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Q9NSK0

- KLC4_HUMAN

UniProt

Q9NSK0 - KLC4_HUMAN

Protein

Kinesin light chain 4

Gene

KLC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    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

    1. microtubule motor activity Source: InterPro

    Keywords - Molecular functioni

    Motor protein

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21624. KLC4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. kinesin complex Source: InterPro
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134934134.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 619618Kinesin light chain 4PRO_0000215097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei460 – 4601Phosphoserine3 Publications
    Modified residuei590 – 5901Phosphoserine5 Publications
    Modified residuei612 – 6121Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NSK0.
    PaxDbiQ9NSK0.
    PRIDEiQ9NSK0.

    PTM databases

    PhosphoSiteiQ9NSK0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NSK0.
    BgeeiQ9NSK0.
    CleanExiHS_KLC4.
    GenevestigatoriQ9NSK0.

    Organism-specific databases

    HPAiHPA030168.
    HPA030169.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi124648. 21 interactions.
    IntActiQ9NSK0. 4 interactions.
    MINTiMINT-4999921.
    STRINGi9606.ENSP00000259708.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NSK0.
    SMRiQ9NSK0. Positions 65-90, 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 coili32 – 150119Sequence 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

    eggNOGiCOG0457.
    HOGENOMiHOG000261663.
    HOVERGENiHBG006217.
    InParanoidiQ9NSK0.
    KOiK10407.
    OMAiMSKSRHR.
    OrthoDBiEOG7TXKGD.
    PhylomeDBiQ9NSK0.
    TreeFamiTF314010.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR002151. 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]
    PfamiPF09311. Rab5-bind. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    PRINTSiPR00381. KINESINLIGHT.
    SMARTiSM00028. TPR. 4 hits.
    [Graphical view]
    PROSITEiPS01160. KINESIN_LIGHT. 3 hits.
    PS50005. TPR. 6 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NSK0-1) [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

    MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT    50
    IECLQQGGHE EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES 100
    EKQKLRAQVR RLCQENQWLR DELAGTQQRL QRSEQAVAQL EEEKKHLEFL 150
    GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP NEEEEDPSNG LSRGQGATAA 200
    QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED LERTSGRGHP 250
    DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN 300
    LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ 350
    GKYEAVERYY QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET 400
    LYKEILTRAH VQEFGSVDDD HKPIWMHAEE REEMSKSRHH EGGTPYAEYG 450
    GWYKACKVSS PTVNTTLRNL GALYRRQGKL EAAETLEECA LRSRRQGTDP 500
    ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE WSGDGSGTLQ 550
    RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA 600
    PLQVSRGLSA STMDLSSSS 619
    Length:619
    Mass (Da):68,640
    Last modified:October 17, 2006 - v3
    Checksum:i32DFC2A9A91B5574
    GO
    Isoform 2 (identifier: Q9NSK0-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:131
    Mass (Da):13,682
    Checksum:i18DB578896960243
    GO
    Isoform 3 (identifier: Q9NSK0-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:637
    Mass (Da):70,552
    Checksum:iCAA62901967C6918
    GO
    Isoform 4 (identifier: Q9NSK0-4) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:315
    Mass (Da):35,102
    Checksum:iB2F27C231C949391
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541L → LQTIECL in BAC87179. (PubMed:14702039)Curated
    Sequence conflicti286 – 2861T → S in BAG51695. (PubMed:14702039)Curated
    Sequence conflicti366 – 3661I → T in BAG51695. (PubMed:14702039)Curated
    Sequence conflicti434 – 4341M → L in BAG52815. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721R → H.1 Publication
    Corresponds to variant rs11558979 [ dbSNP | Ensembl ].
    VAR_049708

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEVTGFGVTRPGKVPQARM in isoform 3. 1 PublicationVSP_038083
    Alternative sequencei87 – 13145VMLAL…QQRLQ → NLELRGCAHLGDAGSSQPPE HSGVGETEAAGSGAAAMPGE PVAAG in isoform 2. 1 PublicationVSP_037875Add
    BLAST
    Alternative sequencei132 – 619488Missing in isoform 2. 1 PublicationVSP_037876Add
    BLAST
    Alternative sequencei295 – 31521AATLN…YKEAE → SIPCPPHPTPRTPHHCCFGL S in isoform 4. 1 PublicationVSP_043324Add
    BLAST
    Alternative sequencei316 – 619304Missing in isoform 4. 1 PublicationVSP_043325Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47429.1. [Q9NSK0-4]
    CCDS4882.1. [Q9NSK0-3]
    CCDS4883.1. [Q9NSK0-1]
    PIRiT47147.
    RefSeqiNP_001275963.1. NM_001289034.1. [Q9NSK0-1]
    NP_001275964.1. NM_001289035.1.
    NP_612352.1. NM_138343.3. [Q9NSK0-4]
    NP_958929.1. NM_201521.2. [Q9NSK0-1]
    NP_958930.1. NM_201522.2. [Q9NSK0-1]
    NP_958931.1. NM_201523.2. [Q9NSK0-3]
    UniGeneiHs.655123.

    Genome annotation databases

    EnsembliENST00000259708; ENSP00000259708; ENSG00000137171. [Q9NSK0-3]
    ENST00000347162; ENSP00000340221; ENSG00000137171. [Q9NSK0-1]
    ENST00000394056; ENSP00000377620; ENSG00000137171. [Q9NSK0-1]
    ENST00000458460; ENSP00000410358; ENSG00000137171. [Q9NSK0-4]
    ENST00000467906; ENSP00000418759; ENSG00000137171. [Q9NSK0-2]
    ENST00000479388; ENSP00000418031; ENSG00000137171. [Q9NSK0-1]
    GeneIDi89953.
    KEGGihsa:89953.
    UCSCiuc003otu.3. human. [Q9NSK0-4]
    uc003otv.1. human. [Q9NSK0-1]
    uc003otw.1. human. [Q9NSK0-3]

    Polymorphism databases

    DMDMi116242607.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS47429.1. [Q9NSK0-4 ]
    CCDS4882.1. [Q9NSK0-3 ]
    CCDS4883.1. [Q9NSK0-1 ]
    PIRi T47147.
    RefSeqi NP_001275963.1. NM_001289034.1. [Q9NSK0-1 ]
    NP_001275964.1. NM_001289035.1.
    NP_612352.1. NM_138343.3. [Q9NSK0-4 ]
    NP_958929.1. NM_201521.2. [Q9NSK0-1 ]
    NP_958930.1. NM_201522.2. [Q9NSK0-1 ]
    NP_958931.1. NM_201523.2. [Q9NSK0-3 ]
    UniGenei Hs.655123.

    3D structure databases

    ProteinModelPortali Q9NSK0.
    SMRi Q9NSK0. Positions 65-90, 192-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124648. 21 interactions.
    IntActi Q9NSK0. 4 interactions.
    MINTi MINT-4999921.
    STRINGi 9606.ENSP00000259708.

    PTM databases

    PhosphoSitei Q9NSK0.

    Polymorphism databases

    DMDMi 116242607.

    Proteomic databases

    MaxQBi Q9NSK0.
    PaxDbi Q9NSK0.
    PRIDEi Q9NSK0.

    Protocols and materials databases

    DNASUi 89953.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259708 ; ENSP00000259708 ; ENSG00000137171 . [Q9NSK0-3 ]
    ENST00000347162 ; ENSP00000340221 ; ENSG00000137171 . [Q9NSK0-1 ]
    ENST00000394056 ; ENSP00000377620 ; ENSG00000137171 . [Q9NSK0-1 ]
    ENST00000458460 ; ENSP00000410358 ; ENSG00000137171 . [Q9NSK0-4 ]
    ENST00000467906 ; ENSP00000418759 ; ENSG00000137171 . [Q9NSK0-2 ]
    ENST00000479388 ; ENSP00000418031 ; ENSG00000137171 . [Q9NSK0-1 ]
    GeneIDi 89953.
    KEGGi hsa:89953.
    UCSCi uc003otu.3. human. [Q9NSK0-4 ]
    uc003otv.1. human. [Q9NSK0-1 ]
    uc003otw.1. human. [Q9NSK0-3 ]

    Organism-specific databases

    CTDi 89953.
    GeneCardsi GC06P043008.
    HGNCi HGNC:21624. KLC4.
    HPAi HPA030168.
    HPA030169.
    neXtProti NX_Q9NSK0.
    PharmGKBi PA134934134.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000261663.
    HOVERGENi HBG006217.
    InParanoidi Q9NSK0.
    KOi K10407.
    OMAi MSKSRHR.
    OrthoDBi EOG7TXKGD.
    PhylomeDBi Q9NSK0.
    TreeFami TF314010.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.

    Miscellaneous databases

    GeneWikii KLC4.
    GenomeRNAii 89953.
    NextBioi 76452.
    PROi Q9NSK0.

    Gene expression databases

    ArrayExpressi Q9NSK0.
    Bgeei Q9NSK0.
    CleanExi HS_KLC4.
    Genevestigatori Q9NSK0.

    Family and domain databases

    Gene3Di 1.25.40.10. 3 hits.
    InterProi 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 ]
    Pfami PF09311. Rab5-bind. 1 hit.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00381. KINESINLIGHT.
    SMARTi SM00028. TPR. 4 hits.
    [Graphical view ]
    PROSITEi PS01160. KINESIN_LIGHT. 3 hits.
    PS50005. TPR. 6 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKLC4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSK0
    Secondary accession number(s): B3KNY4
    , B3KPI3, B3KSQ3, Q66K28, Q96EG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3