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Q9HCE7 (SMUF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processUbl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionLigase
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP 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

Inferred from direct assay PubMed 11278251. Source: BHF-UCL

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_componentcytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from direct assay PubMed 12151385. Source: BHF-UCL

   Molecular_functionI-SMAD binding

Inferred from physical interaction PubMed 11278251PubMed 12151385. Source: BHF-UCL

R-SMAD binding

Inferred from physical interaction PubMed 11278251. Source: BHF-UCL

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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 757757E3 ubiquitin-protein ligase SMURF1
PRO_0000120326

Regions

Domain1 – 9999C2
Domain234 – 26734WW 1
Domain306 – 33934WW 2
Domain420 – 757338HECT

Sites

Active site7251Glycyl thioester intermediate

Amino acid modifications

Cross-link381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
Cross-link383Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Natural variations

Alternative sequence269 – 29426Missing in isoform Short.
VSP_006812
Natural variant4661S → Y.
Corresponds to variant rs13246077 [ dbSNP | Ensembl ].
VAR_052959

Experimental info

Mutagenesis281K → A: Fails to ubiquitinate RHOA; when associated with A-85. Ref.11
Mutagenesis851K → A: Fails to ubiquitinate RHOA; when associated with A-28. Ref.11
Mutagenesis3501K → R: Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381 and R-381. Ref.10
Mutagenesis3811K → 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
Mutagenesis3831K → 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
Mutagenesis7251C → A: Loss of enzyme activity, without abolishing FBXL15-mediated ubiquitination. Ref.9 Ref.10
Sequence conflict4471W → G in AAI44415. Ref.6
Sequence conflict697 – 6993Missing in AAI36805. Ref.6
Sequence conflict697 – 6993Missing in AAI44415. Ref.6

Secondary structure

.................................. 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: 89A171CFC47B40E9

FASTA75786,114
        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 

« Hide

Isoform Short [UniParc].

Checksum: F106E00CA3C210AA
Show »

FASTA73183,440

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001186776.1. NM_001199847.1.
NP_065162.1. NM_020429.2.
NP_851994.1. NM_181349.2.
UniGeneHs.189329.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LAZNMR-A235-267[»]
2LB0NMR-A235-267[»]
2LB1NMR-A305-339[»]
2LTXNMR-A306-340[»]
3PYCX-ray1.96A13-140[»]
ProteinModelPortalQ9HCE7.
SMRQ9HCE7. Positions 13-140, 228-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121411. 319 interactions.
DIPDIP-36709N.
IntActQ9HCE7. 13 interactions.
MINTMINT-102628.
STRING9606.ENSP00000354621.

PTM databases

PhosphoSiteQ9HCE7.

Polymorphism databases

DMDM17865625.

Proteomic databases

PaxDbQ9HCE7.
PRIDEQ9HCE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361125; ENSP00000354621; ENSG00000198742. [Q9HCE7-1]
ENST00000361368; ENSP00000355326; ENSG00000198742. [Q9HCE7-2]
GeneID57154.
KEGGhsa:57154.
UCSCuc003upt.3. human. [Q9HCE7-2]
uc003upu.2. human. [Q9HCE7-1]

Organism-specific databases

CTD57154.
GeneCardsGC07M098627.
HGNCHGNC:16807. SMURF1.
HPACAB013009.
MIM605568. gene.
neXtProtNX_Q9HCE7.
PharmGKBPA134987175.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000208451.
HOVERGENHBG004134.
InParanoidQ9HCE7.
KOK04678.
OMAGHTPQNR.
OrthoDBEOG77Q4W4.
PhylomeDBQ9HCE7.
TreeFamTF323658.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ9HCE7.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9HCE7.
BgeeQ9HCE7.
CleanExHS_SMURF1.
GenevestigatorQ9HCE7.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]
PIRSFPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMURF1. human.
EvolutionaryTraceQ9HCE7.
GeneWikiSMURF1.
GenomeRNAi57154.
NextBio63133.
PROQ9HCE7.
SOURCESearch...

Entry information

Entry nameSMUF1_HUMAN
AccessionPrimary (citable) accession number: Q9HCE7
Secondary accession number(s): A4D279 expand/collapse secondary AC list , B7ZMB6, B9EGV3, O75853, Q547Q3, Q9UJT8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM