Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Kinesin-like protein KIFC3

 KIFC3_HUMAN             Reviewed;         833 AA.
Q9BVG8; A8K6S2; B7Z484; O75299; Q49A29; Q49AQ0; Q59G19; Q8IUT3;
Q96HW6;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 4.
27-SEP-2017, entry version 154.
RecName: Full=Kinesin-like protein KIFC3;
Name=KIFC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Placenta, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 105-833 (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 106-833 (ISOFORM 3), AND VARIANT
VAL-391.
TISSUE=Brain, Muscle, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 86-833 (ISOFORM 2).
TISSUE=Retina;
PubMed=9782090; DOI=10.1006/geno.1998.5431;
Hoang E.H., Whitehead J.L., Dose A.C., Burnside B.;
"Cloning of a novel C-terminal kinesin (KIFC3) that maps to human
chromosome 16q13-q21 and thus is a candidate gene for Bardet-Biedl
syndrome.";
Genomics 52:219-222(1998).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19041755; DOI=10.1016/j.cell.2008.09.040;
Meng W., Mushika Y., Ichii T., Takeichi M.;
"Anchorage of microtubule minus ends to adherens junctions regulates
epithelial cell-cell contacts.";
Cell 135:948-959(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813 AND SER-817, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 443-770 IN COMPLEX WITH ADP.
Structural genomics consortium (SGC);
"Crystal structure of the KIFC3 motor domain in complex with ADP.";
Submitted (JUN-2006) to the PDB data bank.
-!- FUNCTION: Minus-end microtubule-dependent motor protein. Involved
in apically targeted transport (By similarity). Required for
zonula adherens maintenance. {ECO:0000250,
ECO:0000269|PubMed:19041755}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-2125614, EBI-743598;
Q08117:AES; NbExp=3; IntAct=EBI-2125614, EBI-717810;
P15336:ATF2; NbExp=3; IntAct=EBI-2125614, EBI-1170906;
P41182:BCL6; NbExp=3; IntAct=EBI-2125614, EBI-765407;
Q9NX04:C1orf109; NbExp=4; IntAct=EBI-2125614, EBI-8643161;
Q9H257-2:CARD9; NbExp=4; IntAct=EBI-14069005, EBI-11530605;
Q9HC52:CBX8; NbExp=3; IntAct=EBI-2125614, EBI-712912;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-2125614, EBI-10171570;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-2125614, EBI-10171416;
Q8IYE0:CCDC146; NbExp=4; IntAct=EBI-14069005, EBI-10749669;
Q7Z6N9:CCDC28A; NbExp=3; IntAct=EBI-2125614, EBI-10258115;
Q8IWP9:CCDC28A; NbExp=3; IntAct=EBI-2125614, EBI-355471;
Q8TD31-3:CCHCR1; NbExp=4; IntAct=EBI-14069005, EBI-10175300;
Q07002:CDK18; NbExp=3; IntAct=EBI-2125614, EBI-746238;
Q01850:CDR2; NbExp=3; IntAct=EBI-2125614, EBI-1181367;
Q96L14:CEP170P1; NbExp=4; IntAct=EBI-14069005, EBI-743488;
Q53EZ4:CEP55; NbExp=3; IntAct=EBI-2125614, EBI-747776;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-2125614, EBI-10181988;
Q8N3C7:CLIP4; NbExp=3; IntAct=EBI-2125614, EBI-5655540;
Q02930-3:CREB5; NbExp=3; IntAct=EBI-2125614, EBI-10192698;
Q8WWE8:CYTH4; NbExp=3; IntAct=EBI-2125614, EBI-10277443;
Q13561:DCTN2; NbExp=4; IntAct=EBI-14069005, EBI-715074;
O43602:DCX; NbExp=3; IntAct=EBI-2125614, EBI-8646694;
Q05D60:DEUP1; NbExp=3; IntAct=EBI-2125614, EBI-748597;
Q96EV8:DTNBP1; NbExp=3; IntAct=EBI-2125614, EBI-465804;
P62508:ESRRG; NbExp=3; IntAct=EBI-2125614, EBI-2834260;
O00471:EXOC5; NbExp=6; IntAct=EBI-14069005, EBI-949824;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-2125614, EBI-744506;
Q5VWN6:FAM208B; NbExp=4; IntAct=EBI-14069005, EBI-745958;
Q9NW38:FANCL; NbExp=3; IntAct=EBI-2125614, EBI-2339898;
O94868:FCHSD2; NbExp=3; IntAct=EBI-2125614, EBI-1215612;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-2125614, EBI-10172181;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-2125614, EBI-618309;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-2125614, EBI-739467;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-2125614, EBI-2514791;
O75506:HSBP1; NbExp=5; IntAct=EBI-2125614, EBI-748664;
Q8NDH6:ICA1L; NbExp=3; IntAct=EBI-2125614, EBI-10269733;
Q8NA54:IQUB; NbExp=4; IntAct=EBI-14069005, EBI-10220600;
Q13352:ITGB3BP; NbExp=3; IntAct=EBI-2125614, EBI-712105;
Q13352-5:ITGB3BP; NbExp=3; IntAct=EBI-2125614, EBI-10175826;
Q63ZY3:KANK2; NbExp=4; IntAct=EBI-14069005, EBI-2556193;
Q7Z3B3:KANSL1; NbExp=3; IntAct=EBI-2125614, EBI-740244;
P19012:KRT15; NbExp=3; IntAct=EBI-2125614, EBI-739566;
P08727:KRT19; NbExp=3; IntAct=EBI-2125614, EBI-742756;
Q15323:KRT31; NbExp=3; IntAct=EBI-2125614, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-2125614, EBI-10171697;
P13647:KRT5; NbExp=3; IntAct=EBI-2125614, EBI-702187;
P02538:KRT6A; NbExp=5; IntAct=EBI-2125614, EBI-702198;
P04259:KRT6B; NbExp=3; IntAct=EBI-2125614, EBI-740907;
P48668:KRT6C; NbExp=3; IntAct=EBI-2125614, EBI-2564105;
Q96BZ8:LENG1; NbExp=3; IntAct=EBI-2125614, EBI-726510;
Q96GY3:LIN37; NbExp=3; IntAct=EBI-2125614, EBI-748884;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-14069005, EBI-739832;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-2125614, EBI-741037;
P33993:MCM7; NbExp=3; IntAct=EBI-2125614, EBI-355924;
Q9NPJ6:MED4; NbExp=4; IntAct=EBI-14069005, EBI-394607;
P55081:MFAP1; NbExp=3; IntAct=EBI-2125614, EBI-1048159;
Q9UJV3-2:MID2; NbExp=4; IntAct=EBI-14069005, EBI-10172526;
P00540:MOS; NbExp=3; IntAct=EBI-2125614, EBI-1757866;
O14777:NDC80; NbExp=4; IntAct=EBI-14069005, EBI-715849;
Q9GZM8:NDEL1; NbExp=3; IntAct=EBI-2125614, EBI-928842;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-2125614, EBI-10172876;
I6L9F6:NEFL; NbExp=3; IntAct=EBI-2125614, EBI-10178578;
P37198:NUP62; NbExp=3; IntAct=EBI-2125614, EBI-347978;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-2125614, EBI-713786;
Q96KQ4:PPP1R13B; NbExp=4; IntAct=EBI-14069005, EBI-1105153;
P54646:PRKAA2; NbExp=4; IntAct=EBI-2125614, EBI-1383852;
P20618:PSMB1; NbExp=3; IntAct=EBI-2125614, EBI-372273;
O75771:RAD51D; NbExp=3; IntAct=EBI-2125614, EBI-1055693;
Q9UHP6:RSPH14; NbExp=3; IntAct=EBI-2125614, EBI-748350;
O95171:SCEL; NbExp=3; IntAct=EBI-2125614, EBI-7543896;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-2125614, EBI-747107;
Q969G3:SMARCE1; NbExp=4; IntAct=EBI-2125614, EBI-455078;
P35711:SOX5; NbExp=3; IntAct=EBI-2125614, EBI-3505701;
Q8NA61:SPERT; NbExp=5; IntAct=EBI-2125614, EBI-741724;
Q8NA61-2:SPERT; NbExp=4; IntAct=EBI-14069005, EBI-11524851;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-2125614, EBI-6872807;
Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-2125614, EBI-954696;
Q15025:TNIP1; NbExp=3; IntAct=EBI-2125614, EBI-357849;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-2125614, EBI-10184033;
Q12933:TRAF2; NbExp=3; IntAct=EBI-2125614, EBI-355744;
P36406:TRIM23; NbExp=3; IntAct=EBI-2125614, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-2125614, EBI-719493;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-2125614, EBI-725997;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-2125614, EBI-2130429;
Q99816:TSG101; NbExp=3; IntAct=EBI-2125614, EBI-346882;
Q3SY00:TSGA10IP; NbExp=4; IntAct=EBI-14069005, EBI-10241197;
Q969E8:TSR2; NbExp=3; IntAct=EBI-2125614, EBI-746981;
O75604:USP2; NbExp=3; IntAct=EBI-2125614, EBI-743272;
Q05516:ZBTB16; NbExp=4; IntAct=EBI-14069005, EBI-711925;
Q96BR9:ZBTB8A; NbExp=3; IntAct=EBI-2125614, EBI-742740;
Q8N5A5:ZGPAT; NbExp=4; IntAct=EBI-2125614, EBI-3439227;
Q8N5A5-2:ZGPAT; NbExp=3; IntAct=EBI-2125614, EBI-10183064;
Q9UJW8:ZNF180; NbExp=3; IntAct=EBI-2125614, EBI-10322527;
P17024:ZNF20; NbExp=3; IntAct=EBI-2125614, EBI-717634;
Q7Z3I7:ZNF572; NbExp=6; IntAct=EBI-2125614, EBI-10172590;
Q8N720:ZNF655; NbExp=3; IntAct=EBI-2125614, EBI-625509;
-!- SUBCELLULAR LOCATION: Cell junction, adherens junction
{ECO:0000269|PubMed:19041755}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:19041755}. Cytoplasmic vesicle membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Note=Apical cell membrane. On membrane organelles immediately
beneath the apical plasma membrane of renal tubular epithelial
cells. Localized in the distal tubules and loops of Henle in the
kidney, but not in the proximal tubules or the glomeruli, with
stronger staining in the apical area of these epithelial cells (By
similarity). Localizes along zonula adherens only at mature cell-
cell contacts. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9BVG8-3; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q9BVG8-2; Sequence=VSP_021018;
Name=3;
IsoId=Q9BVG8-4; Sequence=VSP_022361, VSP_022362;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q9BVG8-5; Sequence=VSP_043724, VSP_021018;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9BVG8-6; Sequence=VSP_057224, VSP_021018;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
-!- SEQUENCE CAUTION:
Sequence=AAH34234.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAH41132.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAH47051.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAD92527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK291737; BAF84426.1; -; mRNA.
EMBL; AK296995; BAH12470.1; -; mRNA.
EMBL; AB209290; BAD92527.1; ALT_INIT; mRNA.
EMBL; AC010543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO082293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW82955.1; -; Genomic_DNA.
EMBL; BC001211; AAH01211.2; -; mRNA.
EMBL; BC008014; AAH08014.1; -; mRNA.
EMBL; BC034234; AAH34234.1; ALT_INIT; mRNA.
EMBL; BC041132; AAH41132.1; ALT_INIT; mRNA.
EMBL; BC047051; AAH47051.1; ALT_SEQ; mRNA.
EMBL; AF004426; AAC24153.1; -; mRNA.
CCDS; CCDS10789.2; -. [Q9BVG8-3]
CCDS; CCDS45493.1; -. [Q9BVG8-2]
CCDS; CCDS45494.1; -. [Q9BVG8-5]
CCDS; CCDS81989.1; -. [Q9BVG8-6]
RefSeq; NP_001123571.1; NM_001130099.1. [Q9BVG8-5]
RefSeq; NP_001123572.1; NM_001130100.1. [Q9BVG8-2]
RefSeq; NP_001305639.1; NM_001318710.1. [Q9BVG8-6]
RefSeq; NP_001305640.1; NM_001318711.1.
RefSeq; NP_001305641.1; NM_001318712.1.
RefSeq; NP_001305642.1; NM_001318713.1.
RefSeq; NP_001305643.1; NM_001318714.1. [Q9BVG8-5]
RefSeq; NP_001305644.1; NM_001318715.1. [Q9BVG8-5]
RefSeq; NP_005541.3; NM_005550.3. [Q9BVG8-3]
UniGene; Hs.23131; -.
PDB; 2H58; X-ray; 1.85 A; A=443-770.
PDBsum; 2H58; -.
ProteinModelPortal; Q9BVG8; -.
SMR; Q9BVG8; -.
BioGrid; 110002; 122.
DIP; DIP-52406N; -.
IntAct; Q9BVG8; 221.
MINT; MINT-4989557; -.
STRING; 9606.ENSP00000368976; -.
ChEMBL; CHEMBL1075119; -.
iPTMnet; Q9BVG8; -.
PhosphoSitePlus; Q9BVG8; -.
BioMuta; KIFC3; -.
DMDM; 357529584; -.
PaxDb; Q9BVG8; -.
PeptideAtlas; Q9BVG8; -.
PRIDE; Q9BVG8; -.
DNASU; 3801; -.
Ensembl; ENST00000379655; ENSP00000368976; ENSG00000140859. [Q9BVG8-3]
Ensembl; ENST00000421376; ENSP00000396399; ENSG00000140859. [Q9BVG8-5]
Ensembl; ENST00000445690; ENSP00000401696; ENSG00000140859. [Q9BVG8-2]
Ensembl; ENST00000465878; ENSP00000454659; ENSG00000140859. [Q9BVG8-5]
Ensembl; ENST00000541240; ENSP00000442008; ENSG00000140859. [Q9BVG8-6]
Ensembl; ENST00000562903; ENSP00000456239; ENSG00000140859. [Q9BVG8-5]
GeneID; 3801; -.
KEGG; hsa:3801; -.
UCSC; uc002emm.4; human. [Q9BVG8-3]
CTD; 3801; -.
DisGeNET; 3801; -.
EuPathDB; HostDB:ENSG00000140859.15; -.
GeneCards; KIFC3; -.
HGNC; HGNC:6326; KIFC3.
HPA; HPA021240; -.
MIM; 604535; gene.
neXtProt; NX_Q9BVG8; -.
OpenTargets; ENSG00000140859; -.
PharmGKB; PA30112; -.
eggNOG; KOG0239; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00550000074610; -.
HOGENOM; HOG000116164; -.
HOVERGEN; HBG052259; -.
InParanoid; Q9BVG8; -.
KO; K10406; -.
OMA; IKYVIKT; -.
OrthoDB; EOG091G01HX; -.
TreeFam; TF105238; -.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
ChiTaRS; KIFC3; human.
EvolutionaryTrace; Q9BVG8; -.
GeneWiki; KIFC3; -.
GenomeRNAi; 3801; -.
PRO; PR:Q9BVG8; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140859; -.
CleanEx; HS_KIFC3; -.
ExpressionAtlas; Q9BVG8; baseline and differential.
Genevisible; Q9BVG8; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005915; C:zonula adherens; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008569; F:ATP-dependent microtubule motor activity, minus-end-directed; IEA:InterPro.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0003777; F:microtubule motor activity; TAS:ProtInc.
GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
GO; GO:0045218; P:zonula adherens maintenance; IMP:UniProtKB.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR027325; KIFC3.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115:SF655; PTHR24115:SF655; 1.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell junction;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Membrane; Microtubule; Motor protein;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 833 Kinesin-like protein KIFC3.
/FTId=PRO_0000125431.
DOMAIN 445 768 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 528 535 ATP.
COILED 102 362 {ECO:0000255}.
COILED 395 432 {ECO:0000255}.
MOD_RES 813 813 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 817 817 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 139 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043724.
VAR_SEQ 1 1 M -> MCASACKDTAAWCPEEAAEPQAM (in isoform
5). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_057224.
VAR_SEQ 626 637 FEFGHTNRTTEF -> WRREPLTTATLL (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_022361.
VAR_SEQ 638 833 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022362.
VAR_SEQ 826 833 GKSRPLPV -> A (in isoform 2, isoform 4
and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9782090,
ECO:0000303|Ref.2}.
/FTId=VSP_021018.
VARIANT 391 391 G -> V (in dbSNP:rs17854089).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028114.
CONFLICT 150 150 M -> L (in Ref. 6; AAC24153).
{ECO:0000305}.
CONFLICT 185 185 S -> P (in Ref. 5; AAH34234).
{ECO:0000305}.
CONFLICT 281 281 H -> S (in Ref. 5; AAH08014).
{ECO:0000305}.
CONFLICT 736 736 D -> G (in Ref. 5; AAH34234).
{ECO:0000305}.
STRAND 446 452 {ECO:0000244|PDB:2H58}.
HELIX 457 459 {ECO:0000244|PDB:2H58}.
HELIX 463 465 {ECO:0000244|PDB:2H58}.
STRAND 469 471 {ECO:0000244|PDB:2H58}.
STRAND 478 483 {ECO:0000244|PDB:2H58}.
STRAND 486 491 {ECO:0000244|PDB:2H58}.
STRAND 493 496 {ECO:0000244|PDB:2H58}.
HELIX 502 506 {ECO:0000244|PDB:2H58}.
TURN 507 509 {ECO:0000244|PDB:2H58}.
HELIX 510 517 {ECO:0000244|PDB:2H58}.
STRAND 522 529 {ECO:0000244|PDB:2H58}.
HELIX 534 538 {ECO:0000244|PDB:2H58}.
STRAND 542 545 {ECO:0000244|PDB:2H58}.
HELIX 547 560 {ECO:0000244|PDB:2H58}.
STRAND 566 578 {ECO:0000244|PDB:2H58}.
STRAND 581 584 {ECO:0000244|PDB:2H58}.
STRAND 614 616 {ECO:0000244|PDB:2H58}.
HELIX 619 632 {ECO:0000244|PDB:2H58}.
HELIX 644 646 {ECO:0000244|PDB:2H58}.
STRAND 647 659 {ECO:0000244|PDB:2H58}.
TURN 660 662 {ECO:0000244|PDB:2H58}.
STRAND 665 674 {ECO:0000244|PDB:2H58}.
HELIX 689 712 {ECO:0000244|PDB:2H58}.
HELIX 720 722 {ECO:0000244|PDB:2H58}.
HELIX 724 728 {ECO:0000244|PDB:2H58}.
HELIX 730 733 {ECO:0000244|PDB:2H58}.
STRAND 738 745 {ECO:0000244|PDB:2H58}.
HELIX 749 751 {ECO:0000244|PDB:2H58}.
HELIX 752 765 {ECO:0000244|PDB:2H58}.
SEQUENCE 833 AA; 92775 MW; 50983587270BDC2F CRC64;
MVPSRRTWNL GATPSLRGLW RVGRAPEPEP GMARPAPAPA SPAARPFPHT GPGRLRTGRG
KDTPVCGDED SSARSAARPA LAQCRALSVD WAGPGSPHGL YLTLQVEHLK EKLISQAQEV
SRLRSELGGT DLEKHRDLLM VENERLRQEM RRCEAELQEL RTKPAGPCPG CEHSQESAQL
RDKLSQLQLE MAESKGMLSE LNLEVQQKTD RLAEVELRLK DCLAEKAQEE ERLSRRLRDS
HETIASLRAQ SPPVKYVIKT VEVESSKTKQ ALSESQARNQ HLQEQVAMQR QVLKEMEQQL
QSSHQLTARL RAQIAMYESE LERAHGQMLE EMQSLEEDKN RAIEEAFARA QVEMKAVHEN
LAGVRTNLLT LQPALRTLTN DYNGLKRQVR GFPLLLQEAL RSVKAEIGQA IEEVNSNNQE
LLRKYRRELQ LRKKCHNELV RLKGNIRVIA RVRPVTKEDG EGPEATNAVT FDADDDSIIH
LLHKGKPVSF ELDKVFSPQA SQQDVFQEVQ ALVTSCIDGF NVCIFAYGQT GAGKTYTMEG
TAENPGINQR ALQLLFSEVQ EKASDWEYTI TVSAAEIYNE VLRDLLGKEP QEKLEIRLCP
DGSGQLYVPG LTEFQVQSVD DINKVFEFGH TNRTTEFTNL NEHSSRSHAL LIVTVRGVDC
STGLRTTGKL NLVDLAGSER VGKSGAEGSR LREAQHINKS LSALGDVIAA LRSRQGHVPF
RNSKLTYLLQ DSLSGDSKTL MVVQVSPVEK NTSETLYSLK FAERVRSVEL GPGLRRAELG
SWSSQEHLEW EPACQTPQPS ARAHSAPSSG TSSRPGSIRR KLQPSGKSRP LPV


Related products :

Catalog number Product name Quantity
25-168 KIFC3 belongs to the kinesin-like protein family. It contains 1 kinesin-motor domain. KIFC3 is the minus-end microtubule-dependent motor protein. It is involved in apically targeted transport. 0.05 mg
KIFC3_MOUSE ELISA Kit FOR Kinesin-like protein KIFC3; organism: Mouse; gene name: Kifc3 96T
CSB-EL012350HU Human Kinesin-like protein KIFC3(KIFC3) ELISA kit SpeciesHuman 96T
CSB-EL012350MO Mouse Kinesin-like protein KIFC3(KIFC3) ELISA kit SpeciesMouse 96T
CSB-EL012350MO Mouse Kinesin-like protein KIFC3(KIFC3) ELISA kit 96T
CSB-EL012350HU Human Kinesin-like protein KIFC3(KIFC3) ELISA kit 96T
KIN KIFC3 Gene kinesin family member C3
201-20-2963 KIFC3{kinesin family member C3}rabbit.pAb 0.2ml
KIFC3 KIFC1 Gene kinesin family member C1
CSB-EL012350HU Human kinesin family member C3 (KIFC3) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL012350MO Mouse kinesin family member C3 (KIFC3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
18-003-43864 Kinesin-like protein KIF23 - Mitotic kinesin-like protein 1; Kinesin-like protein 5 Polyclonal 0.1 mg Protein A
18-003-42456 Kinesin-like protein KIF3B - Microtubule plus end-directed kinesin motor 3B; HH0048 Polyclonal 0.05 mg Aff Pur
25-178 KIF2A belongs to the kinesin-like protein family, MCAK_KIF2 subfamily. It contains 1 kinesin-motor domain. KIF2A plus end-directed microtubule-dependent motor required for normal brain development. It 0.05 mg
E0155m ELISA Kiaa4086,Kif5,Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Mouse,Mus musculus,Neuronal kinesin heavy chain,NKHC,Nkhc1 96T
E0155m ELISA kit Kiaa4086,Kif5,Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Mouse,Mus musculus,Neuronal kinesin heavy chain,NKHC,Nkhc1 96T
U0155m CLIA Kiaa4086,Kif5,Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Mouse,Mus musculus,Neuronal kinesin heavy chain,NKHC,Nkhc1 96T
E0155h ELISA Homo sapiens,Human,KIF5A,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,NKHC1 96T
U0155h CLIA Homo sapiens,Human,KIF5A,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,NKHC1 96T
E0155h ELISA kit Homo sapiens,Human,KIF5A,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,NKHC1 96T
E0155r ELISA Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,Rat,Rattus norvegicus 96T
E0155r ELISA kit Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,Rat,Rattus norvegicus 96T
U0155r CLIA Kif5a,Kinesin heavy chain isoform 5A,Kinesin heavy chain neuron-specific 1,Neuronal kinesin heavy chain,NKHC,Rat,Rattus norvegicus 96T
18-003-42449 Kinesin heavy chain isoform 5A - Neuronal kinesin heavy chain; NKHC; Kinesin heavy chain neuron-specific 1 Polyclonal 0.05 mg Aff Pur
11-434-C100 Rabbit Polyclonal to Kinesin Antigen Kinesin Isotype Antigen Kinesin Isotype 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur