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Protein

E3 ubiquitin-protein ligase SMURF1

Gene

SMURF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

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

GO - Molecular functioni

  • activin binding Source: BHF-UCL
  • I-SMAD binding Source: BHF-UCL
  • ligase activity Source: UniProtKB-KW
  • phospholipid binding Source: ParkinsonsUK-UCL
  • R-SMAD binding Source: BHF-UCL
  • ubiquitin protein ligase activity Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • BMP signaling pathway Source: UniProtKB
  • cell differentiation Source: UniProtKB
  • ectoderm development Source: UniProtKB
  • negative regulation of BMP signaling pathway Source: UniProtKB
  • negative regulation of ossification Source: Ensembl
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • positive regulation of dendrite extension Source: UniProtKB
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CACAO
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • protein export from nucleus Source: BHF-UCL
  • protein localization to cell surface Source: BHF-UCL
  • protein polyubiquitination Source: UniProtKB
  • protein targeting to plasma membrane Source: ParkinsonsUK-UCL
  • protein targeting to vacuole involved in autophagy Source: ParkinsonsUK-UCL
  • protein ubiquitination Source: BHF-UCL
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • receptor catabolic process Source: BHF-UCL
  • transforming growth factor beta receptor signaling pathway Source: GO_Central
  • ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B9. 2681.
6.3.2.19. 2681.
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_264478. Asymmetric localization of PCP proteins.
REACT_268718. Hedgehog 'on' state.
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16807. SMURF1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleoplasm Source: Reactome
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiSMURF1.
DMDMi17865625.

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

BgeeiQ9HCE7.
CleanExiHS_SMURF1.
GenevisibleiQ9HCE7. HS.

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
CHEK1O147574EBI-9845742,EBI-974488
FBXL15Q9H4696EBI-976466,EBI-6144096
ING2Q9H1603EBI-9845742,EBI-389787
KLF2Q9Y5W34EBI-9845742,EBI-9846663
PLEKHO1Q53GL04EBI-9845742,EBI-949945
PSME3P612895EBI-976466,EBI-355546
RHOAP615862EBI-9845742,EBI-446668
RHOBP627453EBI-9845742,EBI-602647
SMAD1Q157972EBI-976466,EBI-1567153
TRAF4Q9BUZ44EBI-9845742,EBI-3650647

Protein-protein interaction databases

BioGridi121411. 327 interactions.
DIPiDIP-36709N.
IntActiQ9HCE7. 24 interactions.
MINTiMINT-102628.
STRINGi9606.ENSP00000354621.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9HCE7.
KOiK04678.
OMAiTDNGRIY.
OrthoDBiEOG77Q4W4.
PhylomeDBiQ9HCE7.
TreeFamiTF323658.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]
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. AlignAdd to basket

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

        10         20         30         40         50
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS
60 70 80 90 100
TDTVKNTLDP KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL
110 120 130 140 150
LSNAISRLKD TGYQRLDLCK LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV
160 170 180 190 200
DCRGLLENEG TVYEDSGPGR PLSCFMEEPA PYTDSTGAAA GGGNCRFVES
210 220 230 240 250
PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY EQRTTVQGQV
260 270 280 290 300
YFLHTQTGVS TWHDPRIPSP SGTIPGGDAA FLYEFLLQGH TSEPRDLNSV
310 320 330 340 350
NCDELGPLPP GWEVRSTVSG RIYFVDHNNR TTQFTDPRLH HIMNHQCQLK
360 370 380 390 400
EPSQPLPLPS EGSLEDEELP AQRYERDLVQ KLKVLRHELS LQQPQAGHCR
410 420 430 440 450
IEVSREEIFE ESYRQIMKMR PKDLKKRLMV KFRGEEGLDY GGVAREWLYL
460 470 480 490 500
LCHEMLNPYY GLFQYSTDNI YMLQINPDSS INPDHLSYFH FVGRIMGLAV
510 520 530 540 550
FHGHYINGGF TVPFYKQLLG KPIQLSDLES VDPELHKSLV WILENDITPV
560 570 580 590 600
LDHTFCVEHN AFGRILQHEL KPNGRNVPVT EENKKEYVRL YVNWRFMRGI
610 620 630 640 650
EAQFLALQKG FNELIPQHLL KPFDQKELEL IIGGLDKIDL NDWKSNTRLK
660 670 680 690 700
HCVADSNIVR WFWQAVETFD EERRARLLQF VTGSTRVPLQ GFKALQGSTG
710 720 730 740 750
AAGPRLFTIH LIDANTDNLP KAHTCFNRID IPPYESYEKL YEKLLTAVEE

TCGFAVE
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi121411. 327 interactions.
DIPiDIP-36709N.
IntActiQ9HCE7. 24 interactions.
MINTiMINT-102628.
STRINGi9606.ENSP00000354621.

PTM databases

PhosphoSiteiQ9HCE7.

Polymorphism and mutation databases

BioMutaiSMURF1.
DMDMi17865625.

Proteomic databases

MaxQBiQ9HCE7.
PaxDbiQ9HCE7.
PRIDEiQ9HCE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi57154.
GeneCardsiGC07M098627.
HGNCiHGNC:16807. SMURF1.
HPAiCAB013009.
MIMi605568. gene.
neXtProtiNX_Q9HCE7.
PharmGKBiPA134987175.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9HCE7.
KOiK04678.
OMAiTDNGRIY.
OrthoDBiEOG77Q4W4.
PhylomeDBiQ9HCE7.
TreeFamiTF323658.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B9. 2681.
6.3.2.19. 2681.
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_264478. Asymmetric localization of PCP proteins.
REACT_268718. Hedgehog 'on' state.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9HCE7.

Miscellaneous databases

ChiTaRSiSMURF1. human.
EvolutionaryTraceiQ9HCE7.
GeneWikiiSMURF1.
GenomeRNAii57154.
NextBioi63133.
PROiQ9HCE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCE7.
CleanExiHS_SMURF1.
GenevisibleiQ9HCE7. HS.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 144 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.