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P61979

- HNRPK_MOUSE

UniProt

P61979 - HNRPK_MOUSE

Protein

Heterogeneous nuclear ribonucleoprotein K

Gene

Hnrnpk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction By similarity. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest.By similarity1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. RNA binding Source: MGI

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. RNA splicing Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor, Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoprotein K
    Short name:
    hnRNP K
    Gene namesi
    Name:Hnrnpk
    Synonyms:Hnrpk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:99894. Hnrnpk.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleoplasm By similarity. Cell projectionpodosome By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. cytoplasm Source: UniProtKB-SubCell
    4. nucleoplasm Source: UniProtKB-SubCell
    5. podosome Source: UniProtKB-SubCell
    6. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Heterogeneous nuclear ribonucleoprotein KPRO_0000050097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei116 – 1161PhosphoserineBy similarity
    Modified residuei198 – 1981N6-acetyllysine1 Publication
    Modified residuei214 – 2141PhosphoserineBy similarity
    Modified residuei216 – 2161PhosphoserineBy similarity
    Modified residuei284 – 2841PhosphoserineBy similarity
    Modified residuei296 – 2961Omega-N-methylated arginineBy similarity
    Modified residuei299 – 2991Omega-N-methylated arginineBy similarity
    Modified residuei379 – 3791PhosphoserineBy similarity
    Modified residuei380 – 3801PhosphotyrosineBy similarity
    Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions By similarity.By similarity
    Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination By similarity.By similarity
    O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP61979.
    PaxDbiP61979.
    PRIDEiP61979.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00223253.
    P61979.

    PTM databases

    PhosphoSiteiP61979.

    Expressioni

    Inductioni

    By DNA damage. This up-regulation is due to protein stabilization. The constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway.1 Publication

    Gene expression databases

    ArrayExpressiP61979.
    BgeeiP61979.
    GenevestigatoriP61979.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex By similarity. Interacts with ANKRD28 and RBM42. Interacts with DDX1 By similarity. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation By similarity. Interacts with p53/TP53 By similarity. Interacts with ZIK1. Interacts with BRDT.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi200359. 5 interactions.
    IntActiP61979. 12 interactions.
    MINTiMINT-1510077.

    Structurei

    3D structure databases

    ProteinModelPortaliP61979.
    SMRiP61979. Positions 45-216, 385-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 10463KH 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati54 – 76231-1Add
    BLAST
    Repeati59 – 6243-1
    Domaini144 – 20966KH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati245 – 25062-1
    Repeati257 – 26043-2
    Repeati267 – 27043-3
    Repeati295 – 29843-4
    Repeati324 – 32962-2
    Domaini387 – 45165KH 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati399 – 421231-2Add
    BLAST
    Repeati404 – 40743-5

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 276276Necessary for interaction with DDX1By similarityAdd
    BLAST
    Regioni54 – 4213682 X 22 AA approximate repeatsAdd
    BLAST
    Regioni59 – 4073495 X 4 AA repeats of G-X-G-GAdd
    BLAST
    Regioni209 – 337129Interaction with ZIK1Add
    BLAST
    Regioni236 – 27338RNA-binding RGG-boxAdd
    BLAST
    Regioni245 – 329852 X 6 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi289 – 2946Poly-Pro
    Compositional biasi310 – 3156Poly-Pro

    Sequence similaritiesi

    Contains 3 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG285495.
    GeneTreeiENSGT00730000110620.
    HOVERGENiHBG051916.
    KOiK12886.
    OMAiKALRTDX.
    OrthoDBiEOG7CZK81.
    TreeFamiTF316335.

    Family and domain databases

    Gene3Di3.30.1370.10. 3 hits.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012987. ROK_N.
    [Graphical view]
    PfamiPF00013. KH_1. 3 hits.
    PF08067. ROKNT. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 3 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 3 hits.
    PROSITEiPS50084. KH_TYPE_1. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61979-1) [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

    METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ    50
    SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI 100
    LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL 150
    IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD RVVLIGGKPD 200
    RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT MMFDDRRGRP 250
    VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 300
    GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID 350
    TWSPSEWQMA YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG 400
    SIIGKGGQRI KQIRHESGAS IKIDEPLEGS EDRIITITGT QDQIQNAQYL 450
    LQNSVKQYSG KFF 463
    Length:463
    Mass (Da):50,976
    Last modified:June 7, 2004 - v1
    Checksum:i0F70EE169B2A064A
    GO
    Isoform 2 (identifier: P61979-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         459-463: SGKFF → ADVEGF

    Show »
    Length:464
    Mass (Da):51,028
    Checksum:i0B4EC22FE4534A06
    GO
    Isoform 3 (identifier: P61979-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-134: Missing.

    Show »
    Length:439
    Mass (Da):48,510
    Checksum:i7BCA66B4E39776DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321C → V in AAA21731. (PubMed:8021272)Curated
    Sequence conflicti136 – 1361Q → P in AAA21731. (PubMed:8021272)Curated
    Sequence conflicti154 – 1541S → T in AAA21731. (PubMed:8021272)Curated
    Sequence conflicti334 – 3341D → S in AAA21731. (PubMed:8021272)Curated
    Sequence conflicti350 – 3501D → E in AAA21731. (PubMed:8021272)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 13424Missing in isoform 3. 1 PublicationVSP_012581Add
    BLAST
    Alternative sequencei459 – 4635SGKFF → ADVEGF in isoform 2. 3 PublicationsVSP_010622

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31961 mRNA. Translation: AAA21731.1.
    AK011428 mRNA. Translation: BAB27614.1.
    AK051313 mRNA. Translation: BAC34601.1.
    AK078777 mRNA. Translation: BAC37389.1.
    AK088462 mRNA. Translation: BAC40368.1.
    BC006694 mRNA. Translation: AAH06694.1.
    CCDSiCCDS49283.1.
    RefSeqiNP_079555.1. NM_025279.2. [P61979-1]
    XP_006517164.1. XM_006517101.1. [P61979-2]
    XP_006517165.1. XM_006517102.1. [P61979-2]
    XP_006517166.1. XM_006517103.1. [P61979-2]
    XP_006517167.1. XM_006517104.1. [P61979-2]
    XP_006517170.1. XM_006517107.1. [P61979-3]
    UniGeneiMm.142872.

    Genome annotation databases

    EnsembliENSMUST00000043269; ENSMUSP00000039269; ENSMUSG00000021546. [P61979-1]
    ENSMUST00000116403; ENSMUSP00000112104; ENSMUSG00000021546. [P61979-2]
    ENSMUST00000176207; ENSMUSP00000135354; ENSMUSG00000021546. [P61979-3]
    GeneIDi15387.
    KEGGimmu:15387.
    UCSCiuc007qtw.1. mouse.
    uc007qty.1. mouse. [P61979-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31961 mRNA. Translation: AAA21731.1 .
    AK011428 mRNA. Translation: BAB27614.1 .
    AK051313 mRNA. Translation: BAC34601.1 .
    AK078777 mRNA. Translation: BAC37389.1 .
    AK088462 mRNA. Translation: BAC40368.1 .
    BC006694 mRNA. Translation: AAH06694.1 .
    CCDSi CCDS49283.1.
    RefSeqi NP_079555.1. NM_025279.2. [P61979-1 ]
    XP_006517164.1. XM_006517101.1. [P61979-2 ]
    XP_006517165.1. XM_006517102.1. [P61979-2 ]
    XP_006517166.1. XM_006517103.1. [P61979-2 ]
    XP_006517167.1. XM_006517104.1. [P61979-2 ]
    XP_006517170.1. XM_006517107.1. [P61979-3 ]
    UniGenei Mm.142872.

    3D structure databases

    ProteinModelPortali P61979.
    SMRi P61979. Positions 45-216, 385-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200359. 5 interactions.
    IntActi P61979. 12 interactions.
    MINTi MINT-1510077.

    PTM databases

    PhosphoSitei P61979.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00223253.
    P61979.

    Proteomic databases

    MaxQBi P61979.
    PaxDbi P61979.
    PRIDEi P61979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043269 ; ENSMUSP00000039269 ; ENSMUSG00000021546 . [P61979-1 ]
    ENSMUST00000116403 ; ENSMUSP00000112104 ; ENSMUSG00000021546 . [P61979-2 ]
    ENSMUST00000176207 ; ENSMUSP00000135354 ; ENSMUSG00000021546 . [P61979-3 ]
    GeneIDi 15387.
    KEGGi mmu:15387.
    UCSCi uc007qtw.1. mouse.
    uc007qty.1. mouse. [P61979-3 ]

    Organism-specific databases

    CTDi 3190.
    MGIi MGI:99894. Hnrnpk.

    Phylogenomic databases

    eggNOGi NOG285495.
    GeneTreei ENSGT00730000110620.
    HOVERGENi HBG051916.
    KOi K12886.
    OMAi KALRTDX.
    OrthoDBi EOG7CZK81.
    TreeFami TF316335.

    Miscellaneous databases

    NextBioi 12686.
    PROi P61979.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61979.
    Bgeei P61979.
    Genevestigatori P61979.

    Family and domain databases

    Gene3Di 3.30.1370.10. 3 hits.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012987. ROK_N.
    [Graphical view ]
    Pfami PF00013. KH_1. 3 hits.
    PF08067. ROKNT. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 3 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 3 hits.
    PROSITEi PS50084. KH_TYPE_1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cloning, and expression of a murine phosphoprotein that binds the kappa B motif in vitro identifies it as the homolog of the human heterogeneous nuclear ribonucleoprotein K protein. Description of a novel DNA-dependent phosphorylation process."
      Ostrowski J., van Seuningen I., Seger R., Rauch C.T., Sleath P.R., McMullen B.A., Bomsztyk K.
      J. Biol. Chem. 269:17626-17634(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
      Tissue: Lymphoma.
    2. "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] (ISOFORMS 1; 2 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Spinal ganglion, Testis and Thymus.
    3. "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 2).
    4. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 149-163 AND 207-219, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    5. "Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein."
      Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I., Bomsztyk K.
      J. Biol. Chem. 271:27701-27706(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZIK1.
    6. "hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage."
      Moumen A., Masterson P., O'Connor M.J., Jackson S.P.
      Cell 123:1065-1078(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
      Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
      Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
      Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
      Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRDT.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHNRPK_MOUSE
    AccessioniPrimary (citable) accession number: P61979
    Secondary accession number(s): Q07244
    , Q15671, Q60577, Q8BGQ8, Q922Y7, Q96J62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 118 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, Direct protein sequencing, 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

    External Data

    Dasty 3