Q9NSK0 (KLC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin light chain 4
Short name=KLC 4

Alternative name(s):
Kinesin-like protein 8

Gene names

Name:	KLC4
Synonyms:	KNSL8

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	619 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity By similarity.
Subunit structure	Oligomeric complex composed of two heavy chains and two light chains By similarity.
Subcellular location	Cytoplasm › cytoskeleton Probable.
Sequence similarities	Belongs to the kinesin light chain family. Contains 7 TPR repeats.
Sequence caution	The sequence BAC86788.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat TPR repeat
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinesin complex Inferred from electronic annotation. Source: InterPro microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	microtubule motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NSK0-1)

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.

Isoform 2 (identifier: Q9NSK0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-131: VMLALASHLS...ELAGTQQRLQ → NLELRGCAHL...AMPGEPVAAG
     132-619: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Isoform 3 (identifier: Q9NSK0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEVTGFGVTRPGKVPQARM

Isoform 4 (identifier: Q9NSK0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     295-315: AATLNNLAVLYGKRGKYKEAE → SIPCPPHPTPRTPHHCCFGLS
     316-619: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 619	619	Kinesin light chain 4		PRO_0000215097
Regions
	Repeat	55 – 88	34	TPR 1
	Repeat	211 – 244	34	TPR 2
	Repeat	253 – 286	34	TPR 3
	Repeat	295 – 328	34	TPR 4
	Repeat	337 – 370	34	TPR 5
	Repeat	379 – 412	34	TPR 6
	Repeat	464 – 497	34	TPR 7
	Coiled coil	32 – 150	119	Potential
Amino acid modifications
	Modified residue	174	1	Phosphoserine By similarity
	Modified residue	460	1	Phosphoserine Ref.6 Ref.9 Ref.13
	Modified residue	566	1	Phosphoserine By similarity
	Modified residue	590	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.13
	Modified residue	612	1	Phosphothreonine Ref.11
Natural variations
	Alternative sequence	1	1	M → MEVTGFGVTRPGKVPQARM in isoform 3.		VSP_038083
	Alternative sequence	87 – 131	45	VMLAL…QQRLQ → NLELRGCAHLGDAGSSQPPE HSGVGETEAAGSGAAAMPGE PVAAG in isoform 2.		VSP_037875
	Alternative sequence	132 – 619	488	Missing in isoform 2.		VSP_037876
	Alternative sequence	295 – 315	21	AATLN…YKEAE → SIPCPPHPTPRTPHHCCFGL S in isoform 4.		VSP_043324
	Alternative sequence	316 – 619	304	Missing in isoform 4.		VSP_043325
	Natural variant	72	1	R → H. Ref.1 Corresponds to variant rs11558979 [ dbSNP | Ensembl ].		VAR_049708
Experimental info
	Sequence conflict	54	1	L → LQTIECL in BAC87179. Ref.1
	Sequence conflict	286	1	T → S in BAG51695. Ref.1
	Sequence conflict	366	1	I → T in BAG51695. Ref.1
	Sequence conflict	434	1	M → L in BAG52815. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 32DFC2A9A91B5574	FASTA	619	68,640
	10 20 30 40 50 60 MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE 70 80 90 100 110 120 EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR 130 140 150 160 170 180 DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP 190 200 210 220 230 240 NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED 250 260 270 280 290 300 LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN 310 320 330 340 350 360 LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ GKYEAVERYY 370 380 390 400 410 420 QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET LYKEILTRAH VQEFGSVDDD 430 440 450 460 470 480 HKPIWMHAEE REEMSKSRHH EGGTPYAEYG GWYKACKVSS PTVNTTLRNL GALYRRQGKL 490 500 510 520 530 540 EAAETLEECA LRSRRQGTDP ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE 550 560 570 580 590 600 WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA 610 PLQVSRGLSA STMDLSSSS
	Isoform 2 [UniParc]. Checksum: 18DB578896960243	FASTA	131	13,682
	10 20 30 40 50 60 MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE 70 80 90 100 110 120 EGLVHEKARQ LRRSMENIEL GLSEAQNLEL RGCAHLGDAG SSQPPEHSGV GETEAAGSGA 130 AAMPGEPVAA G
	Isoform 3 [UniParc]. Checksum: CAA62901967C6918	FASTA	637	70,552
	10 20 30 40 50 60 MEVTGFGVTR PGKVPQARMS GLVLGQRDEP AGHRLSQEEI LGSTRLVSQG LEALRSEHQA 70 80 90 100 110 120 VLQSLSQTIE CLQQGGHEEG LVHEKARQLR RSMENIELGL SEAQVMLALA SHLSTVESEK 130 140 150 160 170 180 QKLRAQVRRL CQENQWLRDE LAGTQQRLQR SEQAVAQLEE EKKHLEFLGQ LRQYDEDGHT 190 200 210 220 230 240 SEEKEGDATK DSLDDLFPNE EEEDPSNGLS RGQGATAAQQ GGYEIPARLR TLHNLVIQYA 250 260 270 280 290 300 AQGRYEVAVP LCKQALEDLE RTSGRGHPDV ATMLNILALV YRDQNKYKEA AHLLNDALSI 310 320 330 340 350 360 RESTLGPDHP AVAATLNNLA VLYGKRGKYK EAEPLCQRAL EIREKVLGTN HPDVAKQLNN 370 380 390 400 410 420 LALLCQNQGK YEAVERYYQR ALAIYEGQLG PDNPNVARTK NNLASCYLKQ GKYAEAETLY 430 440 450 460 470 480 KEILTRAHVQ EFGSVDDDHK PIWMHAEERE EMSKSRHHEG GTPYAEYGGW YKACKVSSPT 490 500 510 520 530 540 VNTTLRNLGA LYRRQGKLEA AETLEECALR SRRQGTDPIS QTKVAELLGE SDGRRTSQEG 550 560 570 580 590 600 PGDSVKFEGG EDASVAVEWS GDGSGTLQRS GSLGKIRDVL RRSSELLVRK LQGTEPRPSS 610 620 630 SNMKRAASLN YLNQPSAAPL QVSRGLSAST MDLSSSS
	Isoform 4 [UniParc]. Checksum: B2F27C231C949391	FASTA	315	35,102
	10 20 30 40 50 60 MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE 70 80 90 100 110 120 EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR 130 140 150 160 170 180 DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP 190 200 210 220 230 240 NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED 250 260 270 280 290 300 LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVSIPCPP 310 HPTPRTPHHC CFGLS

References

[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 1; 2 AND 3), VARIANT HIS-72. Tissue: Adrenal gland, Brain and Small intestine.
[2]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala and Esophageal carcinoma.
[3]	"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].
[4]	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 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] (ISOFORMS 1 AND 4). Tissue: Prostate and Skin.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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-590 AND THR-612, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK055293 mRNA. Translation: BAG51496.1. AK056393 mRNA. Translation: BAG51695.1. AK094102 mRNA. Translation: BAG52815.1. AK127018 mRNA. Translation: BAC86788.1. Sequence problems. AK127894 mRNA. Translation: BAC87179.1. AL162078 mRNA. Translation: CAB82411.1. AL136304 Genomic DNA. No translation available. AL355385 Genomic DNA. Translation: CAI13781.1. CH471081 Genomic DNA. Translation: EAX04149.1. BC012357 mRNA. Translation: AAH12357.1. BC080637 mRNA. Translation: AAH80637.1. BC103727 mRNA. Translation: AAI03728.1. BX640717 mRNA. Translation: CAE45836.1.
IPI	IPI00061476. IPI00398812. IPI00743879. IPI00788630.
PIR	T47147.
RefSeq	NP_612352.1. NM_138343.2. NP_958929.1. NM_201521.1. NP_958930.1. NM_201522.1. NP_958931.1. NM_201523.1.
UniGene	Hs.655123.
3D structure databases
ProteinModelPortal	Q9NSK0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NSK0. 3 interactions.
MINT	MINT-4999921.
STRING	9606.ENSP00000259708.
PTM databases
PhosphoSite	Q9NSK0.
Polymorphism databases
DMDM	116242607.
Proteomic databases
PaxDb	Q9NSK0.
PRIDE	Q9NSK0.
Protocols and materials databases
DNASU	89953.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259708; ENSP00000259708; ENSG00000137171. ENST00000347162; ENSP00000340221; ENSG00000137171. ENST00000394056; ENSP00000377620; ENSG00000137171. ENST00000394058; ENSP00000377622; ENSG00000137171. ENST00000458460; ENSP00000410358; ENSG00000137171. ENST00000467906; ENSP00000418759; ENSG00000137171. ENST00000479388; ENSP00000418031; ENSG00000137171.
GeneID	89953.
KEGG	hsa:89953.
UCSC	uc003otv.1. human. uc003otw.1. human.
Organism-specific databases
CTD	89953.
GeneCards	GC06P043008.
HGNC	HGNC:21624. KLC4.
HPA	HPA030168. HPA030169.
neXtProt	NX_Q9NSK0.
PharmGKB	PA134934134.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0457.
HOGENOM	HOG000261663.
HOVERGEN	HBG006217.
InParanoid	Q9NSK0.
KO	K10407.
OMA	MSKSRHR.
OrthoDB	EOG4NZTT0.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9NSK0.
Bgee	Q9NSK0.
CleanEx	HS_KLC4.
Genevestigator	Q9NSK0.
GermOnline	ENSG00000137171. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.10. 3 hits.
InterPro	IPR002151. Kinesin_light. IPR015792. Kinesin_light_repeat. IPR015390. Rabaptin_Rab5-bd_dom. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR013105. TPR_2. IPR019734. TPR_repeat. [Graphical view]
Pfam	PF09311. Rab5-bind. 1 hit. PF07719. TPR_2. 1 hit. [Graphical view]
PRINTS	PR00381. KINESINLIGHT.
SMART	SM00028. TPR. 4 hits. [Graphical view]
PROSITE	PS01160. KINESIN_LIGHT. 3 hits. PS50005. TPR. 6 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	89953.
NextBio	76452.

Entry information

Entry name

KLC4_HUMAN

Accession

Primary (citable) accession number: Q9NSK0
Secondary accession number(s): B3KNY4 , B3KPI3, B3KSQ3, Q66K28, Q96EG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 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.