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Q9HCE7

- SMUF1_HUMAN

UniProt

Q9HCE7 - SMUF1_HUMAN

Protein

E3 ubiquitin-protein ligase SMURF1

Gene

SMURF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (13 Dec 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA.3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei725 – 7251Glycyl thioester intermediate

    GO - Molecular functioni

    1. activin binding Source: BHF-UCL
    2. I-SMAD binding Source: BHF-UCL
    3. ligase activity Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. R-SMAD binding Source: BHF-UCL
    6. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. BMP signaling pathway Source: UniProtKB
    2. cell differentiation Source: UniProtKB
    3. ectoderm development Source: UniProtKB
    4. negative regulation of BMP signaling pathway Source: UniProtKB
    5. negative regulation of ossification Source: Ensembl
    6. negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCL
    8. protein export from nucleus Source: BHF-UCL
    9. protein localization to cell surface Source: BHF-UCL
    10. protein polyubiquitination Source: UniProtKB
    11. protein ubiquitination Source: BHF-UCL
    12. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    13. receptor catabolic process Source: BHF-UCL
    14. transforming growth factor beta receptor signaling pathway Source: Reactome
    15. ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_12034. Signaling by BMP.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9HCE7.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase SMURF1 (EC:6.3.2.-)
    Short name:
    hSMURF1
    Alternative name(s):
    SMAD ubiquitination regulatory factor 1
    SMAD-specific E3 ubiquitin-protein ligase 1
    Gene namesi
    Name:SMURF1
    Synonyms:KIAA1625
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:16807. SMURF1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. neuronal cell body Source: Ensembl
    5. nucleoplasm Source: Reactome
    6. nucleus Source: RefGenome
    7. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281K → A: Fails to ubiquitinate RHOA; when associated with A-85. 1 Publication
    Mutagenesisi85 – 851K → A: Fails to ubiquitinate RHOA; when associated with A-28. 1 Publication
    Mutagenesisi350 – 3501K → R: Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381 and R-381. 1 Publication
    Mutagenesisi381 – 3811K → R: Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-350 and R-383. Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-383. 1 Publication
    Mutagenesisi383 – 3831K → R: Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-350 and R-381. Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381. 1 Publication
    Mutagenesisi725 – 7251C → A: Loss of enzyme activity, without abolishing FBXL15-mediated ubiquitination. 2 Publications

    Organism-specific databases

    PharmGKBiPA134987175.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 757757E3 ubiquitin-protein ligase SMURF1PRO_0000120326Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki381 – 381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki383 – 383Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Ubiquitinated by the SCF(FBXL15) complex at Lys-381 and Lys-383, leading to its degradation by the proteasome. Lys-383 is the primary ubiquitination site.1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9HCE7.
    PaxDbiQ9HCE7.
    PRIDEiQ9HCE7.

    PTM databases

    PhosphoSiteiQ9HCE7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HCE7.
    BgeeiQ9HCE7.
    CleanExiHS_SMURF1.
    GenevestigatoriQ9HCE7.

    Organism-specific databases

    HPAiCAB013009.

    Interactioni

    Subunit structurei

    Interacts with TRAF4. Interacts (via HECT domain) with FBXL15 (via LRR repeats). Interacts with SMAD7 and TGFBR1; SMAD7 recruits SMURF1 to TGFBR1 and regulates TGF-beta receptor degradation.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FBXL15Q9H4696EBI-976466,EBI-6144096
    ING2Q9H1604EBI-976466,EBI-389787
    PLEKHO1Q53GL02EBI-976466,EBI-949945
    PSME3P612895EBI-976466,EBI-355546
    RHOAP615862EBI-976466,EBI-446668
    SMAD1Q157974EBI-976466,EBI-1567153

    Protein-protein interaction databases

    BioGridi121411. 323 interactions.
    DIPiDIP-36709N.
    IntActiQ9HCE7. 15 interactions.
    MINTiMINT-102628.
    STRINGi9606.ENSP00000354621.

    Structurei

    Secondary structure

    1
    757
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 2412
    Beta strandi36 – 427
    Turni43 – 453
    Beta strandi48 – 503
    Beta strandi61 – 7111
    Beta strandi76 – 827
    Helixi83 – 853
    Turni90 – 934
    Beta strandi94 – 1007
    Helixi102 – 1087
    Beta strandi114 – 1174
    Beta strandi131 – 1399
    Beta strandi241 – 2455
    Turni246 – 2483
    Beta strandi249 – 2546
    Turni255 – 2584
    Beta strandi259 – 2635
    Beta strandi312 – 3176
    Turni318 – 3203
    Beta strandi321 – 3266
    Turni327 – 3304
    Beta strandi331 – 3344

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LAZNMR-A235-267[»]
    2LB0NMR-A235-267[»]
    2LB1NMR-A305-339[»]
    2LTXNMR-A306-340[»]
    3PYCX-ray1.96A13-140[»]
    ProteinModelPortaliQ9HCE7.
    SMRiQ9HCE7. Positions 13-140, 228-754.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HCE7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9999C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini234 – 26734WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini306 – 33934WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini420 – 757338HECTPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C2 domain mediates membrane localization and substrate selection.1 Publication

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 2 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    HOGENOMiHOG000208451.
    HOVERGENiHBG004134.
    InParanoidiQ9HCE7.
    KOiK04678.
    OMAiHVQTPQN.
    OrthoDBiEOG77Q4W4.
    PhylomeDBiQ9HCE7.
    TreeFamiTF323658.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 2 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 2 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 2 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9HCE7-1) [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

    MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS    50
    TDTVKNTLDP KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL 100
    LSNAISRLKD TGYQRLDLCK LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV 150
    DCRGLLENEG TVYEDSGPGR PLSCFMEEPA PYTDSTGAAA GGGNCRFVES 200
    PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY EQRTTVQGQV 250
    YFLHTQTGVS TWHDPRIPSP SGTIPGGDAA FLYEFLLQGH TSEPRDLNSV 300
    NCDELGPLPP GWEVRSTVSG RIYFVDHNNR TTQFTDPRLH HIMNHQCQLK 350
    EPSQPLPLPS EGSLEDEELP AQRYERDLVQ KLKVLRHELS LQQPQAGHCR 400
    IEVSREEIFE ESYRQIMKMR PKDLKKRLMV KFRGEEGLDY GGVAREWLYL 450
    LCHEMLNPYY GLFQYSTDNI YMLQINPDSS INPDHLSYFH FVGRIMGLAV 500
    FHGHYINGGF TVPFYKQLLG KPIQLSDLES VDPELHKSLV WILENDITPV 550
    LDHTFCVEHN AFGRILQHEL KPNGRNVPVT EENKKEYVRL YVNWRFMRGI 600
    EAQFLALQKG FNELIPQHLL KPFDQKELEL IIGGLDKIDL NDWKSNTRLK 650
    HCVADSNIVR WFWQAVETFD EERRARLLQF VTGSTRVPLQ GFKALQGSTG 700
    AAGPRLFTIH LIDANTDNLP KAHTCFNRID IPPYESYEKL YEKLLTAVEE 750
    TCGFAVE 757
    Length:757
    Mass (Da):86,114
    Last modified:December 13, 2001 - v2
    Checksum:i89A171CFC47B40E9
    GO
    Isoform Short (identifier: Q9HCE7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-294: Missing.

    Show »
    Length:731
    Mass (Da):83,440
    Checksum:iF106E00CA3C210AA
    GO

    Sequence cautioni

    The sequence BAB13451.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti447 – 4471W → G in AAI44415. (PubMed:15489334)Curated
    Sequence conflicti697 – 6993Missing in AAI36805. (PubMed:15489334)Curated
    Sequence conflicti697 – 6993Missing in AAI44415. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti466 – 4661S → Y.
    Corresponds to variant rs13246077 [ dbSNP | Ensembl ].
    VAR_052959

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei269 – 29426Missing in isoform Short. 2 PublicationsVSP_006812Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046845 mRNA. Translation: BAB13451.1. Different initiation.
    AC004893 Genomic DNA. Translation: AAC62434.1.
    AF464850 mRNA. Translation: AAM90910.1.
    AC073468 Genomic DNA. No translation available.
    AC114500 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23885.1.
    CH236956 Genomic DNA. Translation: EAL23886.1.
    CH471091 Genomic DNA. Translation: EAW76687.1.
    CH471091 Genomic DNA. Translation: EAW76688.1.
    BC136804 mRNA. Translation: AAI36805.1.
    BC144414 mRNA. Translation: AAI44415.1.
    BC152468 mRNA. Translation: AAI52469.1.
    AF199364 mRNA. Translation: AAF08298.2.
    CCDSiCCDS34689.1. [Q9HCE7-2]
    CCDS34690.1. [Q9HCE7-1]
    RefSeqiNP_001186776.1. NM_001199847.1.
    NP_065162.1. NM_020429.2. [Q9HCE7-1]
    NP_851994.1. NM_181349.2. [Q9HCE7-2]
    UniGeneiHs.189329.

    Genome annotation databases

    EnsembliENST00000361125; ENSP00000354621; ENSG00000198742. [Q9HCE7-1]
    ENST00000361368; ENSP00000355326; ENSG00000198742. [Q9HCE7-2]
    GeneIDi57154.
    KEGGihsa:57154.
    UCSCiuc003upt.3. human. [Q9HCE7-2]
    uc003upu.2. human. [Q9HCE7-1]

    Polymorphism databases

    DMDMi17865625.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046845 mRNA. Translation: BAB13451.1 . Different initiation.
    AC004893 Genomic DNA. Translation: AAC62434.1 .
    AF464850 mRNA. Translation: AAM90910.1 .
    AC073468 Genomic DNA. No translation available.
    AC114500 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23885.1 .
    CH236956 Genomic DNA. Translation: EAL23886.1 .
    CH471091 Genomic DNA. Translation: EAW76687.1 .
    CH471091 Genomic DNA. Translation: EAW76688.1 .
    BC136804 mRNA. Translation: AAI36805.1 .
    BC144414 mRNA. Translation: AAI44415.1 .
    BC152468 mRNA. Translation: AAI52469.1 .
    AF199364 mRNA. Translation: AAF08298.2 .
    CCDSi CCDS34689.1. [Q9HCE7-2 ]
    CCDS34690.1. [Q9HCE7-1 ]
    RefSeqi NP_001186776.1. NM_001199847.1.
    NP_065162.1. NM_020429.2. [Q9HCE7-1 ]
    NP_851994.1. NM_181349.2. [Q9HCE7-2 ]
    UniGenei Hs.189329.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LAZ NMR - A 235-267 [» ]
    2LB0 NMR - A 235-267 [» ]
    2LB1 NMR - A 305-339 [» ]
    2LTX NMR - A 306-340 [» ]
    3PYC X-ray 1.96 A 13-140 [» ]
    ProteinModelPortali Q9HCE7.
    SMRi Q9HCE7. Positions 13-140, 228-754.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121411. 323 interactions.
    DIPi DIP-36709N.
    IntActi Q9HCE7. 15 interactions.
    MINTi MINT-102628.
    STRINGi 9606.ENSP00000354621.

    PTM databases

    PhosphoSitei Q9HCE7.

    Polymorphism databases

    DMDMi 17865625.

    Proteomic databases

    MaxQBi Q9HCE7.
    PaxDbi Q9HCE7.
    PRIDEi Q9HCE7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361125 ; ENSP00000354621 ; ENSG00000198742 . [Q9HCE7-1 ]
    ENST00000361368 ; ENSP00000355326 ; ENSG00000198742 . [Q9HCE7-2 ]
    GeneIDi 57154.
    KEGGi hsa:57154.
    UCSCi uc003upt.3. human. [Q9HCE7-2 ]
    uc003upu.2. human. [Q9HCE7-1 ]

    Organism-specific databases

    CTDi 57154.
    GeneCardsi GC07M098627.
    HGNCi HGNC:16807. SMURF1.
    HPAi CAB013009.
    MIMi 605568. gene.
    neXtProti NX_Q9HCE7.
    PharmGKBi PA134987175.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000208451.
    HOVERGENi HBG004134.
    InParanoidi Q9HCE7.
    KOi K04678.
    OMAi HVQTPQN.
    OrthoDBi EOG77Q4W4.
    PhylomeDBi Q9HCE7.
    TreeFami TF323658.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_12034. Signaling by BMP.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9HCE7.

    Miscellaneous databases

    ChiTaRSi SMURF1. human.
    EvolutionaryTracei Q9HCE7.
    GeneWikii SMURF1.
    GenomeRNAii 57154.
    NextBioi 63133.
    PROi Q9HCE7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCE7.
    Bgeei Q9HCE7.
    CleanExi HS_SMURF1.
    Genevestigatori Q9HCE7.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 2 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Brain.
    2. "Smurf1-beta, an alternatively spliced variant of Smad-ubiquitin E3 ligase Smurf1."
      Liang M., Lin X., Feng X.-H.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS LONG AND SHORT).
      Tissue: Brain and Testis.
    7. "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation."
      Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.
      Nature 400:687-693(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-731 (ISOFORM SHORT), FUNCTION.
    8. "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
      Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
      Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD7 AND TGFBR1.
    9. "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
      Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
      Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-725, INTERACTION WITH TRAF4.
    10. "SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
      Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
      EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-381 AND LYS-383, INTERACTION WITH FBXL15, MUTAGENESIS OF LYS-350; LYS-381; LYS-383 AND CYS-725.
    11. "Pivotal role of the C2 domain of the Smurf1 ubiquitin ligase in substrate selection."
      Lu K., Li P., Zhang M., Xing G., Li X., Zhou W., Bartlam M., Zhang L., Rao Z., He F.
      J. Biol. Chem. 286:16861-16870(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 13-140, FUNCTION, DOMAIN C2, INTERACTION WITH RHOA, MUTAGENESIS OF LYS-28 AND LYS-85.

    Entry informationi

    Entry nameiSMUF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCE7
    Secondary accession number(s): A4D279
    , B7ZMB6, B9EGV3, O75853, Q547Q3, Q9UJT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3