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Q8CJ53

- CIP4_MOUSE

UniProt

Q8CJ53 - CIP4_MOUSE

Protein

Cdc42-interacting protein 4

Gene

Trip10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL By similarity. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei166 – 1661Mediates end-to-end attachment of dimersBy similarity

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. endocytosis Source: UniProtKB-KW

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_210090. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cdc42-interacting protein 4
    Alternative name(s):
    Thyroid receptor-interacting protein 10
    Short name:
    TR-interacting protein 10
    Short name:
    TRIP-10
    Gene namesi
    Name:Trip10
    Synonyms:Cip4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2146901. Trip10.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcell cortex. Lysosome. Golgi apparatus By similarity. Cell membrane. Cell projectionphagocytic cup By similarity
    Note: Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9 By similarity. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell projection Source: UniProtKB-KW
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. lysosome Source: UniProtKB-SubCell
    5. microtubule Source: MGI
    6. phagocytic cup Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi454 – 4541I → S: Impairs interaction with CDC42 and RHOQ and reduces insulin-stimulated translocation to the plasma membrane. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603Cdc42-interacting protein 4PRO_0000261439Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei296 – 2961PhosphoserineBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei335 – 3351PhosphoserineBy similarity
    Modified residuei351 – 3511PhosphoserineBy similarity
    Modified residuei482 – 4821PhosphoserineBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated. Also phosphorylated by PKA By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8CJ53.
    PaxDbiQ8CJ53.
    PRIDEiQ8CJ53.

    PTM databases

    PhosphoSiteiQ8CJ53.

    Expressioni

    Gene expression databases

    BgeeiQ8CJ53.
    CleanExiMM_TRIP10.
    GenevestigatoriQ8CJ53.

    Interactioni

    Subunit structurei

    Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures By similarity. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and WAS/WASP. Interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. May interact with CTNNB1 and HD/HTT By similarity. Interacts specifically with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi223098. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CJ53.
    SMRiQ8CJ53. Positions 10-288, 384-481, 546-601.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati405 – 48177REMAdd
    BLAST
    Domaini542 – 60362SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 288288F-BAR domainBy similarityAdd
    BLAST
    Regioni1 – 117117Required for podosome formation and interaction with AKAP9 and microtubulesBy similarityAdd
    BLAST
    Regioni1 – 117117Required for translocation to the plasma membrane in response to insulinAdd
    BLAST
    Regioni293 – 603311Interaction with PDE6GBy similarityAdd
    BLAST
    Regioni293 – 539247Interaction with CDC42By similarityAdd
    BLAST
    Regioni471 – 603133Required for interaction with FASLG and localization to lysosomesBy similarityAdd
    BLAST
    Regioni487 – 54357Interaction with DNM2 and WASLAdd
    BLAST
    Regioni532 – 60372Interaction with DNM1 and WASLBy similarityAdd
    BLAST
    Regioni540 – 60364Required for podosome formationBy similarityAdd
    BLAST
    Regioni546 – 60358Interaction with WASBy similarityAdd
    BLAST
    Regioni548 – 60356Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 259193By similarityAdd
    BLAST
    Coiled coili388 – 48194By similarityAdd
    BLAST

    Domaini

    The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation By similarity.By similarity

    Sequence similaritiesi

    Belongs to the FNBP1 family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG323796.
    GeneTreeiENSGT00510000046403.
    HOGENOMiHOG000231767.
    HOVERGENiHBG002489.
    InParanoidiQ8CJ53.
    KOiK07196.
    OMAiSPKFGRD.
    OrthoDBiEOG780RQK.
    PhylomeDBiQ8CJ53.
    TreeFamiTF351162.

    Family and domain databases

    InterProiIPR028498. CIP4.
    IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR12602:SF7. PTHR12602:SF7. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 2 hits.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CJ53-1) [UniParc]FASTAAdd to Basket

    Also known as: Cip4/2

    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

    MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERAEVEQ AYAKQLRSLV    50
    KKYLPKRPTK DDPEVKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL 100
    ELAKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK 150
    AAHTAERLDQ DINATKADVE KAKQQAHLRN HMAEESKNEY AAQLQRFNRD 200
    QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ VVPIIGKCLE 250
    GMKVAAESVD AKNDSQVLIE LHKSGFARPG DLEFEDFSQV INRVPSDSSL 300
    GTPDGRPELR AASSRSRAKR WPFGKKNKPR PPSLSLLGGH LPSTLSDGPS 350
    SPRSGRDPLA ILSEISKSVK PRLASFRSFR GGRGTVATED FSHLPPEQQR 400
    KRLQQQLEER NRELQKEEDQ REALKKMKDV YEKTPQMGDP ASLEPRIAET 450
    LGNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPTTAPPDS 500
    SSSSTNSGSQ DNKESSSEEP PSEGQDTPIY TEFDEDFEEP ASPIGQCVAI 550
    YHFEGSSEGT VSMSEGEDLS LMEEDKGDGW TRVRRKQGAE GYVPTSYLRV 600
    TLN 603
    Length:603
    Mass (Da):68,489
    Last modified:November 28, 2006 - v2
    Checksum:iDDA6271D5FD515AC
    GO
    Isoform 2 (identifier: Q8CJ53-2) [UniParc]FASTAAdd to Basket

    Also known as: H

    The sequence of this isoform differs from the canonical sequence as follows:
         515-515: Missing.

    Show »
    Length:602
    Mass (Da):68,402
    Checksum:i165D63A9EC6CD884
    GO
    Isoform 3 (identifier: Q8CJ53-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-384: Missing.

    Show »
    Length:547
    Mass (Da):62,654
    Checksum:i5DE65DB3D6C9B8E2
    GO
    Isoform 4 (identifier: Q8CJ53-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-384: Missing.
         515-515: Missing.

    Show »
    Length:546
    Mass (Da):62,567
    Checksum:i8627CD20F0C19667
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti321 – 3211W → C in AAN38709. (PubMed:12242347)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei329 – 38456Missing in isoform 3 and isoform 4. 2 PublicationsVSP_021722Add
    BLAST
    Alternative sequencei515 – 5151Missing in isoform 2 and isoform 4. 2 PublicationsVSP_021723

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY081142 mRNA. Translation: AAL89589.1.
    AF502565 mRNA. Translation: AAN38709.1.
    AK088909 mRNA. Translation: BAC40648.1.
    AK149902 mRNA. Translation: BAE29155.1.
    BC003249 mRNA. Translation: AAH03249.1.
    CCDSiCCDS28930.1. [Q8CJ53-3]
    RefSeqiNP_001229318.1. NM_001242389.1. [Q8CJ53-1]
    NP_001229319.1. NM_001242390.1. [Q8CJ53-2]
    NP_001229320.1. NM_001242391.1. [Q8CJ53-4]
    NP_598886.1. NM_134125.4. [Q8CJ53-3]
    UniGeneiMm.37368.

    Genome annotation databases

    EnsembliENSMUST00000019631; ENSMUSP00000019631; ENSMUSG00000019487. [Q8CJ53-3]
    GeneIDi106628.
    KEGGimmu:106628.
    UCSCiuc008dej.2. mouse. [Q8CJ53-3]
    uc008dek.2. mouse. [Q8CJ53-1]
    uc008del.2. mouse. [Q8CJ53-2]
    uc008dem.2. mouse. [Q8CJ53-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY081142 mRNA. Translation: AAL89589.1 .
    AF502565 mRNA. Translation: AAN38709.1 .
    AK088909 mRNA. Translation: BAC40648.1 .
    AK149902 mRNA. Translation: BAE29155.1 .
    BC003249 mRNA. Translation: AAH03249.1 .
    CCDSi CCDS28930.1. [Q8CJ53-3 ]
    RefSeqi NP_001229318.1. NM_001242389.1. [Q8CJ53-1 ]
    NP_001229319.1. NM_001242390.1. [Q8CJ53-2 ]
    NP_001229320.1. NM_001242391.1. [Q8CJ53-4 ]
    NP_598886.1. NM_134125.4. [Q8CJ53-3 ]
    UniGenei Mm.37368.

    3D structure databases

    ProteinModelPortali Q8CJ53.
    SMRi Q8CJ53. Positions 10-288, 384-481, 546-601.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223098. 1 interaction.

    PTM databases

    PhosphoSitei Q8CJ53.

    Proteomic databases

    MaxQBi Q8CJ53.
    PaxDbi Q8CJ53.
    PRIDEi Q8CJ53.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019631 ; ENSMUSP00000019631 ; ENSMUSG00000019487 . [Q8CJ53-3 ]
    GeneIDi 106628.
    KEGGi mmu:106628.
    UCSCi uc008dej.2. mouse. [Q8CJ53-3 ]
    uc008dek.2. mouse. [Q8CJ53-1 ]
    uc008del.2. mouse. [Q8CJ53-2 ]
    uc008dem.2. mouse. [Q8CJ53-4 ]

    Organism-specific databases

    CTDi 9322.
    MGIi MGI:2146901. Trip10.

    Phylogenomic databases

    eggNOGi NOG323796.
    GeneTreei ENSGT00510000046403.
    HOGENOMi HOG000231767.
    HOVERGENi HBG002489.
    InParanoidi Q8CJ53.
    KOi K07196.
    OMAi SPKFGRD.
    OrthoDBi EOG780RQK.
    PhylomeDBi Q8CJ53.
    TreeFami TF351162.

    Enzyme and pathway databases

    Reactomei REACT_210090. Rho GTPase cycle.

    Miscellaneous databases

    NextBioi 358316.
    PROi Q8CJ53.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CJ53.
    CleanExi MM_TRIP10.
    Genevestigatori Q8CJ53.

    Family and domain databases

    InterProi IPR028498. CIP4.
    IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR12602:SF7. PTHR12602:SF7. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
      Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
      Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Heart.
    2. "The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes."
      Chang L., Adams R.D., Saltiel A.R.
      Proc. Natl. Acad. Sci. U.S.A. 99:12835-12840(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42 AND RHOQ, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-454.
      Tissue: Adipocyte.
    3. "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] (ISOFORM 4).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow and Thymus.
    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 3).
      Strain: FVB/N.
      Tissue: Mammary gland.
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 98-104, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle."
      Archila S., King M.A., Carlson G.M., Rice N.A.
      Biochem. Biophys. Res. Commun. 345:1592-1599(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
      Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
      J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION.
    8. "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes."
      Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M., Pessin J.E., Saltiel A.R.
      Cell Metab. 5:59-72(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAPVD1.

    Entry informationi

    Entry nameiCIP4_MOUSE
    AccessioniPrimary (citable) accession number: Q8CJ53
    Secondary accession number(s): Q8BTR8, Q8R433, Q99LI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 85 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

    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