Q9BW19 (KIFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIFC1

Alternative name(s):
Kinesin-like protein 2
Kinesin-related protein HSET

Gene names

Name:	KIFC1
Synonyms:	HSET, KNSL2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. Ref.5
Subunit structure	Binds NUBP1 and NUBP2. Interacts with PPP1R42 By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Early endosome By similarity. Note: Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis By similarity.
Miscellaneous	HeLa cells lacking KIFC1 show multipolar mitotic spindles and a defect in chromosome congression and chromosome alignment during mitosis.
Sequence similarities	Belongs to the kinesin-like protein family. NCD subfamily. Contains 1 kinesin-motor domain.
Sequence caution	The sequence AAH00712.2 differs from that shown. Reason: Erroneous initiation. The sequence AAH63567.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH73878.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH98438.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA03509.1 differs from that shown. Reason: Frameshift at positions 223 and 256.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Endosome Microtubule Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Traceable author statement. Source: Reactome mitotic sister chromatid segregation Non-traceable author statement Ref.4. Source: UniProtKB
Cellular_component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Non-traceable author statement. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Non-traceable author statement Ref.4. Source: UniProtKB microtubule motor activity Non-traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 673

673

Kinesin-like protein KIFC1

PRO_0000125428

Regions

Domain

307 – 594

288

Kinesin-motor

Nucleotide binding

410 – 417

8

ATP By similarity

Coiled coil

142 – 306

165

Potential

Amino acid modifications

Modified residue

31

1

Phosphoserine Ref.7

Modified residue

33

1

Phosphoserine By similarity

Natural variations

Natural variant

219

1

R → Q. Ref.1

VAR_012650

Experimental info

Sequence conflict

368

1

T → P in AAH00712. Ref.3

Secondary structure

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673

Helix Strand Turn

Details...

Beta strand

311 – 317

7

Helix

329 – 331

3

Beta strand

347 – 349

3

Beta strand

371 – 373

3

Beta strand

375 – 378

4

Helix

384 – 396

13

Helix

397 – 400

4

Beta strand

404 – 409

6

Helix

416 – 420

5

Helix

428 – 430

3

Helix

433 – 447

15

Helix

448 – 451

4

Beta strand

453 – 465

13

Beta strand

468 – 471

4

Beta strand

487 – 489

3

Beta strand

497 – 499

3

Beta strand

505 – 507

3

Helix

510 – 526

17

Helix

535 – 537

3

Beta strand

538 – 553

16

Beta strand

556 – 565

10

Helix

596 – 607

12

Helix

615 – 617

3

Helix

619 – 623

5

Helix

625 – 627

3

Beta strand

633 – 640

8

Helix

644 – 646

3

Helix

647 – 660

14

Sequences

	Sequence		Length	Mass (Da)
	Q9BW19 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 9E99737665BF1E92	FASTA	673	73,748
	10 20 30 40 50 60 MDPQRSPLLE VKGNIELKRP LIKAPSQLPL SGSRLKRRPD QMEDGLEPEK KRTRGLGATT 70 80 90 100 110 120 KITTSHPRVP SLTTVPQTQG QTTAQKVSKK TGPRCSTAIA TGLKNQKPVP AVPVQKSGTS 130 140 150 160 170 180 GVPPMAGGKK PSKRPAWDLK GQLCDLNAEL KRCRERTQTL DQENQQLQDQ LRDAQQQVKA 190 200 210 220 230 240 LGTERTTLEG HLAKVQAQAE QGQQELKNLR ACVLELEERL STQEGLVQEL QKKQVELQEE 250 260 270 280 290 300 RRGLMSQLEE KERRLQTSEA ALSSSQAEVA SLRQETVAQA ALLTEREERL HGLEMERRRL 310 320 330 340 350 360 HNQLQELKGN IRVFCRVRPV LPGEPTPPPG LLLFPSGPGG PSDPPTRLSL SRSDERRGTL 370 380 390 400 410 420 SGAPAPPTRH DFSFDRVFPP GSGQDEVFEE IAMLVQSALD GYPVCIFAYG QTGSGKTFTM 430 440 450 460 470 480 EGGPGGDPQL EGLIPRALRH LFSVAQELSG QGWTYSFVAS YVEIYNETVR DLLATGTRKG 490 500 510 520 530 540 QGGECEIRRA GPGSEELTVT NARYVPVSCE KEVDALLHLA RQNRAVARTA QNERSSRSHS 550 560 570 580 590 600 VFQLQISGEH SSRGLQCGAP LSLVDLAGSE RLDPGLALGP GERERLRETQ AINSSLSTLG 610 620 630 640 650 660 LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI SPLEENVSES LNSLRFASKV 670 NQCVIGTAQA NRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization of the HSET locus and the possible association of HLA-linked genes with immotile cilia syndrome (ICS)." Janitz K., Wild A., Beck S., Savasta S., Beluffi G., Ziegler A., Volz A. Immunogenetics 49:644-652(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-219.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Brain, Kidney, Muscle and Uterus.
[4]	"Cloning of a new kinesin-related gene located at the centromeric end of the human MHC region." Ando A., Yara-Kikuti Y., Kawata H., Okamoto N., Imai T., Eki T., Yokoyama K., Soeda E., Ikemura T., Abe K., Inoko H. Immunogenetics 39:194-200(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 155-673. Tissue: Testis.
[5]	"Functional analysis of human microtubule-based motor proteins, the kinesins and dyneins, in mitosis/cytokinesis using RNA interference." Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B., Abraham R.T., Jiang W. Mol. Biol. Cell 16:3187-3199(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ010479 mRNA. Translation: CAA09217.1.
AL021366 Genomic DNA. Translation: CAA16157.1.
AL050332 Genomic DNA. Translation: CAB63782.1.
AL662799 Genomic DNA. Translation: CAI18269.1.
BX088650 Genomic DNA. Translation: CAM26294.1.
BX248088 Genomic DNA. Translation: CAI41792.1.
BC000712 mRNA. Translation: AAH00712.2. Different initiation.
BC063567 mRNA. Translation: AAH63567.1. Different initiation.
BC073878 mRNA. Translation: AAH73878.1. Different initiation.
BC098438 mRNA. Translation: AAH98438.1. Different initiation.
BC121041 mRNA. Translation: AAI21042.1.
BC121042 mRNA. Translation: AAI21043.1.
D14678 mRNA. Translation: BAA03509.1. Frameshift.

IPI

IPI00306400.

PIR

I54523.

RefSeq

NP_002254.2. NM_002263.3.

UniGene

Hs.436912.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2REP	X-ray	2.60	A	307-663	[»]

ProteinModelPortal

Q9BW19.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BW19. 4 interactions.

PTM databases

PhosphoSite

Q9BW19.

Polymorphism databases

DMDM

20138710.

Proteomic databases

PaxDb

Q9BW19.

PeptideAtlas

Q9BW19.

PRIDE

Q9BW19.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374523; ENSP00000363647; ENSG00000204197.
ENST00000428849; ENSP00000393963; ENSG00000237649.
ENST00000448818; ENSP00000407885; ENSG00000233450.

GeneID

3833.

KEGG

hsa:3833.

UCSC

uc003oef.4. human.

Organism-specific databases

CTD

3833.

GeneCards

GC06P033359.

HGNC

HGNC:6389. KIFC1.

HPA

HPA055997.

MIM

603763. gene.

neXtProt

NX_Q9BW19.

PharmGKB

PA30178.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOVERGEN

HBG001080.

InParanoid

Q9BW19.

KO

K10405.

OMA

QISGEHS.

OrthoDB

EOG412M52.

PhylomeDB

Q9BW19.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9BW19.

Bgee

Q9BW19.

CleanEx

HS_KIFC1.

Genevestigator

Q9BW19.

GermOnline

ENSG00000204197. Homo sapiens.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BW19.

GenomeRNAi

3833.

NextBio

15065.

SOURCE

Search...

Entry information

Entry name

KIFC1_HUMAN

Accession

Primary (citable) accession number: Q9BW19
Secondary accession number(s): O60887 , Q14834, Q4KMP0, Q5SU09, Q6GMS7, Q6P4A5, Q9UQP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.