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Q9BVG8

- KIFC3_HUMAN

UniProt

Q9BVG8 - KIFC3_HUMAN

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Protein

Kinesin-like protein KIFC3

Gene

KIFC3

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

Functioni

Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi528 – 5358ATP

GO - Molecular functioni

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. microtubule motor activity Source: RefGenome

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. epithelial cell-cell adhesion Source: UniProtKB
  3. Golgi organization Source: Ensembl
  4. metabolic process Source: GOC
  5. microtubule-based movement Source: RefGenome
  6. visual perception Source: ProtInc
  7. zonula adherens maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIFC3
Gene namesi
Name:KIFC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:6326. KIFC3.

Subcellular locationi

Cell junctionadherens junction 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
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.By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. Golgi apparatus Source: Ensembl
  5. kinesin complex Source: RefGenome
  6. membrane Source: UniProtKB-KW
  7. microtubule Source: UniProtKB-KW
  8. zonula adherens Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Kinesin-like protein KIFC3PRO_0000125431Add
BLAST

Proteomic databases

MaxQBiQ9BVG8.
PaxDbiQ9BVG8.
PRIDEiQ9BVG8.

PTM databases

PhosphoSiteiQ9BVG8.

Expressioni

Gene expression databases

BgeeiQ9BVG8.
CleanExiHS_KIFC3.
ExpressionAtlasiQ9BVG8. baseline and differential.
GenevestigatoriQ9BVG8.

Organism-specific databases

HPAiHPA021240.

Interactioni

Protein-protein interaction databases

BioGridi110002. 12 interactions.
IntActiQ9BVG8. 11 interactions.
MINTiMINT-4989557.
STRINGi9606.ENSP00000368976.

Structurei

Secondary structure

1
833
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi446 – 4527
Helixi457 – 4593
Helixi463 – 4653
Beta strandi469 – 4713
Beta strandi478 – 4836
Beta strandi486 – 4916
Beta strandi493 – 4964
Helixi502 – 5065
Turni507 – 5093
Helixi510 – 5178
Beta strandi522 – 5298
Helixi534 – 5385
Beta strandi542 – 5454
Helixi547 – 56014
Beta strandi566 – 57813
Beta strandi581 – 5844
Beta strandi614 – 6163
Helixi619 – 63214
Helixi644 – 6463
Beta strandi647 – 65913
Turni660 – 6623
Beta strandi665 – 67410
Helixi689 – 71224
Helixi720 – 7223
Helixi724 – 7285
Helixi730 – 7334
Beta strandi738 – 7458
Helixi749 – 7513
Helixi752 – 76514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H58X-ray1.85A443-770[»]
ProteinModelPortaliQ9BVG8.
SMRiQ9BVG8. Positions 445-766.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BVG8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini445 – 768324Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili102 – 362261Sequence AnalysisAdd
BLAST
Coiled coili395 – 43238Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00550000074610.
HOGENOMiHOG000116164.
HOVERGENiHBG052259.
InParanoidiQ9BVG8.
KOiK10406.
TreeFamiTF105238.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BVG8-3) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVPSRRTWNL GATPSLRGLW RVGRAPEPEP GMARPAPAPA SPAARPFPHT
60 70 80 90 100
GPGRLRTGRG KDTPVCGDED SSARSAARPA LAQCRALSVD WAGPGSPHGL
110 120 130 140 150
YLTLQVEHLK EKLISQAQEV SRLRSELGGT DLEKHRDLLM VENERLRQEM
160 170 180 190 200
RRCEAELQEL RTKPAGPCPG CEHSQESAQL RDKLSQLQLE MAESKGMLSE
210 220 230 240 250
LNLEVQQKTD RLAEVELRLK DCLAEKAQEE ERLSRRLRDS HETIASLRAQ
260 270 280 290 300
SPPVKYVIKT VEVESSKTKQ ALSESQARNQ HLQEQVAMQR QVLKEMEQQL
310 320 330 340 350
QSSHQLTARL RAQIAMYESE LERAHGQMLE EMQSLEEDKN RAIEEAFARA
360 370 380 390 400
QVEMKAVHEN LAGVRTNLLT LQPALRTLTN DYNGLKRQVR GFPLLLQEAL
410 420 430 440 450
RSVKAEIGQA IEEVNSNNQE LLRKYRRELQ LRKKCHNELV RLKGNIRVIA
460 470 480 490 500
RVRPVTKEDG EGPEATNAVT FDADDDSIIH LLHKGKPVSF ELDKVFSPQA
510 520 530 540 550
SQQDVFQEVQ ALVTSCIDGF NVCIFAYGQT GAGKTYTMEG TAENPGINQR
560 570 580 590 600
ALQLLFSEVQ EKASDWEYTI TVSAAEIYNE VLRDLLGKEP QEKLEIRLCP
610 620 630 640 650
DGSGQLYVPG LTEFQVQSVD DINKVFEFGH TNRTTEFTNL NEHSSRSHAL
660 670 680 690 700
LIVTVRGVDC STGLRTTGKL NLVDLAGSER VGKSGAEGSR LREAQHINKS
710 720 730 740 750
LSALGDVIAA LRSRQGHVPF RNSKLTYLLQ DSLSGDSKTL MVVQVSPVEK
760 770 780 790 800
NTSETLYSLK FAERVRSVEL GPGLRRAELG SWSSQEHLEW EPACQTPQPS
810 820 830
ARAHSAPSSG TSSRPGSIRR KLQPSGKSRP LPV

Note: No experimental confirmation available.

Length:833
Mass (Da):92,775
Last modified:November 16, 2011 - v4
Checksum:i50983587270BDC2F
GO
Isoform 2 (identifier: Q9BVG8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     826-833: GKSRPLPV → A

Show »
Length:826
Mass (Da):92,011
Checksum:iFA9B17728E570AE8
GO
Isoform 3 (identifier: Q9BVG8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     626-637: FEFGHTNRTTEF → WRREPLTTATLL
     638-833: Missing.

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.

Show »
Length:637
Mass (Da):71,607
Checksum:i367120F4FC3C3B78
GO
Isoform 4 (identifier: Q9BVG8-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.
     826-833: GKSRPLPV → A

Note: No experimental confirmation available.

Show »
Length:687
Mass (Da):77,089
Checksum:iEA21C203FC8B29A8
GO

Sequence cautioni

The sequence AAH34234.1 differs from that shown. Reason: Intron retention.
The sequence AAH41132.1 differs from that shown. Reason: Intron retention.
The sequence AAH47051.1 differs from that shown. Reason: Intron retention.
The sequence BAD92527.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501M → L in AAC24153. (PubMed:9782090)Curated
Sequence conflicti185 – 1851S → P in AAH34234. (PubMed:15489334)Curated
Sequence conflicti281 – 2811H → S in AAH08014. (PubMed:15489334)Curated
Sequence conflicti736 – 7361D → G in AAH34234. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911G → V.1 Publication
Corresponds to variant rs17854089 [ dbSNP | Ensembl ].
VAR_028114

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 4. 1 PublicationVSP_043724Add
BLAST
Alternative sequencei626 – 63712FEFGH…RTTEF → WRREPLTTATLL in isoform 3. 1 PublicationVSP_022361Add
BLAST
Alternative sequencei638 – 833196Missing in isoform 3. 1 PublicationVSP_022362Add
BLAST
Alternative sequencei826 – 8338GKSRPLPV → A in isoform 2 and isoform 4. 4 PublicationsVSP_021018

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK291737 mRNA. Translation: BAF84426.1.
AB209290 mRNA. Translation: BAD92527.1. Different initiation.
AC092118 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW82955.1.
BC001211 mRNA. Translation: AAH01211.2.
BC008014 mRNA. Translation: AAH08014.1.
BC034234 mRNA. Translation: AAH34234.1. Different initiation.
BC041132 mRNA. Translation: AAH41132.1. Different initiation.
BC047051 mRNA. Translation: AAH47051.1. Sequence problems.
AF004426 mRNA. Translation: AAC24153.1.
CCDSiCCDS10789.2. [Q9BVG8-3]
CCDS45493.1. [Q9BVG8-2]
CCDS45494.1. [Q9BVG8-5]
RefSeqiNP_001123571.1. NM_001130099.1. [Q9BVG8-5]
NP_001123572.1. NM_001130100.1. [Q9BVG8-2]
NP_005541.3. NM_005550.3. [Q9BVG8-3]
UniGeneiHs.23131.

Genome annotation databases

EnsembliENST00000379655; ENSP00000368976; ENSG00000140859. [Q9BVG8-3]
ENST00000421376; ENSP00000396399; ENSG00000140859. [Q9BVG8-5]
ENST00000445690; ENSP00000401696; ENSG00000140859. [Q9BVG8-2]
ENST00000465878; ENSP00000454659; ENSG00000140859. [Q9BVG8-5]
ENST00000562903; ENSP00000456239; ENSG00000140859. [Q9BVG8-5]
ENST00000564136; ENSP00000458009; ENSG00000140859.
GeneIDi3801.
KEGGihsa:3801.
UCSCiuc002emm.3. human. [Q9BVG8-5]
uc002emp.3. human. [Q9BVG8-3]
uc002emq.3. human. [Q9BVG8-2]

Polymorphism databases

DMDMi357529584.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK291737 mRNA. Translation: BAF84426.1 .
AB209290 mRNA. Translation: BAD92527.1 . Different initiation.
AC092118 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW82955.1 .
BC001211 mRNA. Translation: AAH01211.2 .
BC008014 mRNA. Translation: AAH08014.1 .
BC034234 mRNA. Translation: AAH34234.1 . Different initiation.
BC041132 mRNA. Translation: AAH41132.1 . Different initiation.
BC047051 mRNA. Translation: AAH47051.1 . Sequence problems.
AF004426 mRNA. Translation: AAC24153.1 .
CCDSi CCDS10789.2. [Q9BVG8-3 ]
CCDS45493.1. [Q9BVG8-2 ]
CCDS45494.1. [Q9BVG8-5 ]
RefSeqi NP_001123571.1. NM_001130099.1. [Q9BVG8-5 ]
NP_001123572.1. NM_001130100.1. [Q9BVG8-2 ]
NP_005541.3. NM_005550.3. [Q9BVG8-3 ]
UniGenei Hs.23131.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H58 X-ray 1.85 A 443-770 [» ]
ProteinModelPortali Q9BVG8.
SMRi Q9BVG8. Positions 445-766.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110002. 12 interactions.
IntActi Q9BVG8. 11 interactions.
MINTi MINT-4989557.
STRINGi 9606.ENSP00000368976.

Chemistry

ChEMBLi CHEMBL1075119.

PTM databases

PhosphoSitei Q9BVG8.

Polymorphism databases

DMDMi 357529584.

Proteomic databases

MaxQBi Q9BVG8.
PaxDbi Q9BVG8.
PRIDEi Q9BVG8.

Protocols and materials databases

DNASUi 3801.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379655 ; ENSP00000368976 ; ENSG00000140859 . [Q9BVG8-3 ]
ENST00000421376 ; ENSP00000396399 ; ENSG00000140859 . [Q9BVG8-5 ]
ENST00000445690 ; ENSP00000401696 ; ENSG00000140859 . [Q9BVG8-2 ]
ENST00000465878 ; ENSP00000454659 ; ENSG00000140859 . [Q9BVG8-5 ]
ENST00000562903 ; ENSP00000456239 ; ENSG00000140859 . [Q9BVG8-5 ]
ENST00000564136 ; ENSP00000458009 ; ENSG00000140859 .
GeneIDi 3801.
KEGGi hsa:3801.
UCSCi uc002emm.3. human. [Q9BVG8-5 ]
uc002emp.3. human. [Q9BVG8-3 ]
uc002emq.3. human. [Q9BVG8-2 ]

Organism-specific databases

CTDi 3801.
GeneCardsi GC16M057792.
HGNCi HGNC:6326. KIFC3.
HPAi HPA021240.
MIMi 604535. gene.
neXtProti NX_Q9BVG8.
PharmGKBi PA30112.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
GeneTreei ENSGT00550000074610.
HOGENOMi HOG000116164.
HOVERGENi HBG052259.
InParanoidi Q9BVG8.
KOi K10406.
TreeFami TF105238.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSi KIFC3. human.
EvolutionaryTracei Q9BVG8.
GeneWikii KIFC3.
GenomeRNAii 3801.
NextBioi 14931.
PROi Q9BVG8.
SOURCEi Search...

Gene expression databases

Bgeei Q9BVG8.
CleanExi HS_KIFC3.
ExpressionAtlasi Q9BVG8. baseline and differential.
Genevestigatori Q9BVG8.

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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Placenta.
  2. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    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.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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), VARIANT VAL-391.
    Tissue: Brain, Muscle and Testis.
  6. "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."
    Hoang E.H., Whitehead J.L., Dose A.C., Burnside B.
    Genomics 52:219-222(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-833 (ISOFORM 2).
    Tissue: Retina.
  7. "Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts."
    Meng W., Mushika Y., Ichii T., Takeichi M.
    Cell 135:948-959(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Crystal structure of the KIFC3 motor domain in complex with ADP."
    Structural genomics consortium (SGC)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 443-770 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiKIFC3_HUMAN
AccessioniPrimary (citable) accession number: Q9BVG8
Secondary accession number(s): A8K6S2
, O75299, Q49A29, Q49AQ0, Q59G19, Q8IUT3, Q96HW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 16, 2011
Last modified: October 29, 2014
This is version 126 of the entry and version 4 of the sequence. [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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3