Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9WUB0

- HOIL1_MOUSE

UniProt

Q9WUB0 - HOIL1_MOUSE

Protein

RanBP-type and C3HC4-type zinc finger-containing protein 1

Gene

Rbck1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri188 – 22033RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri280 – 32546RING-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri360 – 40950IBR-typeAdd
    BLAST
    Zinc fingeri435 – 46127RING-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. ubiquitin binding Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of necroptotic process Source: MGI
    2. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    3. positive regulation of apoptotic process Source: UniProtKB
    4. positive regulation of extrinsic apoptotic signaling pathway Source: MGI
    5. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. positive regulation of NF-kappaB import into nucleus Source: UniProtKB
    7. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    9. protein linear polyubiquitination Source: UniProtKB
    10. T cell receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC:6.3.2.-)
    Alternative name(s):
    Heme-oxidized IRP2 ubiquitin ligase 1 homolog
    Short name:
    HOIL-1
    UbcM4-interacting protein 28
    Ubiquitin-conjugating enzyme 7-interacting protein 3
    Gene namesi
    Name:Rbck1
    Synonyms:Rbck, Ubce7ip3, Uip28
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1344372. Rbck1.

    Subcellular locationi

    GO - Cellular componenti

    1. LUBAC complex Source: UniProtKB

    Pathology & Biotechi

    Disruption phenotypei

    Impaired TNF-alpha-mediated NF-kappa-B activation and enhanced JNK-mediated apoptosis.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508RanBP-type and C3HC4-type zinc finger-containing protein 1PRO_0000056296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei328 – 3281Phosphotyrosine1 Publication

    Post-translational modificationi

    Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome By similarity.By similarity
    Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9WUB0.
    PRIDEiQ9WUB0.

    PTM databases

    PhosphoSiteiQ9WUB0.

    Expressioni

    Gene expression databases

    BgeeiQ9WUB0.
    GenevestigatoriQ9WUB0.

    Interactioni

    Subunit structurei

    Forms homodimers in vitro By similarity. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C (PRKCZ) and with UBE2L3. Isoform 1 and isoform 2 interact with IREB2 only in iron-rich conditions. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with EYA1, TAB2, TAB3, MAP3K7 TRAF6 and RIPK1. Interacts with IRF3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eya1P977672EBI-6141072,EBI-1368503

    Protein-protein interaction databases

    BioGridi204899. 8 interactions.
    DIPiDIP-59198N.
    IntActiQ9WUB0. 2 interactions.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi194 – 1963
    Turni198 – 2003
    Turni212 – 2143
    Helixi232 – 24514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B08X-ray1.70B/E/H/K192-250[»]
    3B0AX-ray1.90B/E192-250[»]
    ProteinModelPortaliQ9WUB0.
    SMRiQ9WUB0. Positions 51-139, 192-249, 276-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 11965Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 268268Interaction with TAB2By similarityAdd
    BLAST
    Regioni1 – 218218Interaction with IRF3By similarityAdd
    BLAST
    Regioni69 – 13163Interaction with RNF31By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili231 – 25929Sequence AnalysisAdd
    BLAST

    Domaini

    The RanBP2-type zinc finger, also called Npl4 zinc finger (NZF), mediates binding to 'Met-1'-linked polyubiquitins.
    The UBL domain mediates association with RNF31 via interaction with its UBA domain.By similarity

    Sequence similaritiesi

    Contains 1 IBR-type zinc finger.Curated
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri188 – 22033RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri280 – 32546RING-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri360 – 40950IBR-typeAdd
    BLAST
    Zinc fingeri435 – 46127RING-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG249934.
    GeneTreeiENSGT00530000063620.
    HOVERGENiHBG061515.
    InParanoidiQ9WUB0.
    KOiK10630.
    OMAiQDIRLWV.
    OrthoDBiEOG7PGDQN.
    PhylomeDBiQ9WUB0.
    TreeFamiTF323486.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF01485. IBR. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50053. UBIQUITIN_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WUB0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEKTKKAEE MALSLARAVA GGDEQAAIKY ATWLAEQRVP LRVQVKPEVS    50
    PTQDIRLCVS VEDAYMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPSLQQ 100
    WVVGQRLARD QETLHSHGIR RNGDGAYLYL LSARNTSLNP QELQRQRQLR 150
    MLEDLGFKDL TLQSRGPLEP VLPKPRTNQE PGQPDAAPES PPVGWQCPGC 200
    TFINKPTRPG CEMCCRARPE TYQIPASYQP DEEERARLAG EEEALRQYQQ 250
    RKQQQQEGNY LQHVQLEQRS LVLNTEPTEC PVCYSVLAPG EAVVLRECLH 300
    TFCRECLQGT IRNSQEAEVA CPFIDSTYSC PGKLLEREIR ALLSPEDYQR 350
    FLDLGVSIAE NRSTLSYHCK TPDCRGWCFF EDDVNEFTCP VCTRVNCLLC 400
    KAIHEHMNCR EYQDDLALRA QNDVAARQTT EMLKVMLQQG EAMHCPQCRI 450
    VVQKKDGCDW IRCTVCHTEI CWVTKGPRWG PGGPGDTSGG CRCRVNGIPC 500
    HPSCQNCH 508
    Length:508
    Mass (Da):57,534
    Last modified:January 15, 2008 - v2
    Checksum:iCBD3B40CD4E55180
    GO

    Sequence cautioni

    The sequence AAD24572.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH34555.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti322 – 3221P → S in BAE38556. (PubMed:16141072)Curated
    Sequence conflicti406 – 4061H → R in BAC40440. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK088591 mRNA. Translation: BAC40440.1.
    AK166075 mRNA. Translation: BAE38556.1.
    AL831735, AL928568 Genomic DNA. Translation: CAM24727.1.
    AL928568, AL831735 Genomic DNA. Translation: CAM23203.1.
    BC034555 mRNA. Translation: AAH34555.1. Different initiation.
    AF124663 mRNA. Translation: AAD24572.1. Different initiation.
    CCDSiCCDS38273.1.
    RefSeqiNP_001077390.1. NM_001083921.1.
    NP_062679.2. NM_019705.3.
    UniGeneiMm.182145.

    Genome annotation databases

    EnsembliENSMUST00000028964; ENSMUSP00000028964; ENSMUSG00000027466.
    ENSMUST00000109847; ENSMUSP00000105473; ENSMUSG00000027466.
    GeneIDi24105.
    KEGGimmu:24105.
    UCSCiuc008nfd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK088591 mRNA. Translation: BAC40440.1 .
    AK166075 mRNA. Translation: BAE38556.1 .
    AL831735 , AL928568 Genomic DNA. Translation: CAM24727.1 .
    AL928568 , AL831735 Genomic DNA. Translation: CAM23203.1 .
    BC034555 mRNA. Translation: AAH34555.1 . Different initiation.
    AF124663 mRNA. Translation: AAD24572.1 . Different initiation.
    CCDSi CCDS38273.1.
    RefSeqi NP_001077390.1. NM_001083921.1.
    NP_062679.2. NM_019705.3.
    UniGenei Mm.182145.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B08 X-ray 1.70 B/E/H/K 192-250 [» ]
    3B0A X-ray 1.90 B/E 192-250 [» ]
    ProteinModelPortali Q9WUB0.
    SMRi Q9WUB0. Positions 51-139, 192-249, 276-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204899. 8 interactions.
    DIPi DIP-59198N.
    IntActi Q9WUB0. 2 interactions.

    PTM databases

    PhosphoSitei Q9WUB0.

    Proteomic databases

    PaxDbi Q9WUB0.
    PRIDEi Q9WUB0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028964 ; ENSMUSP00000028964 ; ENSMUSG00000027466 .
    ENSMUST00000109847 ; ENSMUSP00000105473 ; ENSMUSG00000027466 .
    GeneIDi 24105.
    KEGGi mmu:24105.
    UCSCi uc008nfd.1. mouse.

    Organism-specific databases

    CTDi 10616.
    MGIi MGI:1344372. Rbck1.

    Phylogenomic databases

    eggNOGi NOG249934.
    GeneTreei ENSGT00530000063620.
    HOVERGENi HBG061515.
    InParanoidi Q9WUB0.
    KOi K10630.
    OMAi QDIRLWV.
    OrthoDBi EOG7PGDQN.
    PhylomeDBi Q9WUB0.
    TreeFami TF323486.

    Enzyme and pathway databases

    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RBCK1. mouse.
    NextBioi 304117.
    PROi Q9WUB0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WUB0.
    Genevestigatori Q9WUB0.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF01485. IBR. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: NOD.
      Tissue: Lung and Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Strain: FVB/N.
      Tissue: Salivary gland.
    4. "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4."
      Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.
      FEBS Lett. 454:257-261(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-508.
      Strain: BALB/c.
      Tissue: Liver.
    5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    6. Cited for: DISRUPTION PHENOTYPE.
    7. "Sipl1 and Rbck1 are novel Eya1-binding proteins with a role in craniofacial development."
      Landgraf K., Bollig F., Trowe M.O., Besenbeck B., Ebert C., Kruspe D., Kispert A., Hanel F., Englert C.
      Mol. Cell. Biol. 30:5764-5775(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EYA1.
    8. "Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex."
      Sato Y., Fujita H., Yoshikawa A., Yamashita M., Yamagata A., Kaiser S.E., Iwai K., Fukai S.
      Proc. Natl. Acad. Sci. U.S.A. 108:20520-20525(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 192-250 IN COMPLEX WITH LINEAR DIUBIQUITIN.

    Entry informationi

    Entry nameiHOIL1_MOUSE
    AccessioniPrimary (citable) accession number: Q9WUB0
    Secondary accession number(s): A2ANR4, Q3TM86, Q8C2I0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3