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Protein

Kinesin-like protein KIFC3

Gene

KIFC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • microtubule motor activity Source: ProtInc

GO - Biological processi

  • epithelial cell-cell adhesion Source: UniProtKB
  • Golgi organization Source: Ensembl
  • metabolic process Source: GOC
  • microtubule-based movement Source: GO_Central
  • visual perception Source: ProtInc
  • 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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:6326. KIFC3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • kinesin complex Source: ProtInc
  • microtubule Source: UniProtKB-KW
  • zonula adherens Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30112.

Polymorphism and mutation databases

BioMutaiKIFC3.
DMDMi357529584.

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.
GenevisibleiQ9BVG8. HS.

Organism-specific databases

HPAiHPA021240.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-2125614,EBI-743598
AESQ081173EBI-2125614,EBI-717810
ATF2P153363EBI-2125614,EBI-1170906
BCL6P411823EBI-2125614,EBI-765407
C1orf109Q9NX044EBI-2125614,EBI-8643161
CBX8Q9HC523EBI-2125614,EBI-712912
CCDC102BA1A4H13EBI-2125614,EBI-10171570
CCDC136Q96JN2-23EBI-2125614,EBI-10171416
CCDC28AQ7Z6N93EBI-2125614,EBI-10258115
CCDC28AQ8IWP93EBI-2125614,EBI-355471
CCDC67Q05D603EBI-2125614,EBI-748597
CDK18Q070023EBI-2125614,EBI-746238
CDR2Q018503EBI-2125614,EBI-1181367
CEP170P1Q96L144EBI-2125614,EBI-743488
CEP55D3DR373EBI-2125614,EBI-10173536
CEP57L1Q8IYX8-23EBI-2125614,EBI-10181988
CLIP4Q8N3C73EBI-2125614,EBI-5655540
CREB5Q02930-33EBI-2125614,EBI-10192698
CYTH4Q8WWE83EBI-2125614,EBI-10277443
DCTN2Q135613EBI-2125614,EBI-715074
DCXO436023EBI-2125614,EBI-8646694
DTNBP1Q96EV83EBI-2125614,EBI-465804
ESRRGP625083EBI-2125614,EBI-2834260
FAM124AQ86V423EBI-2125614,EBI-744506
FANCLQ9NW383EBI-2125614,EBI-2339898
FCHSD2O948683EBI-2125614,EBI-1215612
FLJ13057Q53SE73EBI-2125614,EBI-10172181
GOLGA2Q083793EBI-2125614,EBI-618309
GORASP2Q9H8Y83EBI-2125614,EBI-739467
HAUS1Q96CS23EBI-2125614,EBI-2514791
HSBP1O755065EBI-2125614,EBI-748664
ICA1LQ8NDH63EBI-2125614,EBI-10269733
ITGB3BPQ133523EBI-2125614,EBI-712105
ITGB3BPQ13352-53EBI-2125614,EBI-10175826
KANSL1I3L4J33EBI-2125614,EBI-10178305
KRT15P190123EBI-2125614,EBI-739566
KRT19P087273EBI-2125614,EBI-742756
KRT31Q153233EBI-2125614,EBI-948001
KRT40Q6A1623EBI-2125614,EBI-10171697
KRT5P136473EBI-2125614,EBI-702187
KRT6AP025385EBI-2125614,EBI-702198
KRT6BP042593EBI-2125614,EBI-740907
KRT6CP486683EBI-2125614,EBI-2564105
LENG1Q96BZ83EBI-2125614,EBI-726510
LIN37Q96GY33EBI-2125614,EBI-748884
LZTS2Q9BRK43EBI-2125614,EBI-741037
MCM7P339933EBI-2125614,EBI-355924
MED4Q9NPJ63EBI-2125614,EBI-394607
MFAP1P550813EBI-2125614,EBI-1048159
MID2Q9UJV3-23EBI-2125614,EBI-10172526
MOSP005403EBI-2125614,EBI-1757866
NDEL1Q9GZM83EBI-2125614,EBI-928842
NECAB2H3BTW23EBI-2125614,EBI-10172876
NEFLI6L9F63EBI-2125614,EBI-10178578
NUP62P371983EBI-2125614,EBI-347978
PHC2Q8IXK03EBI-2125614,EBI-713786
PRKAA2P546464EBI-2125614,EBI-1383852
PSMB1P206183EBI-2125614,EBI-372273
RAD51DO757713EBI-2125614,EBI-1055693
RSPH14Q9UHP63EBI-2125614,EBI-748350
SCELO951713EBI-2125614,EBI-7543896
SIAH1Q8IUQ43EBI-2125614,EBI-747107
SMARCE1Q969G34EBI-2125614,EBI-455078
SOX5P357113EBI-2125614,EBI-3505701
SPERTQ8NA615EBI-2125614,EBI-741724
SYCE1Q8N0S23EBI-2125614,EBI-6872807
TCEANCQ8N8B73EBI-2125614,EBI-954696
TNIP1Q150253EBI-2125614,EBI-357849
TPM3Q5VU623EBI-2125614,EBI-10184033
TRAF2Q129333EBI-2125614,EBI-355744
TRIM23P364063EBI-2125614,EBI-740098
TRIM27P143733EBI-2125614,EBI-719493
TRIM41Q8WV443EBI-2125614,EBI-725997
TRIM54Q9BYV23EBI-2125614,EBI-2130429
TSG101Q998163EBI-2125614,EBI-346882
TSR2Q969E83EBI-2125614,EBI-746981
USP2O756043EBI-2125614,EBI-743272
ZBTB8AQ96BR93EBI-2125614,EBI-742740
ZGPATQ8N5A54EBI-2125614,EBI-3439227
ZGPATQ8N5A5-23EBI-2125614,EBI-10183064
ZNF180Q9UJW83EBI-2125614,EBI-10322527
ZNF20P170243EBI-2125614,EBI-717634
ZNF572A1L4E93EBI-2125614,EBI-10172590
ZNF572Q7Z3I73EBI-2125614,EBI-10257016
ZNF655Q8N7203EBI-2125614,EBI-625509

Protein-protein interaction databases

BioGridi110002. 95 interactions.
IntActiQ9BVG8. 89 interactions.
MINTiMINT-4989557.
STRINGi9606.ENSP00000368976.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiLTEFRVQ.
OrthoDBiEOG72G16X.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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
Isoform 5 (identifier: Q9BVG8-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCASACKDTAAWCPEEAAEPQAM
     826-833: GKSRPLPV → A

Note: No experimental confirmation available.
Show »
Length:848
Mass (Da):94,276
Checksum:i23229203DAE90BDF
GO

Sequence cautioni

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

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 sequencei1 – 11M → MCASACKDTAAWCPEEAAEP QAM in isoform 5. 1 PublicationVSP_057224
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, isoform 4 and isoform 5. 4 PublicationsVSP_021018

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291737 mRNA. Translation: BAF84426.1.
AK296995 mRNA. Translation: BAH12470.1.
AB209290 mRNA. Translation: BAD92527.1. Different initiation.
AC010543 Genomic DNA. No translation available.
AC092118 Genomic DNA. No translation available.
FO082293 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]
XP_011521382.1. XM_011523080.1. [Q9BVG8-5]
UniGeneiHs.23131.

Genome annotation databases

EnsembliENST00000379655; ENSP00000368976; ENSG00000140859.
ENST00000421376; ENSP00000396399; ENSG00000140859. [Q9BVG8-5]
ENST00000445690; ENSP00000401696; ENSG00000140859. [Q9BVG8-2]
ENST00000465878; ENSP00000454659; ENSG00000140859. [Q9BVG8-5]
ENST00000541240; ENSP00000442008; ENSG00000140859. [Q9BVG8-6]
ENST00000562903; ENSP00000456239; ENSG00000140859. [Q9BVG8-5]
GeneIDi3801.
KEGGihsa:3801.
UCSCiuc002emm.3. human. [Q9BVG8-5]
uc002emp.3. human. [Q9BVG8-3]
uc002emq.3. human. [Q9BVG8-2]
uc010vhz.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291737 mRNA. Translation: BAF84426.1.
AK296995 mRNA. Translation: BAH12470.1.
AB209290 mRNA. Translation: BAD92527.1. Different initiation.
AC010543 Genomic DNA. No translation available.
AC092118 Genomic DNA. No translation available.
FO082293 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]
XP_011521382.1. XM_011523080.1. [Q9BVG8-5]
UniGeneiHs.23131.

3D structure databases

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

Protein-protein interaction databases

BioGridi110002. 95 interactions.
IntActiQ9BVG8. 89 interactions.
MINTiMINT-4989557.
STRINGi9606.ENSP00000368976.

Chemistry

ChEMBLiCHEMBL1075119.

PTM databases

PhosphoSiteiQ9BVG8.

Polymorphism and mutation databases

BioMutaiKIFC3.
DMDMi357529584.

Proteomic databases

MaxQBiQ9BVG8.
PaxDbiQ9BVG8.
PRIDEiQ9BVG8.

Protocols and materials databases

DNASUi3801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379655; ENSP00000368976; ENSG00000140859.
ENST00000421376; ENSP00000396399; ENSG00000140859. [Q9BVG8-5]
ENST00000445690; ENSP00000401696; ENSG00000140859. [Q9BVG8-2]
ENST00000465878; ENSP00000454659; ENSG00000140859. [Q9BVG8-5]
ENST00000541240; ENSP00000442008; ENSG00000140859. [Q9BVG8-6]
ENST00000562903; ENSP00000456239; ENSG00000140859. [Q9BVG8-5]
GeneIDi3801.
KEGGihsa:3801.
UCSCiuc002emm.3. human. [Q9BVG8-5]
uc002emp.3. human. [Q9BVG8-3]
uc002emq.3. human. [Q9BVG8-2]
uc010vhz.2. human.

Organism-specific databases

CTDi3801.
GeneCardsiGC16M057792.
HGNCiHGNC:6326. KIFC3.
HPAiHPA021240.
MIMi604535. gene.
neXtProtiNX_Q9BVG8.
PharmGKBiPA30112.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00550000074610.
HOGENOMiHOG000116164.
HOVERGENiHBG052259.
InParanoidiQ9BVG8.
KOiK10406.
OMAiLTEFRVQ.
OrthoDBiEOG72G16X.
TreeFamiTF105238.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiKIFC3. human.
EvolutionaryTraceiQ9BVG8.
GeneWikiiKIFC3.
GenomeRNAii3801.
NextBioi14931.
PROiQ9BVG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVG8.
CleanExiHS_KIFC3.
ExpressionAtlasiQ9BVG8. baseline and differential.
GenevisibleiQ9BVG8. HS.

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.
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Publicationsi

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  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] (ISOFORMS 4 AND 5).
    Tissue: Placenta and Tongue.
  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
, B7Z484, O75299, Q49A29, Q49AQ0, Q59G19, Q8IUT3, Q96HW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 16, 2011
Last modified: July 22, 2015
This is version 135 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

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 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.