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Protein

Kinesin light chain 4

Gene

Klc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin light chain 4
Short name:
KLC 4
Alternative name(s):
Kinesin-like protein 8
Gene namesi
Name:Klc4
Synonyms:Knsl8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1922014. Klc4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 619618Kinesin light chain 4PRO_0000215098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei566 – 5661PhosphoserineCombined sources
Modified residuei590 – 5901PhosphoserineCombined sources
Modified residuei612 – 6121PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBS5.
MaxQBiQ9DBS5.
PaxDbiQ9DBS5.
PRIDEiQ9DBS5.

PTM databases

iPTMnetiQ9DBS5.
PhosphoSiteiQ9DBS5.
SwissPalmiQ9DBS5.

Expressioni

Gene expression databases

BgeeiQ9DBS5.
CleanExiMM_KLC4.
GenevisibleiQ9DBS5. MM.

Interactioni

Subunit structurei

Oligomeric complex composed of two heavy chains and two light chains.By similarity

Protein-protein interaction databases

BioGridi217004. 8 interactions.
DIPiDIP-48704N.
IntActiQ9DBS5. 9 interactions.
MINTiMINT-4099881.
STRINGi10090.ENSMUSP00000003642.

Structurei

3D structure databases

ProteinModelPortaliQ9DBS5.
SMRiQ9DBS5. Positions 65-93, 192-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati55 – 8834TPR 1Add
BLAST
Repeati211 – 24434TPR 2Add
BLAST
Repeati253 – 28634TPR 3Add
BLAST
Repeati295 – 32834TPR 4Add
BLAST
Repeati337 – 37034TPR 5Add
BLAST
Repeati379 – 41234TPR 6Add
BLAST
Repeati464 – 49734TPR 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili65 – 15591Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the kinesin light chain family.Curated
Contains 7 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1840. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ9DBS5.
KOiK10407.
OMAiMSKSRHR.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ9DBS5.
TreeFamiTF314010.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13374. TPR_10. 2 hits.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLVLGQRD EPAGHRLSQE EILGSTKVVS QGLEALHSEH QAVLQSLSHT
60 70 80 90 100
IECLQQGGHE EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES
110 120 130 140 150
EKQKLRAQVR RLCQENQWLR DELAGTQQRL QRSEQAVAQL EEEKKHLEFL
160 170 180 190 200
RQLRQYDEDG HGMEEKEGEA TKDSLDDLFP NEEEEDSGND LSRGQGAAAA
210 220 230 240 250
QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED LERTSGRGHP
260 270 280 290 300
DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGRD HPAVAATLNN
310 320 330 340 350
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TDHPDVAKQL NNLALLCQNQ
360 370 380 390 400
GKYEAVERYY QRALAIYESQ LGPDNPNVAR TKNNLASCYL KQGKYSEAEA
410 420 430 440 450
LYKEILTCAH VQEFGSVDDD HKPIWMHAEE REEMSRSRPR DSSAPYAEYG
460 470 480 490 500
GWYKACRVSS PTVNTTLKNL GALYRRQGKL EAAETLEECA LRSRKQGTDP
510 520 530 540 550
ISQTKVAELL GEGDGRKAIQ EGPGDSVKFE GGEDASVAVE WSGDGSGTLQ
560 570 580 590 600
RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSSMKRAAS LNYLNQPNAA
610
PLQVSRGLSA STVDLSSSS
Length:619
Mass (Da):68,613
Last modified:April 27, 2001 - v1
Checksum:iBE2D6B3CD451A7BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004774 mRNA. Translation: BAB23552.1.
AK170793 mRNA. Translation: BAE42032.1.
CCDSiCCDS28832.1.
RefSeqiNP_083367.1. NM_029091.2.
XP_006525106.1. XM_006525043.2.
XP_011244990.1. XM_011246688.1.
XP_011244991.1. XM_011246689.1.
UniGeneiMm.279599.

Genome annotation databases

EnsembliENSMUST00000003642; ENSMUSP00000003642; ENSMUSG00000003546.
GeneIDi74764.
KEGGimmu:74764.
UCSCiuc008ctj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004774 mRNA. Translation: BAB23552.1.
AK170793 mRNA. Translation: BAE42032.1.
CCDSiCCDS28832.1.
RefSeqiNP_083367.1. NM_029091.2.
XP_006525106.1. XM_006525043.2.
XP_011244990.1. XM_011246688.1.
XP_011244991.1. XM_011246689.1.
UniGeneiMm.279599.

3D structure databases

ProteinModelPortaliQ9DBS5.
SMRiQ9DBS5. Positions 65-93, 192-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217004. 8 interactions.
DIPiDIP-48704N.
IntActiQ9DBS5. 9 interactions.
MINTiMINT-4099881.
STRINGi10090.ENSMUSP00000003642.

PTM databases

iPTMnetiQ9DBS5.
PhosphoSiteiQ9DBS5.
SwissPalmiQ9DBS5.

Proteomic databases

EPDiQ9DBS5.
MaxQBiQ9DBS5.
PaxDbiQ9DBS5.
PRIDEiQ9DBS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003642; ENSMUSP00000003642; ENSMUSG00000003546.
GeneIDi74764.
KEGGimmu:74764.
UCSCiuc008ctj.1. mouse.

Organism-specific databases

CTDi89953.
MGIiMGI:1922014. Klc4.

Phylogenomic databases

eggNOGiKOG1840. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ9DBS5.
KOiK10407.
OMAiMSKSRHR.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ9DBS5.
TreeFamiTF314010.

Miscellaneous databases

ChiTaRSiKlc4. mouse.
PROiQ9DBS5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBS5.
CleanExiMM_KLC4.
GenevisibleiQ9DBS5. MM.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13374. TPR_10. 2 hits.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Lung.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-566 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiKLC4_MOUSE
AccessioniPrimary (citable) accession number: Q9DBS5
Secondary accession number(s): Q3TCC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.