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Q8BGG7

- UBS3B_MOUSE

UniProt

Q8BGG7 - UBS3B_MOUSE

Protein

Ubiquitin-associated and SH3 domain-containing protein B

Gene

Ubash3b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.4 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei379 – 3791
    Active sitei380 – 3801Tele-phosphohistidine intermediate
    Active sitei565 – 5651

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. negative regulation of platelet aggregation Source: MGI
    2. negative regulation of protein kinase activity Source: MGI
    3. peptidyl-tyrosine dephosphorylation Source: MGI
    4. regulation of release of sequestered calcium ion into cytosol Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-associated and SH3 domain-containing protein B (EC:3.1.3.48)
    Alternative name(s):
    Cbl-interacting protein p70
    Suppressor of T-cell receptor signaling 1
    Short name:
    STS-1
    T-cell ubiquitin ligand 2
    Short name:
    TULA-2
    Tyrosine-protein phosphatase STS1/TULA2
    Gene namesi
    Name:Ubash3b
    Synonyms:Sts1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1920078. Ubash3b.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice display strikingly elevated levels of tyrosine phosphorylated, ubiquitinated proteins following TCR stimulation. They are prothrombotic and have shorter bleeding times, which is attributed to insufficient SYK dephosphorylation in platelets.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 638638Ubiquitin-associated and SH3 domain-containing protein BPRO_0000245509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91PhosphoserineBy similarity
    Modified residuei12 – 121PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BGG7.
    PaxDbiQ8BGG7.
    PRIDEiQ8BGG7.

    PTM databases

    PhosphoSiteiQ8BGG7.

    Expressioni

    Tissue specificityi

    Detected in splenic T-cells and B-cells, total spleen, skeletal muscle, heart, lung, kidney, thymus, brain and liver (at protein level). Highly expressed in brain. Detected in heart, spleen, lung, liver, kidney and testis.2 Publications

    Gene expression databases

    ArrayExpressiQ8BGG7.
    BgeeiQ8BGG7.
    CleanExiMM_UBASH3B.
    GenevestigatoriQ8BGG7.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with JAK2 (in vitro). Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZAP70P4340310EBI-8846415,EBI-1211276From a different organism.

    Protein-protein interaction databases

    IntActiQ8BGG7. 1 interaction.
    STRINGi10090.ENSMUSP00000043865.

    Structurei

    Secondary structure

    1
    638
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi374 – 3796
    Helixi384 – 3885
    Helixi392 – 3954
    Helixi421 – 4244
    Helixi432 – 44716
    Beta strandi454 – 4574
    Helixi461 – 47313
    Turni477 – 4793
    Beta strandi482 – 4843
    Helixi486 – 4883
    Helixi492 – 4943
    Beta strandi495 – 4995
    Helixi506 – 5116
    Helixi526 – 5283
    Helixi535 – 55319
    Turni554 – 5563
    Beta strandi558 – 5647
    Helixi568 – 5714
    Turni572 – 5743
    Helixi575 – 5773
    Helixi584 – 5918
    Beta strandi599 – 6046
    Beta strandi606 – 6083
    Beta strandi611 – 6144
    Helixi631 – 6355

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H0QX-ray1.82A/B/C373-633[»]
    2IKQX-ray2.61A/B/M369-638[»]
    3MBKX-ray1.35A/B373-636[»]
    ProteinModelPortaliQ8BGG7.
    SMRiQ8BGG7. Positions 15-67, 238-317, 373-636.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8BGG7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 6543UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini243 – 30866SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni369 – 638270Protein tyrosine phosphataseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi325 – 3284Poly-Ser

    Sequence similaritiesi

    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG276661.
    GeneTreeiENSGT00390000018249.
    HOGENOMiHOG000012936.
    HOVERGENiHBG018025.
    InParanoidiQ8BGG7.
    OMAiADECGTW.
    OrthoDBiEOG7P5T0D.
    PhylomeDBiQ8BGG7.
    TreeFamiTF313334.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001452. SH3_domain.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PfamiPF00300. His_Phos_1. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF53254. SSF53254. 2 hits.
    PROSITEiPS50002. SH3. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BGG7-1) [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

    MAAREELYSK VTPRRDRLQR PGTVKHGSAL DVLLSMGFPR ARAQKALAST    50
    GGRSVQAACD WLFSHVGDPF LDDPLPREYV LYLRPTGPLA QKLSDFWQQS 100
    KQICGKNKAH NIFPHITLCQ FFMCEDSKVD ALGEALQTTV SRWKCKFSAP 150
    LPLELYTSSN FIGLFVKEDS AEVLKKFAAD FAAEAASKTE VHVEPHKKQL 200
    HVTLAYHFQA SHLPTLEKLA QNIDVKLGCD WVATIFSRDI RFANHETLQV 250
    IYPYSPQNDD ELELVPGDFI FMSPMEQTST SEGWIYGTSL TTGCSGLLPE 300
    NYITKADECS TWIFHGSYSI LNTVSSSSLA FGDGALERRQ YEDQGLGETT 350
    PLTIICQPMQ PLRVNSQPGP QKRCLFVCRH GERMDVVFGK YWLSQCFDAK 400
    GRYIRTNLNM PHSLPQRSGG FRDYEKDAPI TVFGCMQARL VGEALLESNT 450
    VIDHVYCSPS LRCVQTAHNI LKGLQQDNHL KIRVEPGLFE WTKWVAGSTL 500
    PAWIPPSELA AANLSVDTTY RPHIPVSKLA ISESYDTYIN RSFQVTKEII 550
    SECKSKGNNI LIVAHASSLE ACTCQLQGLS PQNSKDFVQM VRKIPYLGFC 600
    SCEELGETGI WQLTDPPILP LTHGPTGGFN WRETLLQE 638
    Length:638
    Mass (Da):71,443
    Last modified:March 1, 2003 - v1
    Checksum:i9B665F45AF208EF6
    GO
    Isoform 2 (identifier: Q8BGG7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-122: Missing.

    Show »
    Length:516
    Mass (Da):57,693
    Checksum:i2F00BDB1F01C31FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3001E → G in BAE30779. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001E → G in BAE30875. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 122122Missing in isoform 2. 1 PublicationVSP_019716Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB075602 mRNA. Translation: BAD06450.1.
    AK013361 mRNA. Translation: BAC25403.1.
    AK034450 mRNA. Translation: BAC28714.1.
    AK035764 mRNA. Translation: BAC29178.1.
    AK133948 mRNA. Translation: BAE21945.1.
    AK151895 mRNA. Translation: BAE30779.1.
    AK152013 mRNA. Translation: BAE30875.1.
    AK154576 mRNA. Translation: BAE32688.1.
    BC053436 mRNA. Translation: AAH53436.1.
    CCDSiCCDS23085.1. [Q8BGG7-1]
    RefSeqiNP_789830.1. NM_176860.5. [Q8BGG7-1]
    XP_006510700.1. XM_006510637.1. [Q8BGG7-2]
    UniGeneiMm.133615.

    Genome annotation databases

    EnsembliENSMUST00000044155; ENSMUSP00000043865; ENSMUSG00000032020. [Q8BGG7-1]
    ENSMUST00000151485; ENSMUSP00000116038; ENSMUSG00000032020. [Q8BGG7-2]
    GeneIDi72828.
    KEGGimmu:72828.
    UCSCiuc009pag.1. mouse. [Q8BGG7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB075602 mRNA. Translation: BAD06450.1 .
    AK013361 mRNA. Translation: BAC25403.1 .
    AK034450 mRNA. Translation: BAC28714.1 .
    AK035764 mRNA. Translation: BAC29178.1 .
    AK133948 mRNA. Translation: BAE21945.1 .
    AK151895 mRNA. Translation: BAE30779.1 .
    AK152013 mRNA. Translation: BAE30875.1 .
    AK154576 mRNA. Translation: BAE32688.1 .
    BC053436 mRNA. Translation: AAH53436.1 .
    CCDSi CCDS23085.1. [Q8BGG7-1 ]
    RefSeqi NP_789830.1. NM_176860.5. [Q8BGG7-1 ]
    XP_006510700.1. XM_006510637.1. [Q8BGG7-2 ]
    UniGenei Mm.133615.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H0Q X-ray 1.82 A/B/C 373-633 [» ]
    2IKQ X-ray 2.61 A/B/M 369-638 [» ]
    3MBK X-ray 1.35 A/B 373-636 [» ]
    ProteinModelPortali Q8BGG7.
    SMRi Q8BGG7. Positions 15-67, 238-317, 373-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BGG7. 1 interaction.
    STRINGi 10090.ENSMUSP00000043865.

    PTM databases

    PhosphoSitei Q8BGG7.

    Proteomic databases

    MaxQBi Q8BGG7.
    PaxDbi Q8BGG7.
    PRIDEi Q8BGG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044155 ; ENSMUSP00000043865 ; ENSMUSG00000032020 . [Q8BGG7-1 ]
    ENSMUST00000151485 ; ENSMUSP00000116038 ; ENSMUSG00000032020 . [Q8BGG7-2 ]
    GeneIDi 72828.
    KEGGi mmu:72828.
    UCSCi uc009pag.1. mouse. [Q8BGG7-1 ]

    Organism-specific databases

    CTDi 84959.
    MGIi MGI:1920078. Ubash3b.

    Phylogenomic databases

    eggNOGi NOG276661.
    GeneTreei ENSGT00390000018249.
    HOGENOMi HOG000012936.
    HOVERGENi HBG018025.
    InParanoidi Q8BGG7.
    OMAi ADECGTW.
    OrthoDBi EOG7P5T0D.
    PhylomeDBi Q8BGG7.
    TreeFami TF313334.

    Miscellaneous databases

    EvolutionaryTracei Q8BGG7.
    NextBioi 337005.
    PROi Q8BGG7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BGG7.
    Bgeei Q8BGG7.
    CleanExi MM_UBASH3B.
    Genevestigatori Q8BGG7.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001452. SH3_domain.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    Pfami PF00300. His_Phos_1. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF53254. SSF53254. 2 hits.
    PROSITEi PS50002. SH3. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NF-E2 inducible megakaryocyte specific novel gene."
      Nagata Y., Oda M., Haruta H., Todokoro K.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Megakaryocyte.
    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 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Cerebellum, Dendritic cell, Diencephalon and Embryo.
    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 1).
      Tissue: Embryonic limb.
    4. "Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein."
      Carpino N., Kobayashi R., Zang H., Takahashi Y., Jou S.-T., Feng J., Nakajima H., Ihle J.N.
      Mol. Cell. Biol. 22:7491-7500(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 93-101; 199-215; 403-410; 482-493 AND 495-515, INTERACTION WITH JAK2, TISSUE SPECIFICITY.
    5. "Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2."
      Carpino N., Turner S., Mekala D., Takahashi Y., Zang H., Geiger T.L., Doherty P., Ihle J.N.
      Immunity 20:37-46(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "The Sts proteins target tyrosine phosphorylated, ubiquitinated proteins within TCR signaling pathways."
      Carpino N., Chen Y., Nassar N., Oh H.W.
      Mol. Immunol. 46:3224-3231(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in platelets."
      Thomas D.H., Getz T.M., Newman T.N., Dangelmaier C.A., Carpino N., Kunapuli S.P., Tsygankov A.Y., Daniel J.L.
      Blood 116:2570-2578(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate."
      Chen X., Ren L., Kim S., Carpino N., Daniel J.L., Kunapuli S.P., Tsygankov A.Y., Pei D.
      J. Biol. Chem. 285:31268-31276(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    9. "The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate."
      Jakoncic J., Sondgeroth B., Carpino N., Nassar N.
      Acta Crystallogr. F 66:643-647(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 373-636 IN COMPLEX WITH SULFATE, SUBUNIT, ACTIVE SITE.
    10. "A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling."
      Mikhailik A., Ford B., Keller J., Chen Y., Nassar N., Carpino N.
      Mol. Cell 27:486-497(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 373-633, SUBUNIT, FUNCTION, PHOSPHATASE ACTIVITY, ACTIVE SITE.

    Entry informationi

    Entry nameiUBS3B_MOUSE
    AccessioniPrimary (citable) accession number: Q8BGG7
    Secondary accession number(s): Q3U8Z2, Q8BMW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 101 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

    3D-structure, Complete proteome, Direct protein sequencing, 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