch H., Nafissi S., De Jonghe P., Reilly M.M., Timmerman V.,
Dion P.A., Rouleau G.A.;
"KIF1A, an axonal transporter of synaptic vesicles, is mutated in
hereditary sensory and autonomic neuropathy type 2.";
Am. J. Hum. Genet. 89:219-230(2011).
[12]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT MRD9 MET-99, AND
CHARACTERIZATION OF VARIANT MRD9 MET-99.
PubMed=21376300; DOI=10.1016/j.ajhg.2011.02.001;
Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y.,
Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A.,
Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O.,
Shekarabi M., Marineau C., Shevell M., Maranda B., Mitchell G.,
Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G.,
Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K.,
Huganir R.L., Rouleau G.A., Michaud J.L.;
"Excess of de novo deleterious mutations in genes associated with
glutamatergic systems in nonsyndromic intellectual disability.";
Am. J. Hum. Genet. 88:306-316(2011).
[13]
ERRATUM.
Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y.,
Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A.,
Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O.,
Shekarabi M., Marineau C., Shevell M., Maranda B., Mitchell G.,
Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G.,
Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K.,
Huganir R.L., Rouleau G.A., Michaud J.L.;
Am. J. Hum. Genet. 88:516-516(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-418; SER-419;
SER-937; SER-1310 AND SER-1548, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
INVOLVEMENT IN AUTOSOMAL DOMINANT SPASTIC PARAPLEGIA, AND VARIANT
LEU-69.
PubMed=25585697; DOI=10.1038/ejhg.2014.297;
Ylikallio E., Kim D., Isohanni P., Auranen M., Kim E., Loennqvist T.,
Tyynismaa H.;
"Dominant transmission of de novo KIF1A motor domain variant
underlying pure spastic paraplegia.";
Eur. J. Hum. Genet. 23:1427-1430(2015).
[16]
INVOLVEMENT IN AUTOSOMAL DOMINANT SPASTIC PARAPLEGIA, VARIANTS LEU-69;
SER-102 AND THR-1026, AND VARIANT MRD9 CYS-167.
PubMed=26410750; DOI=10.1007/s00415-015-7899-9;
Citterio A., Arnoldi A., Panzeri E., Merlini L., D'Angelo M.G.,
Musumeci O., Toscano A., Bondi A., Martinuzzi A., Bresolin N.,
Bassi M.T.;
"Variants in KIF1A gene in dominant and sporadic forms of hereditary
spastic paraparesis.";
J. Neurol. 262:2684-2690(2015).
[17]
VARIANT SPG30 VAL-255.
PubMed=21487076; DOI=10.1101/gr.117143.110;
Erlich Y., Edvardson S., Hodges E., Zenvirt S., Thekkat P., Shaag A.,
Dor T., Hannon G.J., Elpeleg O.;
"Exome sequencing and disease-network analysis of a single family
implicate a mutation in KIF1A in hereditary spastic paraparesis.";
Genome Res. 21:658-664(2011).
[18]
VARIANTS MET-46; ASN-136; ILE-187; MET-205; ILE-220; ASP-233; VAL-336
AND HIS-355, VARIANTS MRD9 MET-99; CYS-216; HIS-216; LYS-253 AND
TRP-316, CHARACTERIZATION OF VARIANTS MRD9 MET-99; CYS-216; LYS-253
AND VAL-255, AND CHARACTERIZATION OF VARIANT ILE-220.
PubMed=26125038; DOI=10.1002/acn3.198;
Esmaeeli Nieh S., Madou M.R., Sirajuddin M., Fregeau B., McKnight D.,
Lexa K., Strober J., Spaeth C., Hallinan B.E., Smaoui N., Pappas J.G.,
Burrow T.A., McDonald M.T., Latibashvili M., Leshinsky-Silver E.,
Lev D., Blumkin L., Vale R.D., Barkovich A.J., Sherr E.H.;
"De novo mutations in KIF1A cause progressive encephalopathy and brain
atrophy.";
Ann. Clin. Transl. Neurol. 2:623-635(2015).
[19]
VARIANTS MRD9 LEU-58; MET-99; ASP-102; PHE-144; CYS-167; PRO-202;
ARG-215; PRO-216; GLN-249; LYS-253; VAL-255; TRP-316 AND GLY-350,
CHARACTERIZATION OF VARIANTS MRD9 MET-99; PRO-202; ARG-215; PRO-216;
LYS-253; VAL-255 AND GLY-350, AND SUBCELLULAR LOCATION.
PubMed=25265257; DOI=10.1002/humu.22709;
Lee J.R., Srour M., Kim D., Hamdan F.F., Lim S.H., Brunel-Guitton C.,
Decarie J.C., Rossignol E., Mitchell G.A., Schreiber A., Moran R.,
Van Haren K., Richardson R., Nicolai J., Oberndorff K.M., Wagner J.D.,
Boycott K.M., Rahikkala E., Junna N., Tyynismaa H., Cuppen I.,
Verbeek N.E., Stumpel C.T., Willemsen M.A., de Munnik S.A.,
Rouleau G.A., Kim E., Kamsteeg E.J., Kleefstra T., Michaud J.L.;
"De novo mutations in the motor domain of KIF1A cause cognitive
impairment, spastic paraparesis, axonal neuropathy, and cerebellar
atrophy.";
Hum. Mutat. 36:69-78(2015).
-!- FUNCTION: Motor for anterograde axonal transport of synaptic
vesicle precursors. {ECO:0000250}.
-!- SUBUNIT: Monomer. Interacts with PPFIA1 and PPFIA4 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-2679809, EBI-2679809;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:21376300}. Note=Expressed in distal regions of
neurites. {ECO:0000269|PubMed:25265257}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q12756-1; Sequence=Displayed;
Name=2;
IsoId=Q12756-2; Sequence=VSP_021853, VSP_021854, VSP_021855;
Name=3;
IsoId=Q12756-3; Sequence=VSP_021853, VSP_021854;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in neurons.
{ECO:0000269|PubMed:21376300}.
-!- DISEASE: Spastic paraplegia 30, autosomal recessive (SPG30)
[MIM:610357]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG30 is characterized by onset in the first or second
decades of unsteady spastic gait and hyperreflexia of the lower
limbs. {ECO:0000269|PubMed:21487076}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Neuropathy, hereditary sensory, 2C (HSN2C) [MIM:614213]:
A neurodegenerative disorder characterized by onset in the first
decade of progressive distal sensory loss leading to ulceration
and amputation of the fingers and toes. Affected individuals also
develop distal muscle weakness, primarily affecting the lower
limbs. {ECO:0000269|PubMed:21820098}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Mental retardation, autosomal dominant 9 (MRD9)
[MIM:614255]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. {ECO:0000269|PubMed:21376300,
ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:26125038,
ECO:0000269|PubMed:26410750}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in KIF1A are a cause autosomal dominant
spastic paraplegia. Spastic paraplegia is a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. {ECO:0000269|PubMed:25585697,
ECO:0000269|PubMed:26410750}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. Unc-104 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00283}.
-!- SEQUENCE CAUTION:
Sequence=AAB97363.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE06111.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAE06111.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to C-terminal exon with non-canonical splice junction.; Evidence={ECO:0000305};
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EMBL; X90840; CAA62346.1; -; mRNA.
EMBL; AB290172; BAG06726.1; -; mRNA.
EMBL; AC011298; AAX93239.1; -; Genomic_DNA.
EMBL; AC112784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC064906; AAH64906.1; -; mRNA.
EMBL; BC111780; AAI11781.1; -; mRNA.
EMBL; BC111799; AAI11800.1; -; mRNA.
EMBL; AB210029; BAE06111.1; ALT_SEQ; mRNA.
EMBL; AF004425; AAD02917.1; -; mRNA.
EMBL; AB209138; BAD92375.1; -; mRNA.
EMBL; U37194; AAA80352.1; -; mRNA.
EMBL; L79946; AAB04640.1; -; mRNA.
EMBL; AF038173; AAB97363.1; ALT_INIT; mRNA.
EMBL; BX537556; CAH56161.1; -; mRNA.
CCDS; CCDS46561.1; -. [Q12756-1]
CCDS; CCDS58757.1; -. [Q12756-3]
RefSeq; NP_001230937.1; NM_001244008.1. [Q12756-3]
RefSeq; NP_001307634.1; NM_001320705.1.
RefSeq; NP_004312.2; NM_004321.7. [Q12756-1]
RefSeq; XP_016859880.1; XM_017004391.1.
UniGene; Hs.516802; -.
PDB; 4EGX; X-ray; 2.51 A; A/B/C/D=430-607.
PDB; 4EJQ; X-ray; 1.89 A; A/B/C/D/E/F/G/H=458-607.
PDB; 4UXO; EM; 6.30 A; C=1-361.
PDB; 4UXP; EM; 6.30 A; C=1-361.
PDB; 4UXR; EM; 7.00 A; C=1-361.
PDB; 4UXS; EM; 7.00 A; C=1-361.
PDBsum; 4EGX; -.
PDBsum; 4EJQ; -.
PDBsum; 4UXO; -.
PDBsum; 4UXP; -.
PDBsum; 4UXR; -.
PDBsum; 4UXS; -.
ProteinModelPortal; Q12756; -.
SMR; Q12756; -.
BioGrid; 107029; 49.
DIP; DIP-42405N; -.
IntAct; Q12756; 8.
MINT; Q12756; -.
STRING; 9606.ENSP00000322791; -.
ChEMBL; CHEMBL3308914; -.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
iPTMnet; Q12756; -.
PhosphoSitePlus; Q12756; -.
BioMuta; KIF1A; -.
DMDM; 119364606; -.
EPD; Q12756; -.
MaxQB; Q12756; -.
PaxDb; Q12756; -.
PeptideAtlas; Q12756; -.
PRIDE; Q12756; -.
ProteomicsDB; 58905; -.
ProteomicsDB; 58906; -. [Q12756-2]
Ensembl; ENST00000320389; ENSP00000322791; ENSG00000130294. [Q12756-1]
Ensembl; ENST00000498729; ENSP00000438388; ENSG00000130294. [Q12756-3]
GeneID; 547; -.
KEGG; hsa:547; -.
UCSC; uc010fzk.3; human. [Q12756-1]
CTD; 547; -.
DisGeNET; 547; -.
EuPathDB; HostDB:ENSG00000130294.14; -.
GeneCards; KIF1A; -.
GeneReviews; KIF1A; -.
HGNC; HGNC:888; KIF1A.
HPA; HPA005442; -.
MalaCards; KIF1A; -.
MIM; 601255; gene.
MIM; 610357; phenotype.
MIM; 614213; phenotype.
MIM; 614255; phenotype.
neXtProt; NX_Q12756; -.
OpenTargets; ENSG00000130294; -.
Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
Orphanet; 101010; Autosomal recessive spastic paraplegia type 30.
Orphanet; 970; Hereditary sensory and autonomic neuropathy type 2.
PharmGKB; PA25180; -.
eggNOG; KOG0245; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00890000139327; -.
HOGENOM; HOG000165968; -.
HOVERGEN; HBG052251; -.
InParanoid; Q12756; -.
KO; K10392; -.
OMA; HCVFRSD; -.
OrthoDB; EOG091G009V; -.
PhylomeDB; Q12756; -.
TreeFam; TF105221; -.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-983189; Kinesins.
ChiTaRS; KIF1A; human.
GeneWiki; KIF1A; -.
GenomeRNAi; 547; -.
PRO; PR:Q12756; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000130294; Expressed in 140 organ(s), highest expression level in frontal cortex.
ExpressionAtlas; Q12756; baseline and differential.
Genevisible; Q12756; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
GO; GO:0003774; F:motor activity; TAS:ProtInc.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0008089; P:anterograde axonal transport; TAS:ProtInc.
GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
GO; GO:0022027; P:interkinetic nuclear migration; IEA:Ensembl.
GO; GO:0098840; P:protein transport along microtubule; IEA:Ensembl.
GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
CDD; cd00060; FHA; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR022164; Kinesin-like.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR022140; Kinesin-like_KIF1-typ.
InterPro; IPR032405; Kinesin_assoc.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008984; SMAD_FHA_dom_sf.
PANTHER; PTHR24115; PTHR24115; 2.
Pfam; PF12473; DUF3694; 1.
Pfam; PF00498; FHA; 1.
Pfam; PF12423; KIF1B; 1.
Pfam; PF00225; Kinesin; 1.
Pfam; PF16183; Kinesin_assoc; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00240; FHA; 1.
SMART; SM00129; KISc; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
Hereditary spastic paraplegia; Mental retardation; Microtubule;
Motor protein; Neurodegeneration; Neuropathy; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 1690 Kinesin-like protein KIF1A.
/FTId=PRO_0000125405.
DOMAIN 5 354 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
DOMAIN 516 572 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
DOMAIN 1575 1673 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 97 104 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
COILED 366 383 {ECO:0000255}.
COILED 429 462 {ECO:0000255}.
COILED 622 681 {ECO:0000255}.
COILED 801 822 {ECO:0000255}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 607 607 Phosphothreonine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 612 612 Phosphothreonine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 937 937 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1310 1310 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1337 1337 Phosphoserine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 1519 1519 Phosphothreonine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 1523 1523 Phosphothreonine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 1528 1528 Phosphoserine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 1532 1532 Phosphoserine.
{ECO:0000250|UniProtKB:P33173}.
MOD_RES 1548 1548 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 394 394 M -> TNTVPGGPKL (in isoform 2 and isoform
3). {ECO:0000303|Ref.2,
ECO:0000303|Ref.5}.
/FTId=VSP_021853.
VAR_SEQ 848 848 R -> RLVGSSAISGCNSYPLLNTCMSERMAALTPSPTFSS
PDSDATEPAEEQSVGEEEEEEEEEEDEEEEDLEDDVFPEHA
LCDGRDPFYDRPPLFS (in isoform 2 and
isoform 3). {ECO:0000303|Ref.2,
ECO:0000303|Ref.5}.
/FTId=VSP_021854.
VAR_SEQ 1234 1234 D -> DRVSLGNDT (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_021855.
VARIANT 46 46 T -> M (in dbSNP:rs182395595).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075471.
VARIANT 58 58 S -> L (in MRD9; dbSNP:rs672601362).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075472.
VARIANT 69 69 S -> L (probable disease-associated
mutation found in autosomal dominant
spastic paraplegia; dbSNP:rs786200949).
{ECO:0000269|PubMed:25585697,
ECO:0000269|PubMed:26410750}.
/FTId=VAR_077467.
VARIANT 99 99 T -> M (in MRD9; affects the subcellular
location of the protein; there is a
reduced distal localization and increased
accumulation throughout the cell body and
proximal neurites in cells transfected
with a mutant protein; disrupts
microtubule motility; dbSNP:rs387906799).
{ECO:0000269|PubMed:21376300,
ECO:0000269|PubMed:25265257,
ECO:0000269|PubMed:26125038}.
/FTId=VAR_066649.
VARIANT 102 102 G -> D (in MRD9; dbSNP:rs672601363).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075473.
VARIANT 102 102 G -> S (probable disease-associated
mutation found in a sporadic case of
spastic paraplegia; de novo mutation;
dbSNP:rs1064795534).
{ECO:0000269|PubMed:26410750}.
/FTId=VAR_077468.
VARIANT 136 136 D -> N (in dbSNP:rs374178011).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075474.
VARIANT 144 144 V -> F (in MRD9; dbSNP:rs672601364).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075475.
VARIANT 167 167 R -> C (in MRD9; also found in a sporadic
case of spastic paraplegia;
dbSNP:rs672601365).
{ECO:0000269|PubMed:25265257,
ECO:0000269|PubMed:26410750}.
/FTId=VAR_075476.
VARIANT 187 187 T -> I (in dbSNP:rs370623844).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075477.
VARIANT 202 202 A -> P (in MRD9; reduces accumulation in
distal regions of the neurites;
dbSNP:rs672601366).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075478.
VARIANT 205 205 V -> M (in dbSNP:rs371039513).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075479.
VARIANT 215 215 S -> R (in MRD9; reduces accumulation in
distal regions of the neurites;
dbSNP:rs672601367).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075480.
VARIANT 216 216 R -> C (in MRD9; disrupts microtubule
motility; dbSNP:rs797045164).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075481.
VARIANT 216 216 R -> H (in MRD9; dbSNP:rs672601368).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075482.
VARIANT 216 216 R -> P (in MRD9; reduces accumulation in
distal regions of the neurites;
dbSNP:rs672601368).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075483.
VARIANT 220 220 V -> I (polymorphism; no effect on
microtubule motility; dbSNP:rs201314877).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075484.
VARIANT 233 233 E -> D (in dbSNP:rs373882732).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075485.
VARIANT 249 249 L -> Q (in MRD9; dbSNP:rs672601371).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075486.
VARIANT 253 253 E -> K (in MRD9; reduces accumulation in
distal regions of the neurites; disrupts
microtubule motility; dbSNP:rs672601369).
{ECO:0000269|PubMed:25265257,
ECO:0000269|PubMed:26125038}.
/FTId=VAR_075487.
VARIANT 255 255 A -> V (in SPG30 and MRD9; unknown
pathological significance; reduces
accumulation in distal regions of the
neurites; no effect on microtubule
motility; dbSNP:rs387906798).
{ECO:0000269|PubMed:21487076,
ECO:0000269|PubMed:25265257,
ECO:0000269|PubMed:26125038}.
/FTId=VAR_066650.
VARIANT 316 316 R -> W (in MRD9; dbSNP:rs672601370).
{ECO:0000269|PubMed:25265257,
ECO:0000269|PubMed:26125038}.
/FTId=VAR_075488.
VARIANT 336 336 I -> V (in dbSNP:rs375423065).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075489.
VARIANT 350 350 R -> G (in MRD9; reduces accumulation in
distal regions of the neurites;
dbSNP:rs387907259).
{ECO:0000269|PubMed:25265257}.
/FTId=VAR_075490.
VARIANT 355 355 R -> H (in dbSNP:rs373042822).
{ECO:0000269|PubMed:26125038}.
/FTId=VAR_075491.
VARIANT 1026 1026 I -> T (found in a case of autosomal
dominant spastic paraplegia; unknown
pathological significance).
{ECO:0000269|PubMed:26410750}.
/FTId=VAR_077469.
CONFLICT 104 104 S -> T (in Ref. 6; AAD02917).
{ECO:0000305}.
CONFLICT 595 595 N -> T (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 777 777 T -> K (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 1030 1030 D -> E (in Ref. 8; AAA80352).
{ECO:0000305}.
CONFLICT 1034 1034 S -> C (in Ref. 8; AAA80352).
{ECO:0000305}.
CONFLICT 1108 1108 P -> L (in Ref. 2; BAG06726 and 7;
BAD92375). {ECO:0000305}.
CONFLICT 1225 1225 S -> A (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 1232 1232 Q -> H (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 1245 1245 D -> N (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 1257 1257 V -> I (in Ref. 1; CAA62346).
{ECO:0000305}.
CONFLICT 1684 1684 R -> W (in Ref. 4; AAI11781).
{ECO:0000305}.
HELIX 458 471 {ECO:0000244|PDB:4EJQ}.
STRAND 474 476 {ECO:0000244|PDB:4EJQ}.
STRAND 480 485 {ECO:0000244|PDB:4EJQ}.
STRAND 489 491 {ECO:0000244|PDB:4EJQ}.
STRAND 493 496 {ECO:0000244|PDB:4EJQ}.
STRAND 507 510 {ECO:0000244|PDB:4EJQ}.
STRAND 513 519 {ECO:0000244|PDB:4EJQ}.
STRAND 521 525 {ECO:0000244|PDB:4EGX}.
STRAND 528 530 {ECO:0000244|PDB:4EJQ}.
STRAND 538 546 {ECO:0000244|PDB:4EJQ}.
STRAND 550 552 {ECO:0000244|PDB:4EJQ}.
STRAND 554 559 {ECO:0000244|PDB:4EJQ}.
STRAND 565 567 {ECO:0000244|PDB:4EJQ}.
STRAND 583 586 {ECO:0000244|PDB:4EJQ}.
TURN 587 589 {ECO:0000244|PDB:4EJQ}.
STRAND 590 595 {ECO:0000244|PDB:4EJQ}.
HELIX 597 604 {ECO:0000244|PDB:4EJQ}.
SEQUENCE 1690 AA; 191064 MW; FB3CA33B7060AF60 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDMTNALVG MSPSSSLSAL SSRAASVSSL
HERILFAPGS EEAIERLKET EKIIAELNET WEEKLRRTEA IRMEREALLA EMGVAMREDG
GTLGVFSPKK TPHLVNLNED PLMSECLLYY IKDGITRVGR EDGERRQDIV LSGHFIKEEH
CVFRSDSRGG SEAVVTLEPC EGADTYVNGK KVTEPSILRS GNRIIMGKSH VFRFNHPEQA
RQERERTPCA ETPAEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR REREEATYLL
EQQRLDYESK LEALQKQMDS RYYPEVNEEE EEPEDEVQWT ERECELALWA FRKWKWYQFT
SLRDLLWGNA IFLKEANAIS VELKKKVQFQ FVLLTDTLYS PLPPDLLPPE AAKDRETRPF
PRTIVAVEVQ DQKNGATHYW TLEKLRQRLD LMREMYDRAA EVPSSVIEDC DNVVTGGDPF
YDRFPWFRLV GRAFVYLSNL LYPVPLVHRV AIVSEKGEVK GFLRVAVQAI SADEEAPDYG
SGVRQSGTAK ISFDDQHFEK FQSESCPVVG MSRSGTSQEE LRIVEGQGQG ADVGPSADEV
NNNTCSAVPP EGLLLDSSEK AALDGPLDAA LDHLRLGNTF TFRVTVLQAS SISAEYADIF
CQFNFIHRHD EAFSTEPLKN TGRGPPLGFY HVQNIAVEVT KSFIEYIKSQ PIVFEVFGHY
QQHPFPPLCK DVLSPLRPSR RHFPRVMPLS KPVPATKLST LTRPCPGPCH CKYDLLVYFE
ICELEANGDY IPAVVDHRGG MPCMGTFLLH QGIQRRITVT LLHETGSHIR WKEVRELVVG
RIRNTPETDE SLIDPNILSL NILSSGYIHP AQDDRTFYQF EAAWDSSMHN SLLLNRVTPY
REKIYMTLSA YIEMENCTQP AVVTKDFCMV FYSRDAKLPA SRSIRNLFGS GSLRASESNR
VTGVYELSLC HVADAGSPGM QRRRRRVLDT SVAYVRGEEN LAGWRPRSDS LILDHQWELE
KLSLLQEVEK TRHYLLLREK LETAQRPVPE ALSPAFSEDS ESHGSSSASS PLSAEGRPSP
LEAPNERQRE LAVKCLRLLT HTFNREYTHS HVCVSASESK LSEMSVTLLR DPSMSPLGVA
TLTPSSTCPS LVEGRYGATD LRTPQPCSRP ASPEPELLPE ADSKKLPSPA RATETDKEPQ
RLLVPDIQEI RVSPIVSKKG YLHFLEPHTS GWARRFVVVR RPYAYMYNSD KDTVERFVLN
LATAQVEYSE DQQAMLKTPN TFAVCTEHRG ILLQAASDKD MHDWLYAFNP LLAGTIRSKL
SRRRSAQMRV


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