Q9HCE7 (SMUF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase SMURF1
Short name=hSMURF1
EC=6.3.2.-

Alternative name(s):
SMAD ubiquitination regulatory factor 1
SMAD-specific E3 ubiquitin-protein ligase 1

Gene names

Name:	SMURF1
Synonyms:	KIAA1625

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.9 Ref.11
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.8 Ref.9 Ref.10 Ref.11
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.10.
Domain	The C2 domain mediates membrane localization and substrate selection. Ref.11
Post-translational modification	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. Ref.10
Sequence similarities	Contains 1 C2 domain. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 2 WW domains.
Sequence caution	The sequence BAB13451.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from direct assay Ref.10. Source: UniProtKB cell differentiation Inferred from direct assay Ref.7. Source: UniProtKB ectoderm development Traceable author statement Ref.7. Source: UniProtKB negative regulation of BMP signaling pathway Traceable author statement Ref.7. Source: UniProtKB negative regulation of ossification Inferred from electronic annotation. Source: Ensembl negative regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 11278251PubMed 12151385. Source: BHF-UCL proteasome-mediated ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 11278251. Source: BHF-UCL protein export from nucleus Inferred from direct assay PubMed 11278251. Source: BHF-UCL protein localization to cell surface Inferred from direct assay PubMed 12151385. Source: BHF-UCL protein polyubiquitination Inferred from direct assay Ref.9. Source: UniProtKB protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.7Ref.9. Source: UniProtKB receptor catabolic process Inferred from direct assay PubMed 12151385. Source: BHF-UCL transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome ubiquitin-dependent SMAD protein catabolic process Inferred from direct assay PubMed 11278251PubMed 12151385. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome neuronal cell body Inferred from electronic annotation. Source: Ensembl nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 12151385. Source: BHF-UCL
Molecular_function	activin binding Non-traceable author statement PubMed 16720724. Source: BHF-UCL ubiquitin-protein ligase activity Inferred from direct assay Ref.7Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FBXL15	Q9H469	6	EBI-976466,EBI-6144096
ING2	Q9H160	4	EBI-976466,EBI-389787
PLEKHO1	Q53GL0	2	EBI-976466,EBI-949945
PSME3	P61289	5	EBI-976466,EBI-355546
RHOA	P61586	2	EBI-976466,EBI-446668
SMAD1	Q15797	4	EBI-976466,EBI-1567153

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q9HCE7-1)

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.

Isoform Short (identifier: Q9HCE7-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 757

757

E3 ubiquitin-protein ligase SMURF1

PRO_0000120326

Regions

Domain

1 – 99

99

C2

Domain

234 – 267

34

WW 1

Domain

306 – 339

34

WW 2

Domain

420 – 757

338

HECT

Sites

Active site

725

1

Glycyl thioester intermediate

Amino acid modifications

Cross-link

381

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Cross-link

383

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Natural variations

Alternative sequence

269 – 294

26

Missing in isoform Short.

VSP_006812

Natural variant

466

1

S → Y.
Corresponds to variant rs13246077 [ dbSNP | Ensembl ].

VAR_052959

Experimental info

Mutagenesis

28

1

K → A: Fails to ubiquitinate RHOA; when associated with A-85. Ref.11

Mutagenesis

85

1

K → A: Fails to ubiquitinate RHOA; when associated with A-28. Ref.11

Mutagenesis

350

1

K → R: Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381 and R-381. Ref.10

Mutagenesis

381

1

K → 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. Ref.10

Mutagenesis

383

1

K → 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. Ref.10

Mutagenesis

725

1

C → A: Loss of enzyme activity, without abolishing FBXL15-mediated ubiquitination. Ref.9 Ref.10

Sequence conflict

447

1

W → G in AAI44415. Ref.6

Sequence conflict

697 – 699

3

Missing in AAI36805. Ref.6

Sequence conflict

697 – 699

3

Missing in AAI44415. Ref.6

Secondary structure

1

.

.

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.

.

.

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.

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757

Helix Strand Turn

Details...

Beta strand

13 – 24

12

Beta strand

36 – 42

7

Turn

43 – 45

3

Beta strand

48 – 50

3

Beta strand

61 – 71

11

Beta strand

76 – 82

7

Helix

83 – 85

3

Turn

90 – 93

4

Beta strand

94 – 100

7

Helix

102 – 108

7

Beta strand

114 – 117

4

Beta strand

131 – 139

9

Beta strand

241 – 245

5

Turn

246 – 248

3

Beta strand

249 – 254

6

Turn

255 – 258

4

Beta strand

259 – 263

5

Beta strand

312 – 317

6

Turn

318 – 320

3

Beta strand

321 – 326

6

Turn

327 – 330

4

Beta strand

331 – 334

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified December 13, 2001. Version 2. Checksum: 89A171CFC47B40E9	FASTA	757	86,114
	10 20 30 40 50 60 MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP 70 80 90 100 110 120 KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK 130 140 150 160 170 180 LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV DCRGLLENEG TVYEDSGPGR PLSCFMEEPA 190 200 210 220 230 240 PYTDSTGAAA GGGNCRFVES PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY 250 260 270 280 290 300 EQRTTVQGQV YFLHTQTGVS TWHDPRIPSP SGTIPGGDAA FLYEFLLQGH TSEPRDLNSV 310 320 330 340 350 360 NCDELGPLPP GWEVRSTVSG RIYFVDHNNR TTQFTDPRLH HIMNHQCQLK EPSQPLPLPS 370 380 390 400 410 420 EGSLEDEELP AQRYERDLVQ KLKVLRHELS LQQPQAGHCR IEVSREEIFE ESYRQIMKMR 430 440 450 460 470 480 PKDLKKRLMV KFRGEEGLDY GGVAREWLYL LCHEMLNPYY GLFQYSTDNI YMLQINPDSS 490 500 510 520 530 540 INPDHLSYFH FVGRIMGLAV FHGHYINGGF TVPFYKQLLG KPIQLSDLES VDPELHKSLV 550 560 570 580 590 600 WILENDITPV LDHTFCVEHN AFGRILQHEL KPNGRNVPVT EENKKEYVRL YVNWRFMRGI 610 620 630 640 650 660 EAQFLALQKG FNELIPQHLL KPFDQKELEL IIGGLDKIDL NDWKSNTRLK HCVADSNIVR 670 680 690 700 710 720 WFWQAVETFD EERRARLLQF VTGSTRVPLQ GFKALQGSTG AAGPRLFTIH LIDANTDNLP 730 740 750 KAHTCFNRID IPPYESYEKL YEKLLTAVEE TCGFAVE
	Isoform Short [UniParc]. Checksum: F106E00CA3C210AA	FASTA	731	83,440
	10 20 30 40 50 60 MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP 70 80 90 100 110 120 KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK 130 140 150 160 170 180 LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV DCRGLLENEG TVYEDSGPGR PLSCFMEEPA 190 200 210 220 230 240 PYTDSTGAAA GGGNCRFVES PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY 250 260 270 280 290 300 EQRTTVQGQV YFLHTQTGVS TWHDPRIPRD LNSVNCDELG PLPPGWEVRS TVSGRIYFVD 310 320 330 340 350 360 HNNRTTQFTD PRLHHIMNHQ CQLKEPSQPL PLPSEGSLED EELPAQRYER DLVQKLKVLR 370 380 390 400 410 420 HELSLQQPQA GHCRIEVSRE EIFEESYRQI MKMRPKDLKK RLMVKFRGEE GLDYGGVARE 430 440 450 460 470 480 WLYLLCHEML NPYYGLFQYS TDNIYMLQIN PDSSINPDHL SYFHFVGRIM GLAVFHGHYI 490 500 510 520 530 540 NGGFTVPFYK QLLGKPIQLS DLESVDPELH KSLVWILEND ITPVLDHTFC VEHNAFGRIL 550 560 570 580 590 600 QHELKPNGRN VPVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFDQK 610 620 630 640 650 660 ELELIIGGLD KIDLNDWKSN TRLKHCVADS NIVRWFWQAV ETFDEERRAR LLQFVTGSTR 670 680 690 700 710 720 VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF NRIDIPPYES YEKLYEKLLT 730 AVEETCGFAV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

RefSeq

NP_001186776.1. NM_001199847.1.
NP_065162.1. NM_020429.2.
NP_851994.1. NM_181349.2.

UniGene

Hs.189329.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9HCE7.

SMR

Q9HCE7. Positions 13-140, 228-751.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

121411. 319 interactions.

DIP

DIP-36709N.

IntAct

Q9HCE7. 13 interactions.

MINT

MINT-102628.

STRING

9606.ENSP00000354621.

PTM databases

PhosphoSite

Q9HCE7.

Polymorphism databases

DMDM

17865625.

Proteomic databases

PaxDb

Q9HCE7.

PRIDE

Q9HCE7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361125; ENSP00000354621; ENSG00000198742.
ENST00000361368; ENSP00000355326; ENSG00000198742.

GeneID

57154.

KEGG

hsa:57154.

UCSC

uc003upu.2. human.

Organism-specific databases

CTD

57154.

GeneCards

GC07M098627.

HGNC

HGNC:16807. SMURF1.

HPA

CAB013009.

MIM

605568. gene.

neXtProt

NX_Q9HCE7.

PharmGKB

PA134987175.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5021.

HOGENOM

HOG000208451.

HOVERGEN

HBG004134.

InParanoid

Q9HCE7.

KO

K04678.

OMA

GHTPQNR.

OrthoDB

EOG77Q4W4.

PhylomeDB

Q9HCE7.

TreeFam

TF323658.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

SignaLink

Q9HCE7.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9HCE7.

Bgee

Q9HCE7.

CleanEx

HS_SMURF1.

Genevestigator

Q9HCE7.

Family and domain databases

InterPro

IPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]

PIRSF

PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.

SMART

SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 2 hits.
[Graphical view]

SUPFAM

SSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 2 hits.
SSF56204. SSF56204. 1 hit.

PROSITE

PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SMURF1. human.

EvolutionaryTrace

Q9HCE7.

GeneWiki

SMURF1.

GenomeRNAi

57154.

NextBio

63133.

PRO

Q9HCE7.

SOURCE

Search...

Entry information

Entry name

SMUF1_HUMAN

Accession

Primary (citable) accession number: Q9HCE7
Secondary accession number(s): A4D279 , B7ZMB6, B9EGV3, O75853, Q547Q3, Q9UJT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	December 13, 2001
Last modified:	February 19, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.