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Protein

E3 ubiquitin-protein ligase SMURF1

Gene

Smurf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Plays a role in dendrite formation by melanocytes.By similarity

Pathwayi: 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 sitei699 – 6991Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Differentiation, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-201451. Signaling by BMP.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-5632684. Hedgehog 'on' state.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase SMURF1 (EC:6.3.2.-)
Alternative name(s):
SMAD ubiquitination regulatory factor 1
SMAD-specific E3 ubiquitin-protein ligase 1
Gene namesi
Name:Smurf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1923038. Smurf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731E3 ubiquitin-protein ligase SMURF1PRO_0000120327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki355 – 355Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki357 – 357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Ubiquitinated by the SCF(FBXL15) complex at Lys-355 and Lys-357, leading to its degradation by the proteasome. Lys-357 is the primary ubiquitination site (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9CUN6.
PaxDbiQ9CUN6.
PRIDEiQ9CUN6.

PTM databases

iPTMnetiQ9CUN6.
PhosphoSiteiQ9CUN6.

Expressioni

Gene expression databases

BgeeiQ9CUN6.
CleanExiMM_SMURF1.
ExpressionAtlasiQ9CUN6. baseline and differential.
GenevisibleiQ9CUN6. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi217743. 14 interactions.
IntActiQ9CUN6. 2 interactions.
MINTiMINT-1340776.
STRINGi10090.ENSMUSP00000082827.

Structurei

3D structure databases

ProteinModelPortaliQ9CUN6.
SMRiQ9CUN6. Positions 13-140, 228-728.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9999C2PROSITE-ProRule annotationAdd
BLAST
Domaini234 – 26734WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini280 – 31334WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini394 – 731338HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi144 – 1474Poly-Gly

Domaini

The C2 domain mediates membrane localization and substrate selection.By similarity

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

eggNOGiKOG0940. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9CUN6.
KOiK04678.
PhylomeDBiQ9CUN6.
TreeFamiTF323658.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
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]

Sequencei

Sequence statusi: Complete.

Q9CUN6-1 [UniParc]FASTAAdd to basket

« 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 DRIGGGGSVV
160 170 180 190 200
DCRGLLENEG TVYEDSGPGR PLSCLMEEPA PYTDGTGAAA GGGNCRFVES
210 220 230 240 250
PSQDQRLLVQ RLRNPEVRGP LQTPQNRPHG HQSPELPEGY EQRTTVQGQV
260 270 280 290 300
YFLHTQTGVS TWHDPRIPRD LNSVNCDELG PLPPGWEVRS TVSGRIYFVD
310 320 330 340 350
HNNRTTQFTD PRLHHIMNHQ CQLKEPSQPL QLPSEGSVED EELPAQRYER
360 370 380 390 400
DLVQKLKVLR HELSLQQPQA GHCRIEVSRE EIFEESYRQI MKMRPKDLKK
410 420 430 440 450
RLMVKFRGEE GLDYGGVARE WLYLLCHEML NPYYGLFQYS TDNIYTLQIN
460 470 480 490 500
PDSSINPDHL SYFHFVGRIM GLAVFHGHYI NGGFTVPFYK QLLGKPIQLS
510 520 530 540 550
DLESVDPELH KSLVWILEND ITPVLDHTFC VEHNAFGRIL QHELKPNGRN
560 570 580 590 600
VPVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFDQK
610 620 630 640 650
ELELIIGGLD KIDLNDWKSN TRLKHCVADS NIVRWFWQAV ETFDEERRAR
660 670 680 690 700
LLQFVTGSTR VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF
710 720 730
NRIDIPPYES YEKLYEKLLT AVEETCGFAV E
Length:731
Mass (Da):83,356
Last modified:January 10, 2006 - v2
Checksum:iF0A7A1B019CC9D3E
GO

Sequence cautioni

The sequence BAB29770.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631N → S in AAH29097 (PubMed:15489334).Curated
Sequence conflicti204 – 2041D → N in BAB29770 (PubMed:16141072).Curated
Sequence conflicti213 – 2131R → Q in BAB29770 (PubMed:16141072).Curated
Sequence conflicti218 – 2181R → Q in BAB29770 (PubMed:16141072).Curated
Sequence conflicti278 – 2781E → G in BAE32623 (PubMed:16141072).Curated
Sequence conflicti334 – 3341S → N in BAB29770 (PubMed:16141072).Curated
Sequence conflicti446 – 4461T → K in BAB29770 (PubMed:16141072).Curated
Sequence conflicti671 – 6733Missing in BAB29770 (PubMed:16141072).Curated
Sequence conflicti671 – 6733Missing in AAH29097 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015264 mRNA. Translation: BAB29770.2. Different initiation.
AK154491 mRNA. Translation: BAE32623.1.
BC029097 mRNA. Translation: AAH29097.1.
CCDSiCCDS39380.1.
RefSeqiNP_001033716.1. NM_001038627.1.
NP_083714.3. NM_029438.3.
UniGeneiMm.27735.

Genome annotation databases

EnsembliENSMUST00000085684; ENSMUSP00000082827; ENSMUSG00000038780.
GeneIDi75788.
KEGGimmu:75788.
UCSCiuc009alv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015264 mRNA. Translation: BAB29770.2. Different initiation.
AK154491 mRNA. Translation: BAE32623.1.
BC029097 mRNA. Translation: AAH29097.1.
CCDSiCCDS39380.1.
RefSeqiNP_001033716.1. NM_001038627.1.
NP_083714.3. NM_029438.3.
UniGeneiMm.27735.

3D structure databases

ProteinModelPortaliQ9CUN6.
SMRiQ9CUN6. Positions 13-140, 228-728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217743. 14 interactions.
IntActiQ9CUN6. 2 interactions.
MINTiMINT-1340776.
STRINGi10090.ENSMUSP00000082827.

PTM databases

iPTMnetiQ9CUN6.
PhosphoSiteiQ9CUN6.

Proteomic databases

MaxQBiQ9CUN6.
PaxDbiQ9CUN6.
PRIDEiQ9CUN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085684; ENSMUSP00000082827; ENSMUSG00000038780.
GeneIDi75788.
KEGGimmu:75788.
UCSCiuc009alv.1. mouse.

Organism-specific databases

CTDi57154.
MGIiMGI:1923038. Smurf1.

Phylogenomic databases

eggNOGiKOG0940. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9CUN6.
KOiK04678.
PhylomeDBiQ9CUN6.
TreeFamiTF323658.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-201451. Signaling by BMP.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-5632684. Hedgehog 'on' state.

Miscellaneous databases

PROiQ9CUN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CUN6.
CleanExiMM_SMURF1.
ExpressionAtlasiQ9CUN6. baseline and differential.
GenevisibleiQ9CUN6. MM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
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

  1. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Testis.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiSMUF1_MOUSE
AccessioniPrimary (citable) accession number: Q9CUN6
Secondary accession number(s): Q3U412, Q8K300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: January 10, 2006
Last modified: June 8, 2016
This is version 140 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

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 one 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.