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Q69ZI1

- SH3R1_MOUSE

UniProt

Q69ZI1 - SH3R1_MOUSE

Protein

E3 ubiquitin-protein ligase SH3RF1

Gene

Sh3rf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    Functioni

    Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) By similarity. In fibroblasts, induces apoptosis.By similarity1 Publication
    Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis By similarity.By similarity

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: InterPro
    2. protein ubiquitination Source: UniProtKB-UniPathway
    3. regulation of JNK cascade Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase SH3RF1 (EC:6.3.2.-)
    Alternative name(s):
    Plenty of SH3s
    Short name:
    Protein POSH
    SH3 domain-containing RING finger protein 1
    SH3 multiple domains protein 2
    Gene namesi
    Name:Sh3rf1
    Synonyms:Kiaa1494, Posh, Sh3md2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1913066. Sh3rf1.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity. Cell projectionlamellipodium 1 Publication. Golgi apparatustrans-Golgi network 1 Publication
    Note: Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network.By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-SubCell
    2. lamellipodium Source: UniProtKB-SubCell
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi470 – 4701E → Q: Loss of binding to AKT2. 1 Publication
    Mutagenesisi489 – 4891W → A: Loss of binding to AKT2 and enhanced binding to MAP3K11. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 892892E3 ubiquitin-protein ligase SH3RF1PRO_0000334152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac By similarity.By similarity
    Subject to ubiquitination and proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ69ZI1.
    PRIDEiQ69ZI1.

    PTM databases

    PhosphoSiteiQ69ZI1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    GenevestigatoriQ69ZI1.

    Interactioni

    Subunit structurei

    Interacts with HERP1 By similarity. Interacts with Rac; in a GTP-dependent manner. Interacts with MAP3K10 and MAP3K11. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8, MAPK9, AKT1 and AKT2.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bnip3lQ9Z2F74EBI-957380,EBI-1774669
    SIAH1Q8IUQ45EBI-957380,EBI-747107From a different organism.

    Protein-protein interaction databases

    BioGridi208480. 1 interaction.
    IntActiQ69ZI1. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ69ZI1.
    SMRiQ69ZI1. Positions 3-59, 137-255, 457-512, 839-892.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 19360SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini196 – 25964SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini452 – 51362SH3 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini833 – 89260SH3 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni447 – 550104Interaction with AKT2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi84 – 907Poly-Gly
    Compositional biasi397 – 4037Poly-Pro
    Compositional biasi406 – 43126Ala-richAdd
    BLAST

    Domaini

    The RING finger domain is responsible of ubiquitination and proteasomal degradation.

    Sequence similaritiesi

    Belongs to the SH3RF family.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 4 SH3 domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG314495.
    HOGENOMiHOG000045564.
    HOVERGENiHBG069552.
    InParanoidiQ69ZI1.
    KOiK12171.
    PhylomeDBiQ69ZI1.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR028502. POSH1.
    IPR001452. SH3_domain.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PANTHERiPTHR10661:SF8. PTHR10661:SF8. 1 hit.
    PfamiPF14604. SH3_9. 4 hits.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00184. RING. 1 hit.
    SM00326. SH3. 4 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 4 hits.
    PROSITEiPS50002. SH3. 4 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q69ZI1-1) [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

    MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP    50
    ECRTLVGSGV DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ 100
    GSTVVNCGSK DLQSSQCGQQ PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP 150
    GDLKFSKGDI IILRRQVDEN WYHGEVSGVH GFFPTNFVQI IKPLPQPPPQ 200
    CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG MLADKIGIFP 250
    ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAQSTSAS KHPDTKKNTR 300
    KRHSFTSLTM ANKSSQGSQN RHSMEISPPV LISSSNPTAA ARISELSGLS 350
    CSAPSQVHIS TTGLIVTPPP SSPVTTGPAF TFPSDVPYQA ALGSMNPPLP 400
    PPPLLAATVL ASTPSGATAA VAAAAAAAAA AGMGPRPVMG SSEQIAHLRP 450
    QTRPSVYVAI YPYTPRKEDE LELRKGEMFL VFERCQDGWY KGTSMHTSKI 500
    GVFPGNYVAP VTRAVTNASQ AKVSMSTAGQ ASRGVTMVSP STAGGPTQKP 550
    QGNGVAGNPS VVPTAVVSAA HIQTSPQAKV LLHMSGQMTV NQARNAVRTV 600
    AAHSQERPTA AVTPIQVQNA ACLGPASVGL PHHSLASQPL PPMAGPAAHG 650
    AAVSISRTNA PMACAAGASL ASPNMTSAML ETEPSGRTVT ILPGLPTSPE 700
    SAASACGNSS AGKPDKDSKK EKKGLLKLLS GASTKRKPRV SPPASPTLDV 750
    ELGAGEAPLQ GAVGPELPLG GSHGRVGSCP TDGDGPVAAG TAALAQDAFH 800
    RKTSSLDSAV PIAPPPRQAC SSLGPVMNEA RPVVCERHRV VVSYPPQSEA 850
    ELELKEGDIV FVHKKREDGW FKGTLQRNGK TGLFPGSFVE NI 892
    Length:892
    Mass (Da):93,447
    Last modified:May 20, 2008 - v2
    Checksum:iD92071116F4D6EBE
    GO
    Isoform 2 (identifier: Q69ZI1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-189: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:862
    Mass (Da):89,906
    Checksum:iD2B2F85D18812B47
    GO
    Isoform 3 (identifier: Q69ZI1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         788-828: AAGTAALAQD...ACSSLGPVMN → DRWNSSPSPG...GLLLPGPSHE
         829-892: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:828
    Mass (Da):86,342
    Checksum:iC670E8A5CF0EB1D4
    GO
    Isoform 4 (identifier: Q69ZI1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         345-381: ELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFT → APSQVQGRGQLPKRGLLTSGKILAASFIFALVTSSLL
         382-892: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:381
    Mass (Da):41,433
    Checksum:i991E47F760D876CB
    GO

    Sequence cautioni

    The sequence BAD32463.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti160 – 1601I → T in AAC40070. (PubMed:9482736)Curated
    Sequence conflicti321 – 3211R → S in BAE28367. (PubMed:16141072)Curated
    Sequence conflicti342 – 3421R → G in BAE28367. (PubMed:16141072)Curated
    Sequence conflicti431 – 4311Missing in BAC32385. (PubMed:16141072)Curated
    Sequence conflicti431 – 4311Missing in AAH60113. (PubMed:15489334)Curated
    Sequence conflicti431 – 4311Missing in AAH60696. (PubMed:15489334)Curated
    Sequence conflicti630 – 6301L → M in BAE28367. (PubMed:16141072)Curated
    Sequence conflicti679 – 6791M → V in BAC32385. (PubMed:16141072)Curated
    Sequence conflicti679 – 6791M → V in AAH60113. (PubMed:15489334)Curated
    Sequence conflicti679 – 6791M → V in AAH60696. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei160 – 18930Missing in isoform 2. 1 PublicationVSP_033624Add
    BLAST
    Alternative sequencei345 – 38137ELSGL…GPAFT → APSQVQGRGQLPKRGLLTSG KILAASFIFALVTSSLL in isoform 4. 1 PublicationVSP_033625Add
    BLAST
    Alternative sequencei382 – 892511Missing in isoform 4. 1 PublicationVSP_033626Add
    BLAST
    Alternative sequencei788 – 82841AAGTA…GPVMN → DRWNSSPSPGCLPPQDKLPG LRSAHCSTTSPGLLLPGPSH E in isoform 3. 1 PublicationVSP_033627Add
    BLAST
    Alternative sequencei829 – 89264Missing in isoform 3. 1 PublicationVSP_033628Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030131 mRNA. Translation: AAC40070.1.
    AK173185 mRNA. Translation: BAD32463.1. Different initiation.
    BC060113 mRNA. Translation: AAH60113.1.
    BC060696 mRNA. Translation: AAH60696.1.
    AK088003 mRNA. Translation: BAC40088.1.
    AK045470 mRNA. Translation: BAC32385.1.
    AK148137 mRNA. Translation: BAE28367.1.
    PIRiT09071.
    RefSeqiNP_067481.2. NM_021506.2.
    UniGeneiMm.27949.

    Genome annotation databases

    GeneIDi59009.
    KEGGimmu:59009.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030131 mRNA. Translation: AAC40070.1 .
    AK173185 mRNA. Translation: BAD32463.1 . Different initiation.
    BC060113 mRNA. Translation: AAH60113.1 .
    BC060696 mRNA. Translation: AAH60696.1 .
    AK088003 mRNA. Translation: BAC40088.1 .
    AK045470 mRNA. Translation: BAC32385.1 .
    AK148137 mRNA. Translation: BAE28367.1 .
    PIRi T09071.
    RefSeqi NP_067481.2. NM_021506.2.
    UniGenei Mm.27949.

    3D structure databases

    ProteinModelPortali Q69ZI1.
    SMRi Q69ZI1. Positions 3-59, 137-255, 457-512, 839-892.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208480. 1 interaction.
    IntActi Q69ZI1. 5 interactions.

    PTM databases

    PhosphoSitei Q69ZI1.

    Proteomic databases

    PaxDbi Q69ZI1.
    PRIDEi Q69ZI1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 59009.
    KEGGi mmu:59009.

    Organism-specific databases

    CTDi 57630.
    MGIi MGI:1913066. Sh3rf1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG314495.
    HOGENOMi HOG000045564.
    HOVERGENi HBG069552.
    InParanoidi Q69ZI1.
    KOi K12171.
    PhylomeDBi Q69ZI1.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 314548.
    PROi Q69ZI1.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q69ZI1.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR028502. POSH1.
    IPR001452. SH3_domain.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    PANTHERi PTHR10661:SF8. PTHR10661:SF8. 1 hit.
    Pfami PF14604. SH3_9. 4 hits.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00184. RING. 1 hit.
    SM00326. SH3. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 4 hits.
    PROSITEi PS50002. SH3. 4 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways."
      Tapon N., Nagata K., Lamarche N., Hall A.
      EMBO J. 17:1395-1404(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RAC.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Embryonic tail.
    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] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-892 (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Corpora quadrigemina 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 2).
      Strain: C57BL/6.
      Tissue: Brain.
    5. "POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis."
      Xu Z., Kukekov N.V., Greene L.A.
      EMBO J. 22:252-261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND MAPK9.
    6. "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex."
      Figueroa C., Tarras S., Taylor J., Vojtek A.B.
      J. Biol. Chem. 278:47922-47927(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKT2, MUTAGENESIS OF GLU-470 AND TRP-489, SUBCELLULAR LOCATION.
    7. "Siah1 interacts with the scaffold protein POSH to promote JNK activation and apoptosis."
      Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A.
      J. Biol. Chem. 281:303-312(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1.
    8. "Direct interaction of the molecular scaffolds POSH and JIP is required for apoptotic activation of JNKs."
      Kukekov N.V., Xu Z., Greene L.A.
      J. Biol. Chem. 281:15517-15524(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK8IP.

    Entry informationi

    Entry nameiSH3R1_MOUSE
    AccessioniPrimary (citable) accession number: Q69ZI1
    Secondary accession number(s): O70254
    , Q3UG42, Q6P9M8, Q8BR66, Q8C2T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 82 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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3