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Q9NSK0 (KLC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin light chain 4

Short name=KLC 4
Alternative name(s):
Kinesin-like protein 8
Gene names
Name:KLC4
Synonyms:KNSL8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytoskeleton 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 componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
TPR repeat
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmicrotubule 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 619618Kinesin light chain 4
PRO_0000215097

Regions

Repeat55 – 8834TPR 1
Repeat211 – 24434TPR 2
Repeat253 – 28634TPR 3
Repeat295 – 32834TPR 4
Repeat337 – 37034TPR 5
Repeat379 – 41234TPR 6
Repeat464 – 49734TPR 7
Coiled coil32 – 150119 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.16
Modified residue4601Phosphoserine Ref.6 Ref.9 Ref.14
Modified residue5901Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue6121Phosphothreonine Ref.12

Natural variations

Alternative sequence11M → MEVTGFGVTRPGKVPQARM in isoform 3.
VSP_038083
Alternative sequence87 – 13145VMLAL…QQRLQ → NLELRGCAHLGDAGSSQPPE HSGVGETEAAGSGAAAMPGE PVAAG in isoform 2.
VSP_037875
Alternative sequence132 – 619488Missing in isoform 2.
VSP_037876
Alternative sequence295 – 31521AATLN…YKEAE → SIPCPPHPTPRTPHHCCFGL S in isoform 4.
VSP_043324
Alternative sequence316 – 619304Missing in isoform 4.
VSP_043325
Natural variant721R → H. Ref.1
Corresponds to variant rs11558979 [ dbSNP | Ensembl ].
VAR_049708

Experimental info

Sequence conflict541L → LQTIECL in BAC87179. Ref.1
Sequence conflict2861T → S in BAG51695. Ref.1
Sequence conflict3661I → T in BAG51695. Ref.1
Sequence conflict4341M → L in BAG52815. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 32DFC2A9A91B5574

FASTA61968,640
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 18DB578896960243
Show »

FASTA13113,682
Isoform 3 [UniParc].

Checksum: CAA62901967C6918
Show »

FASTA63770,552
Isoform 4 [UniParc].

Checksum: B2F27C231C949391
Show »

FASTA31535,102

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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRT47147.
RefSeqNP_001275963.1. NM_001289034.1.
NP_001275964.1. NM_001289035.1.
NP_612352.1. NM_138343.3.
NP_958929.1. NM_201521.2.
NP_958930.1. NM_201522.2.
NP_958931.1. NM_201523.2.
UniGeneHs.655123.

3D structure databases

ProteinModelPortalQ9NSK0.
SMRQ9NSK0. Positions 118-561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124648. 20 interactions.
IntActQ9NSK0. 4 interactions.
MINTMINT-4999921.
STRING9606.ENSP00000259708.

PTM databases

PhosphoSiteQ9NSK0.

Polymorphism databases

DMDM116242607.

Proteomic databases

PaxDbQ9NSK0.
PRIDEQ9NSK0.

Protocols and materials databases

DNASU89953.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259708; ENSP00000259708; ENSG00000137171. [Q9NSK0-3]
ENST00000347162; ENSP00000340221; ENSG00000137171. [Q9NSK0-1]
ENST00000394056; ENSP00000377620; ENSG00000137171. [Q9NSK0-1]
ENST00000394058; ENSP00000377622; ENSG00000137171. [Q9NSK0-1]
ENST00000458460; ENSP00000410358; ENSG00000137171. [Q9NSK0-4]
ENST00000467906; ENSP00000418759; ENSG00000137171. [Q9NSK0-2]
ENST00000479388; ENSP00000418031; ENSG00000137171. [Q9NSK0-1]
GeneID89953.
KEGGhsa:89953.
UCSCuc003otu.3. human. [Q9NSK0-4]
uc003otv.1. human. [Q9NSK0-1]
uc003otw.1. human. [Q9NSK0-3]

Organism-specific databases

CTD89953.
GeneCardsGC06P043008.
HGNCHGNC:21624. KLC4.
HPAHPA030168.
HPA030169.
neXtProtNX_Q9NSK0.
PharmGKBPA134934134.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000261663.
HOVERGENHBG006217.
InParanoidQ9NSK0.
KOK10407.
OMAMSKSRHR.
OrthoDBEOG7TXKGD.
TreeFamTF314010.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9NSK0.
BgeeQ9NSK0.
CleanExHS_KLC4.
GenevestigatorQ9NSK0.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR002151. 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]
PfamPF09311. Rab5-bind. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSPR00381. KINESINLIGHT.
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKLC4.
GenomeRNAi89953.
NextBio76452.
PROQ9NSK0.

Entry information

Entry nameKLC4_HUMAN
AccessionPrimary (citable) accession number: Q9NSK0
Secondary accession number(s): B3KNY4 expand/collapse secondary AC list , B3KPI3, B3KSQ3, Q66K28, Q96EG6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM