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A2AAY5

- SPD2B_MOUSE

UniProt

A2AAY5 - SPD2B_MOUSE

Protein

SH3 and PX domain-containing protein 2B

Gene

Sh3pxd2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation.3 Publications

    GO - Molecular functioni

    1. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
    2. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    3. phosphatidylinositol-4-phosphate binding Source: UniProtKB
    4. phosphatidylinositol-5-phosphate binding Source: UniProtKB
    5. SH2 domain binding Source: UniProtKB

    GO - Biological processi

    1. adipose tissue development Source: UniProtKB
    2. bone development Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. extracellular matrix disassembly Source: Ensembl
    5. eye development Source: UniProtKB
    6. heart development Source: UniProtKB
    7. podosome assembly Source: UniProtKB
    8. positive regulation of fat cell differentiation Source: UniProtKB
    9. protein localization to membrane Source: UniProtKB
    10. skeletal system development Source: UniProtKB
    11. superoxide metabolic process Source: UniProtKB

    Keywords - Biological processi

    Differentiation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH3 and PX domain-containing protein 2B
    Alternative name(s):
    Factor for adipocyte differentiation 49
    Tyrosine kinase substrate with four SH3 domains
    Gene namesi
    Name:Sh3pxd2b
    Synonyms:Fad49, Tks4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:2442062. Sh3pxd2b.

    Subcellular locationi

    Cytoplasm. Cell projectionpodosome
    Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. cytoplasm Source: UniProtKB
    4. podosome Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Exhibit skeletal, cardiac and eye phenotypes. Mice have glaucoma and suffer growth retardation as well as craniofacial defects. Skeletons show marked kyphosis, poorly aligned teeth, anomalies in the iliac crest, and a prominent xiphisternum. Mice show loss of adipose tissue as well as cardiac deficiencies, such as dysmorphic ventricular chambers, thin mitral valves and immature and disarrayed trabeculae with frequent apical indentation. Mice show loss of ROS formation.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-373 and F-508. 1 Publication
    Mutagenesisi373 – 3731Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-508. 1 Publication
    Mutagenesisi508 – 5081Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-373. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 908908SH3 and PX domain-containing protein 2BPRO_0000312202Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Phosphotyrosine1 Publication
    Modified residuei279 – 2791PhosphoserineBy similarity
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei661 – 6611Phosphotyrosine2 Publications
    Modified residuei840 – 8401Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated in SRC-transformed cells.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiA2AAY5.
    PRIDEiA2AAY5.

    PTM databases

    PhosphoSiteiA2AAY5.

    Expressioni

    Tissue specificityi

    Highly expressed in the stromal-vascular fraction of white adipose tissue with moderate expression in heart, skeletal muscle and the mature adipocyte fraction of white adipose tissue. Also expressed in brain, spleen, kidney and liver. Expressed in white and brown adipose tissues, eye, lung, heart, brain, spleen, stomach, liver and skeletal muscle (at protein level). Not expressed in kidney or bone marrow.3 Publications

    Developmental stagei

    Expression increases quickly after induction of adipocyte differentiation, reaches a maximum after 3 hours and decreases by 12 hours. Expressed from embryonic day E10.5 in heart and hindbrain, followed by an increased expression at E12.5 that also involves a subset of cells on the luminal side of the left ventricular wall in the case of the heart and neuroepithelium in the case of the brain. At E14.5, expression is present in developing bones (proximal ribs, lower jaw and clavicle), but the expression in the heart is no longer detectable. At stages E16.5 and E18.5, strong expression is seen in the long bones of the limbs, particularly in the growth plates, as well as in the facial and cranial bones and the primordial incisor. Expression in the ribs is seen in the proximal regions in those areas where the transition from cartilage to bone is expected to occur. Expression in the eye at E16.5 is highly specific for the ganglion cell layer.2 Publications

    Gene expression databases

    ArrayExpressiA2AAY5.
    BgeeiA2AAY5.
    CleanExiMM_SH3PXD2B.
    GenevestigatoriA2AAY5.

    Interactioni

    Subunit structurei

    Interacts with NOXO1 By similarity. Interacts (via SH3 domains) with NOXA1; the interaction is direct By similarity. Interacts with ADAM15. Interacts with FASLG By similarity.By similarity

    Protein-protein interaction databases

    IntActiA2AAY5. 1 interaction.
    MINTiMINT-4110712.

    Structurei

    3D structure databases

    ProteinModelPortaliA2AAY5.
    SMRiA2AAY5. Positions 7-132, 153-278, 370-432, 844-907.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 129125PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 21160SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini221 – 28060SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini368 – 42760SH3 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini846 – 90863SH3 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi718 – 77760Pro-richAdd
    BLAST

    Domaini

    The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SH3PXD2 family.Curated
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
    Contains 4 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG148927.
    GeneTreeiENSGT00530000063010.
    HOGENOMiHOG000154376.
    HOVERGENiHBG107128.
    InParanoidiA2AAY5.
    OMAiGHKVLAK.
    OrthoDBiEOG7H4DSQ.
    PhylomeDBiA2AAY5.
    TreeFamiTF329347.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00787. PX. 1 hit.
    PF00018. SH3_1. 3 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    SM00326. SH3. 4 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 4 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50002. SH3. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A2AAY5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD    50
    LQMQMLDKFP MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE 100
    YCKALIQLPP YISQCDEVLQ FFETRPEDLN PPKEEHIGKK KSGNDPTSVD 150
    PMVLEQYVVV ADYQKQESSE ISLSVGQVVD IIEKNESGWW FVSTAEEQGW 200
    VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM NLERGAVVEV 250
    VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL 300
    DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR 350
    DMTIPRGLNL PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK 400
    SLSGWWYIQM EDKEGWAPAT FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG 450
    DAAATENNTG PEAVGPSRPL PEAPHGAVDS GMLWSKDWKG GKEAPRKASS 500
    DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE RQKMEPLRGS 550
    SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL 600
    AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE 650
    PAQSEDHVDI YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG 700
    EGPGHGQDRS GRQDGLSPKE TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ 750
    QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR GAQREESRVA PAAGRALLVP 800
    PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS FLNADGPKDS 850
    LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP 900
    SNYLRKKP 908
    Length:908
    Mass (Da):101,517
    Last modified:February 20, 2007 - v1
    Checksum:i83341ABA6DF639AB
    GO

    Sequence cautioni

    The sequence BAC40843.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti464 – 4641V → M in BAG81976. (PubMed:18959745)Curated
    Sequence conflicti464 – 4641V → M in AAI15765. (PubMed:15489334)Curated
    Sequence conflicti744 – 7441V → VSV in BAG81976. (PubMed:18959745)Curated
    Sequence conflicti744 – 7441V → VSV in BAE42425. (PubMed:16141072)Curated
    Sequence conflicti749 – 7491L → Q in BAG81976. (PubMed:18959745)Curated
    Sequence conflicti749 – 7491L → Q in BAE42425. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB430861 mRNA. Translation: BAG81976.1.
    AK089330 mRNA. Translation: BAC40843.1. Frameshift.
    AK171384 mRNA. Translation: BAE42425.1.
    AL662780 Genomic DNA. Translation: CAM22517.1.
    BC115711 mRNA. Translation: AAI15712.1.
    BC115764 mRNA. Translation: AAI15765.1.
    CCDSiCCDS24526.1.
    RefSeqiNP_796338.2. NM_177364.3.
    UniGeneiMm.227616.

    Genome annotation databases

    EnsembliENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
    GeneIDi268396.
    KEGGimmu:268396.
    UCSCiuc007ijq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB430861 mRNA. Translation: BAG81976.1 .
    AK089330 mRNA. Translation: BAC40843.1 . Frameshift.
    AK171384 mRNA. Translation: BAE42425.1 .
    AL662780 Genomic DNA. Translation: CAM22517.1 .
    BC115711 mRNA. Translation: AAI15712.1 .
    BC115764 mRNA. Translation: AAI15765.1 .
    CCDSi CCDS24526.1.
    RefSeqi NP_796338.2. NM_177364.3.
    UniGenei Mm.227616.

    3D structure databases

    ProteinModelPortali A2AAY5.
    SMRi A2AAY5. Positions 7-132, 153-278, 370-432, 844-907.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A2AAY5. 1 interaction.
    MINTi MINT-4110712.

    PTM databases

    PhosphoSitei A2AAY5.

    Proteomic databases

    PaxDbi A2AAY5.
    PRIDEi A2AAY5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038753 ; ENSMUSP00000044276 ; ENSMUSG00000040711 .
    GeneIDi 268396.
    KEGGi mmu:268396.
    UCSCi uc007ijq.1. mouse.

    Organism-specific databases

    CTDi 285590.
    MGIi MGI:2442062. Sh3pxd2b.

    Phylogenomic databases

    eggNOGi NOG148927.
    GeneTreei ENSGT00530000063010.
    HOGENOMi HOG000154376.
    HOVERGENi HBG107128.
    InParanoidi A2AAY5.
    OMAi GHKVLAK.
    OrthoDBi EOG7H4DSQ.
    PhylomeDBi A2AAY5.
    TreeFami TF329347.

    Miscellaneous databases

    NextBioi 392275.
    PROi A2AAY5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A2AAY5.
    Bgeei A2AAY5.
    CleanExi MM_SH3PXD2B.
    Genevestigatori A2AAY5.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00787. PX. 1 hit.
    PF00018. SH3_1. 3 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    SM00326. SH3. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 4 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50002. SH3. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene, fad49, plays a crucial role in the immediate early stage of adipocyte differentiation via involvement in mitotic clonal expansion."
      Hishida T., Eguchi T., Osada S., Nishizuka M., Imagawa M.
      FEBS J. 275:5576-5588(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN.
    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].
      Strain: C57BL/6J.
      Tissue: Dendritic cell.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 1-647.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The podosomal-adaptor protein SH3PXD2B is essential for normal postnatal development."
      Mao M., Thedens D.R., Chang B., Harris B.S., Zheng Q.Y., Johnson K.R., Donahue L.R., Anderson M.G.
      Mamm. Genome 20:462-475(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ADAM15.
    8. "The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation."
      Buschman M.D., Bromann P.A., Cejudo-Martin P., Wen F., Pass I., Courtneidge S.A.
      Mol. Biol. Cell 20:1302-1311(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF TYR-25; TYR-373 AND TYR-508, SUBCELLULAR LOCATION.
    9. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
      Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
      Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    10. Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiSPD2B_MOUSE
    AccessioniPrimary (citable) accession number: A2AAY5
    Secondary accession number(s): B6F0V1
    , Q1LZL8, Q1LZM5, Q3TB89, Q8BIC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 68 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

    External Data

    Dasty 3