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Q9H0B6

- KLC2_HUMAN

UniProt

Q9H0B6 - KLC2_HUMAN

Protein

Kinesin light chain 2

Gene

KLC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. kinesin binding Source: BHF-UCL
    2. microtubule motor activity Source: InterPro
    3. protein binding Source: HGNC

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. axon cargo transport Source: Ensembl
    3. blood coagulation Source: Reactome
    4. microtubule-based movement Source: Reactome

    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 2
    Short name:
    KLC 2
    Gene namesi
    Name:KLC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:20716. KLC2.

    Subcellular locationi

    GO - Cellular componenti

    1. ciliary rootlet Source: Ensembl
    2. cytosol Source: HGNC
    3. kinesin complex Source: HGNC
    4. kinesin I complex Source: BHF-UCL
    5. membrane Source: UniProtKB
    6. microtubule Source: UniProtKB-KW
    7. neuron projection Source: Ensembl
    8. protein complex Source: LIFEdb

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671587.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 622622Kinesin light chain 2PRO_0000215095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei445 – 4451Phosphoserine3 Publications
    Modified residuei581 – 5811Phosphoserine1 Publication
    Modified residuei582 – 5821Phosphoserine3 Publications
    Modified residuei589 – 5891Phosphoserine2 Publications
    Modified residuei610 – 6101Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0B6.
    PaxDbiQ9H0B6.
    PRIDEiQ9H0B6.

    PTM databases

    PhosphoSiteiQ9H0B6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H0B6.
    BgeeiQ9H0B6.
    CleanExiHS_KLC2.
    GenevestigatoriQ9H0B6.

    Organism-specific databases

    HPAiHPA040416.
    HPA040434.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi122313. 28 interactions.
    IntActiQ9H0B6. 11 interactions.
    MINTiMINT-1401363.
    STRINGi9606.ENSP00000314837.

    Structurei

    Secondary structure

    1
    622
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi217 – 23216
    Beta strandi234 – 2363
    Helixi237 – 25216
    Helixi256 – 27318
    Helixi279 – 29315
    Turni294 – 2963
    Helixi298 – 31619
    Helixi321 – 33515
    Turni336 – 3383
    Helixi340 – 35718
    Helixi363 – 37917
    Helixi382 – 40019
    Beta strandi401 – 4033
    Helixi411 – 42010
    Helixi446 – 46116
    Helixi465 – 47612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CEQX-ray2.75A/B217-480[»]
    3EDTX-ray2.70B/D/F/H217-480[»]
    ProteinModelPortaliQ9H0B6.
    SMRiQ9H0B6. Positions 179-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0B6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati198 – 23134TPR 1Add
    BLAST
    Repeati240 – 27334TPR 2Add
    BLAST
    Repeati282 – 31534TPR 3Add
    BLAST
    Repeati324 – 35734TPR 4Add
    BLAST
    Repeati366 – 39934TPR 5Add
    BLAST
    Repeati449 – 48234TPR 6Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili78 – 14366Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the kinesin light chain family.Curated
    Contains 6 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000261663.
    HOVERGENiHBG006217.
    InParanoidiQ9H0B6.
    KOiK10407.
    OMAiNNDNKPI.
    OrthoDBiEOG7TXKGD.
    PhylomeDBiQ9H0B6.
    TreeFamiTF314010.

    Family and domain databases

    Gene3Di1.25.40.10. 2 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. 2 hits.
    PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0B6-1) [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

    MAMMVFPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLVAPEAGEA    50
    EPGSQERCIL LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR 100
    RLVQENQWLR EELAGTQQKL QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA 150
    SPNEEKGDVP KDTLDDLFPN EDEQSPAPSP GGGDVSGQHG GYEIPARLRT 200
    LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA TMLNILALVY 250
    RDQNKYKEAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE 300
    AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA 350
    LEIYATRLGP DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE 400
    FGSVNGDNKP IWMHAEEREE SKDKRRDSAP YGEYGSWYKA CKVDSPTVNT 450
    TLRSLGALYR RQGKLEAAHT LEDCASRNRK QGLDPASQTK VVELLKDGSG 500
    RRGDRRSSRD MAGGAGPRSE SDLEDVGPTA EWNGDGSGSL RRSGSFGKLR 550
    DALRRSSEML VKKLQGGTPQ EPPNPRMKRA SSLNFLNKSV EEPTQPGGTG 600
    LSDSRTLSSS SMDLSRRSSL VG 622
    Length:622
    Mass (Da):68,935
    Last modified:March 1, 2001 - v1
    Checksum:i5B57ABE4DF6E396E
    GO
    Isoform 2 (identifier: Q9H0B6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         77-153: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:545
    Mass (Da):60,047
    Checksum:iB30B27FA163B5D47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61F → Y in BAB14302. (PubMed:14702039)Curated
    Sequence conflicti306 – 3061K → R in BAB14039. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti517 – 5171P → S.
    Corresponds to variant rs2276036 [ dbSNP | Ensembl ].
    VAR_020379

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei77 – 15377Missing in isoform 2. 1 PublicationVSP_043486Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136864 mRNA. Translation: CAB66798.1.
    AK022449 mRNA. Translation: BAB14039.1.
    AK022907 mRNA. Translation: BAB14302.1.
    AK094593 mRNA. Translation: BAG52895.1.
    AK315725 mRNA. Translation: BAG38081.1.
    AP000759 Genomic DNA. No translation available.
    AP001107 Genomic DNA. No translation available.
    BC034373 mRNA. Translation: AAH34373.1.
    CCDSiCCDS44653.1. [Q9H0B6-2]
    CCDS8130.1. [Q9H0B6-1]
    RefSeqiNP_001128246.1. NM_001134774.1. [Q9H0B6-2]
    NP_001128247.1. NM_001134775.1. [Q9H0B6-1]
    NP_001128248.1. NM_001134776.1. [Q9H0B6-1]
    NP_073733.1. NM_022822.2. [Q9H0B6-1]
    XP_005274239.1. XM_005274182.1. [Q9H0B6-1]
    XP_005274240.1. XM_005274183.1. [Q9H0B6-1]
    UniGeneiHs.280792.

    Genome annotation databases

    EnsembliENST00000316924; ENSP00000314837; ENSG00000174996. [Q9H0B6-1]
    ENST00000394066; ENSP00000377630; ENSG00000174996. [Q9H0B6-2]
    ENST00000394067; ENSP00000377631; ENSG00000174996. [Q9H0B6-1]
    ENST00000417856; ENSP00000399403; ENSG00000174996. [Q9H0B6-1]
    ENST00000421552; ENSP00000408484; ENSG00000174996. [Q9H0B6-2]
    GeneIDi64837.
    KEGGihsa:64837.
    UCSCiuc001ohb.2. human. [Q9H0B6-1]
    uc001ohd.2. human. [Q9H0B6-2]

    Polymorphism databases

    DMDMi13878553.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136864 mRNA. Translation: CAB66798.1 .
    AK022449 mRNA. Translation: BAB14039.1 .
    AK022907 mRNA. Translation: BAB14302.1 .
    AK094593 mRNA. Translation: BAG52895.1 .
    AK315725 mRNA. Translation: BAG38081.1 .
    AP000759 Genomic DNA. No translation available.
    AP001107 Genomic DNA. No translation available.
    BC034373 mRNA. Translation: AAH34373.1 .
    CCDSi CCDS44653.1. [Q9H0B6-2 ]
    CCDS8130.1. [Q9H0B6-1 ]
    RefSeqi NP_001128246.1. NM_001134774.1. [Q9H0B6-2 ]
    NP_001128247.1. NM_001134775.1. [Q9H0B6-1 ]
    NP_001128248.1. NM_001134776.1. [Q9H0B6-1 ]
    NP_073733.1. NM_022822.2. [Q9H0B6-1 ]
    XP_005274239.1. XM_005274182.1. [Q9H0B6-1 ]
    XP_005274240.1. XM_005274183.1. [Q9H0B6-1 ]
    UniGenei Hs.280792.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CEQ X-ray 2.75 A/B 217-480 [» ]
    3EDT X-ray 2.70 B/D/F/H 217-480 [» ]
    ProteinModelPortali Q9H0B6.
    SMRi Q9H0B6. Positions 179-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122313. 28 interactions.
    IntActi Q9H0B6. 11 interactions.
    MINTi MINT-1401363.
    STRINGi 9606.ENSP00000314837.

    PTM databases

    PhosphoSitei Q9H0B6.

    Polymorphism databases

    DMDMi 13878553.

    Proteomic databases

    MaxQBi Q9H0B6.
    PaxDbi Q9H0B6.
    PRIDEi Q9H0B6.

    Protocols and materials databases

    DNASUi 64837.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316924 ; ENSP00000314837 ; ENSG00000174996 . [Q9H0B6-1 ]
    ENST00000394066 ; ENSP00000377630 ; ENSG00000174996 . [Q9H0B6-2 ]
    ENST00000394067 ; ENSP00000377631 ; ENSG00000174996 . [Q9H0B6-1 ]
    ENST00000417856 ; ENSP00000399403 ; ENSG00000174996 . [Q9H0B6-1 ]
    ENST00000421552 ; ENSP00000408484 ; ENSG00000174996 . [Q9H0B6-2 ]
    GeneIDi 64837.
    KEGGi hsa:64837.
    UCSCi uc001ohb.2. human. [Q9H0B6-1 ]
    uc001ohd.2. human. [Q9H0B6-2 ]

    Organism-specific databases

    CTDi 64837.
    GeneCardsi GC11P066026.
    HGNCi HGNC:20716. KLC2.
    HPAi HPA040416.
    HPA040434.
    MIMi 611729. gene.
    neXtProti NX_Q9H0B6.
    PharmGKBi PA142671587.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000261663.
    HOVERGENi HBG006217.
    InParanoidi Q9H0B6.
    KOi K10407.
    OMAi NNDNKPI.
    OrthoDBi EOG7TXKGD.
    PhylomeDBi Q9H0B6.
    TreeFami TF314010.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei Q9H0B6.
    GeneWikii KLC2.
    GenomeRNAii 64837.
    NextBioi 66920.
    PROi Q9H0B6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0B6.
    Bgeei Q9H0B6.
    CleanExi HS_KLC2.
    Genevestigatori Q9H0B6.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 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. 2 hits.
    PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "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 AND 2).
      Tissue: Mammary gland and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Lymph.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "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-151; SER-445; SER-581; SER-582 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-582 AND SER-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKLC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0B6
    Secondary accession number(s): A8MXL7
    , B2RDY4, Q9H9C8, Q9HA20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3