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Q9ULT8 (HECD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase HECTD1

EC=6.3.2.-
Alternative name(s):
E3 ligase for inhibin receptor
EULIR
HECT domain-containing protein 1
Gene names
Name:HECTD1
Synonyms:KIAA1131
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2610 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with IGSF1. Ref.7

Sequence similarities

Belongs to the UPL family. K-HECT subfamily.

Contains 4 ANK repeats.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 1 MIB/HERC2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26102610E3 ubiquitin-protein ligase HECTD1
PRO_0000083945

Regions

Repeat395 – 42430ANK 1
Repeat426 – 45530ANK 2
Repeat459 – 49133ANK 3
Repeat579 – 61234ANK 4
Domain1266 – 133873MIB/HERC2
Domain2151 – 2610460HECT
Region2029 – 210375K-box
Compositional bias1350 – 1649300Ser-rich

Sites

Active site25791Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue6311Phosphoserine Ref.12
Modified residue14881Phosphoserine Ref.8

Natural variations

Natural variant6561Q → H.
Corresponds to variant rs11620816 [ dbSNP | Ensembl ].
VAR_059666
Natural variant20271L → P. Ref.3 Ref.4 Ref.5
Corresponds to variant rs1315794 [ dbSNP | Ensembl ].
VAR_067707

Experimental info

Sequence conflict5611K → Q in AAP13073. Ref.1
Sequence conflict6031L → I in AAP13073. Ref.1
Sequence conflict611 – 6133FLD → YKH in AAP13073. Ref.1
Sequence conflict6531K → Q in AAP13073. Ref.1
Sequence conflict8941E → K in AAP13073. Ref.1
Sequence conflict927 – 94418SMDLD…VERIN → VSIFRATKQKQNEVPKVILS in AAP13073. Ref.1
Sequence conflict9511S → T in AAP13073. Ref.1
Sequence conflict12811I → T in BAA86445. Ref.2

Secondary structure

................................. 2610
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ULT8 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 27E56401E07E158C

FASTA2,610289,384
        10         20         30         40         50         60 
MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI 

        70         80         90        100        110        120 
FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA 

       130        140        150        160        170        180 
EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ 

       190        200        210        220        230        240 
DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM 

       250        260        270        280        290        300 
AAAGGTVSGP SSACKPGRST TGAPSTTADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS 

       310        320        330        340        350        360 
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE 

       370        380        390        400        410        420 
RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA 

       430        440        450        460        470        480 
DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVAILQ 

       490        500        510        520        530        540 
SPGDWMCPVN KGDDKKKKDT NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI 

       550        560        570        580        590        600 
RKASLALIRK MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII 

       610        620        630        640        650        660 
RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE DAKELQQGKP 

       670        680        690        700        710        720 
YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG KLATMYSSGS PEGGSDSSES 

       730        740        750        760        770        780 
RSEFLEKLQR ARGQVKPSTS SQPILSAPGP TKLTVGNWSL TCLKEGEIAI HNSDGQQATI 

       790        800        810        820        830        840 
LKEDLPGFVF ESNRGTKHSF TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL 

       850        860        870        880        890        900 
YDDHFKAVES MPRGVVVTLR NIATQLESSW ELHTNRQCIE SENTWRDLMK TALENLIVLL 

       910        920        930        940        950        960 
KDENTISPYE MCSSGLVQAL LTVLNNSMDL DMKQDCSQLV ERINVFKTAF SENEDDESRP 

       970        980        990       1000       1010       1020 
AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR FRLERAPGET ALIDRTGRML 

      1030       1040       1050       1060       1070       1080 
KMEPLATVES LEQYLLKMVA KQWYDFDRSS FVFVRKLREG QNFIFRHQHD FDENGIIYWI 

      1090       1100       1110       1120       1130       1140 
GTNAKTAYEW VNPAAYGLVV VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID 

      1150       1160       1170       1180       1190       1200 
LGLWVIPSAY TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL 

      1210       1220       1230       1240       1250       1260 
DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK AAKEAEANLR 

      1270       1280       1290       1300       1310       1320 
RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGSPQGEGT VTGELHNGWI DVTWDAGGSN 

      1330       1340       1350       1360       1370       1380 
SYRMGAEGKF DLKLAPGYDP DTVASPKPVS STVSGTTQSW SSLVKNNCPD KTSAAAGSSS 

      1390       1400       1410       1420       1430       1440 
RKGSSSSVCS VASSSDISLG STKTERRSEI VMEHSIVSGA DVHEPIVVLS SAENVPQTEV 

      1450       1460       1470       1480       1490       1500 
GSSSSASTST LTAETGSENA ERKLGPDSSV RTPGESSAIS MGIVSVSSPD VSSVSELTNK 

      1510       1520       1530       1540       1550       1560 
EAASQRPLSS SASNRLSVSS LLAAGAPMSS SASVPNLSSR ETSSLESFVR RVANIARTNA 

      1570       1580       1590       1600       1610       1620 
TNNMNLSRSS SDNNTNTLGR NVMSTATSPL MGAQSFPNLT TPGTTSTVTM STSSVTSSSN 

      1630       1640       1650       1660       1670       1680 
VATATTVLSV GQSLSNTLTT SLTSTSSESD TGQEAEYSLY DFLDSCRAST LLAELDDDED 

      1690       1700       1710       1720       1730       1740 
LPEPDEEDDE NEDDNQEDQE YEEVMILRRP SLQRRAGSRS DVTHHAVTSQ LPQVPAGAGS 

      1750       1760       1770       1780       1790       1800 
RPIGEQEEEE YETKGGRRRT WDDDYVLKRQ FSALVPAFDP RPGRTNVQQT TDLEIPPPGT 

      1810       1820       1830       1840       1850       1860 
PHSELLEEVE CTPSPRLALT LKVTGLGTTR EVELPLTNFR STIFYYVQKL LQLSCNGNVK 

      1870       1880       1890       1900       1910       1920 
SDKLRRIWEP TYTIMYREMK DSDKEKENGK MGCWSIEHVE QYLGTDELPK NDLITYLQKN 

      1930       1940       1950       1960       1970       1980 
ADAAFLRHWK LTGTNKSIRK NRNCSQLIAA YKDFCEHGTK SGLNQGAIST LQSSDILNLT 

      1990       2000       2010       2020       2030       2040 
KEQPQAKAGN GQNSCGVEDV LQLLRILYIV ASDPYSRISQ EDGDEQLQFT FPPDEFTSKK 

      2050       2060       2070       2080       2090       2100 
ITTKILQQIE EPLALASGAL PDWCEQLTSK CPFLIPFETR QLYFTCTAFG ASRAIVWLQN 

      2110       2120       2130       2140       2150       2160 
RREATVERTR TTSSVRRDDP GEFRVGRLKH ERVKVPRGES LMEWAENVMQ IHADRKSVLE 

      2170       2180       2190       2200       2210       2220 
VEFLGEEGTG LGPTLEFYAL VAAEFQRTDL GAWLCDDNFP DDESRHVDLG GGLKPPGYYV 

      2230       2240       2250       2260       2270       2280 
QRSCGLFTAP FPQDSDELER ITKLFHFLGI FLAKCIQDNR LVDLPISKPF FKLMCMGDIK 

      2290       2300       2310       2320       2330       2340 
SNMSKLIYES RGDRDLHCTE SQSEASTEEG HDSLSVGSFE EDSKSEFILD PPKPKPPAWF 

      2350       2360       2370       2380       2390       2400 
NGILTWEDFE LVNPHRARFL KEIKDLAIKR RQILSNKGLS EDEKNTKLQE LVLKNPSGSG 

      2410       2420       2430       2440       2450       2460 
PPLSIEDLGL NFQFCPSSRI YGFTAVDLKP SGEDEMITMD NAEEYVDLMF DFCMHTGIQK 

      2470       2480       2490       2500       2510       2520 
QMEAFRDGFN KVFPMEKLSS FSHEEVQMIL CGNQSPSWAA EDIINYTEPK LGYTRDSPGF 

      2530       2540       2550       2560       2570       2580 
LRFVRVLCGM SSDERKAFLQ FTTGCSTLPP GGLANLHPRL TVVRKVDATD ASYPSVNTCV 

      2590       2600       2610 
HYLKLPEYSS EEIMRERLLA ATMEKGFHLN 

« Hide

References

« Hide 'large scale' references
[1]"EULIR is an E3 ubiquitin ligase for inhibin receptor."
Zhang H.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton 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], VARIANT PRO-2027.
[4]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2610, VARIANT PRO-2027.
Tissue: Brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1652-2610, VARIANT PRO-2027.
Tissue: Testis.
[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] OF 2091-2610.
Tissue: Muscle and Urinary bladder.
[7]"Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs."
Nakayama M., Kikuno R., Ohara O.
Genome Res. 12:1773-1784(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGSF1.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of MIB-HERC2 domain in HECT domain containing protein 1."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1266-1338.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY254380 mRNA. Translation: AAP13073.1.
AL121808 Genomic DNA. No translation available.
AL136418 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65950.1.
CH471078 Genomic DNA. Translation: EAW65952.1.
AB032957 mRNA. Translation: BAA86445.2.
AL110222 mRNA. Translation: CAB53681.1.
BC011658 mRNA. Translation: AAH11658.2.
BC063686 mRNA. Translation: AAH63686.1.
PIRT14761.
RefSeqNP_056197.3. NM_015382.3.
XP_005267559.2. XM_005267502.2.
UniGeneHs.708017.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK3NMR-A1266-1338[»]
2LC3NMR-A1879-1966[»]
3DKMX-ray1.60A1271-1341[»]
ProteinModelPortalQ9ULT8.
SMRQ9ULT8. Positions 1266-1338, 1879-1966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117359. 14 interactions.
DIPDIP-31669N.
IntActQ9ULT8. 8 interactions.
MINTMINT-6783566.
STRING9606.ENSP00000382269.

PTM databases

PhosphoSiteQ9ULT8.

Polymorphism databases

DMDM313104227.

Proteomic databases

MaxQBQ9ULT8.
PaxDbQ9ULT8.
PeptideAtlasQ9ULT8.
PRIDEQ9ULT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399332; ENSP00000382269; ENSG00000092148.
ENST00000553700; ENSP00000450697; ENSG00000092148.
GeneID25831.
KEGGhsa:25831.
UCSCuc001wrc.1. human.

Organism-specific databases

CTD25831.
GeneCardsGC14M031569.
HGNCHGNC:20157. HECTD1.
HPAHPA002929.
neXtProtNX_Q9ULT8.
PharmGKBPA134989284.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000018061.
HOVERGENHBG067533.
InParanoidQ9ULT8.
KOK12231.
OMATKHSFTA.
PhylomeDBQ9ULT8.
TreeFamTF323674.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9ULT8.
BgeeQ9ULT8.
CleanExHS_HECTD1.
GenevestigatorQ9ULT8.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.60.120.260. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR012919. Sad1_UNC_C.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
SSF48403. SSF48403. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56204. SSF56204. 4 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHECTD1. human.
EvolutionaryTraceQ9ULT8.
GenomeRNAi25831.
NextBio47125.
PROQ9ULT8.

Entry information

Entry nameHECD1_HUMAN
AccessionPrimary (citable) accession number: Q9ULT8
Secondary accession number(s): D3DS86 expand/collapse secondary AC list , Q6P445, Q86VJ1, Q96F34, Q9UFZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 130 of the entry and version 3 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

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 14

Human chromosome 14: entries, gene names and cross-references to MIM