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A6NHR9 (SMHD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes flexible hinge domain-containing protein 1
Alternative name(s):
SMC hinge domain-containing protein 1
Gene names
Name:SMCHD1
Synonyms:KIAA0650
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2005 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for maintenance of X inactivation in females and hypermethylation of CpG islands associated with inactive X. Involved in a pathway that mediates the methylation of a subset of CpG islands slowly and requires the de novo methyltransferase DNMT3B By similarity. Required for DUX4 silencing in somatic cells. Ref.10

Subcellular location

Chromosome By similarity. Note: Localizes to Barr body By similarity.

Post-translational modification

Sumoylated with SUMO1 By similarity.

Involvement in disease

Facioscapulohumeral muscular dystrophy 2 (FSHD2) [MIM:158901]: A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles.
Note: The disease is caused by mutations affecting the gene represented in this entry. SMCHD1 mutations lead to DUX4 expression in somatic tissues, including muscle cells, when an haplotype on chromosome 4 is permissive for DUX4 expression. Ectopic expression of DUX4 in skeletal muscle activates the expression of stem cell and germline genes, and, when overexpressed in somatic cells, DUX4 can ultimately lead to cell death. Ref.10

Sequence caution

The sequence BAB15202.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BC035774 differs from that shown. Reason: Frameshift at position 1730.

The sequence CAH10538.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A6NHR9-1)

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 2 (identifier: A6NHR9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1907-1917: DLLQQYRSAVC → VHACVPSYSGG
     1918-2005: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: A6NHR9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1065: Missing.
     1826-1827: VF → GC
     1828-2005: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 20052004Structural maintenance of chromosomes flexible hinge domain-containing protein 1
PRO_0000332144

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.7
Modified residue13491N6-acetyllysine Ref.8
Modified residue18021N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 10651065Missing in isoform 3.
VSP_033344
Alternative sequence1826 – 18272VF → GC in isoform 3.
VSP_033345
Alternative sequence1828 – 2005178Missing in isoform 3.
VSP_033346
Alternative sequence1907 – 191711DLLQQYRSAVC → VHACVPSYSGG in isoform 2.
VSP_033347
Alternative sequence1918 – 200588Missing in isoform 2.
VSP_033348
Natural variant3531Y → C in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069067
Natural variant4791R → P in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069068
Natural variant4921C → R in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069069
Natural variant6901P → S in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069070
Natural variant7081V → I.
Corresponds to variant rs2276092 [ dbSNP | Ensembl ].
VAR_042959
Natural variant8681S → N in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069071
Natural variant8791K → N.
Corresponds to variant rs633422 [ dbSNP | Ensembl ].
VAR_042960
Natural variant9601I → V.
Corresponds to variant rs9961682 [ dbSNP | Ensembl ].
VAR_051365
Natural variant15541F → S in FSHD2; decreased protein level in fibroblasts as compared to wild type protein. Ref.10
VAR_069072

Experimental info

Sequence conflict12781Q → E in CAB45732. Ref.3
Sequence conflict13841G → E in CAH10538. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: B662C681424241B7

FASTA2,005226,374
        10         20         30         40         50         60 
MAAADGGGPG GASVGTEEDG GGVGHRTVYL FDRREKESEL GDRPLQVGER SDYAGFRACV 

        70         80         90        100        110        120 
CQTLGISPEE KFVITTTSRK EITCDNFDET VKDGVTLYLL QSVNQLLLTA TKERIDFLPH 

       130        140        150        160        170        180 
YDTLVKSGMY EYYASEGQNP LPFALAELID NSLSATSRNI GVRRIQIKLL FDETQGKPAV 

       190        200        210        220        230        240 
AVIDNGRGMT SKQLNNWAVY RLSKFTRQGD FESDHSGYVR PVPVPRSLNS DISYFGVGGK 

       250        260        270        280        290        300 
QAVFFVGQSA RMISKPADSQ DVHELVLSKE DFEKKEKNKE AIYSGYIRNR KPSDSVHITN 

       310        320        330        340        350        360 
DDERFLHHLI IEEKEKDSFT AVVITGVQPE HIQYLKNYFH LWTRQLAHIY HYYIHGPKGN 

       370        380        390        400        410        420 
EIRTSKEVEP FNNIDIEISM FEKGKVPKIV NLREIQDDMQ TLYVNTAADS FEFKAHVEGD 

       430        440        450        460        470        480 
GVVEGIIRYH PFLYDRETYP DDPCFPSKLK DEDDEDDCFI LEKAARGKRP IFECFWNGRL 

       490        500        510        520        530        540 
IPYTSVEDFD WCTPPKKRGL APIECYNRIS GALFTNDKFQ VSTNKLTFMD LELKLKDKNT 

       550        560        570        580        590        600 
LFTRILNGQE QRMKIDREFA LWLKDCHEKY DKQIKFTLFK GVITRPDLPS KKQGPWATYA 

       610        620        630        640        650        660 
AIEWDGKIYK AGQLVKTIKT LPLFYGSIVR FFLYGDHDGE VYATGGEVQI AMEPQALYDE 

       670        680        690        700        710        720 
VRTVPIAKLD RTVAEKAVKK YVEDEMARLP DRLSVTWPEG DELLPNEVRP AGTPIGALRI 

       730        740        750        760        770        780 
EILNKKGEAM QKLPGTSHGG SKKLLVELKV ILHSSSGNKE IISHISQHGG KWPYWFKKME 

       790        800        810        820        830        840 
NIQKLGNYTL KLQVVLNESN ADTYAGRPLP SKAIKFSVKE GKPEKFSFGL LDLPFRVGVP 

       850        860        870        880        890        900 
FNIPLEFQDE FGHTSQLVTD IQPVLEASGL SLHYEEITKG PNCVIRGVTA KGPVNSCQGK 

       910        920        930        940        950        960 
NYNLKVTLPG LKEDSQILKI RLLPGHPRRL KVKPDSEILV IENGTAFPFQ VEVLDESDNI 

       970        980        990       1000       1010       1020 
TAQPKLIVHC KFSGAPNLPV YVVDCSSSGT SILTGSAIQV QNIKKDQTLK ARIEIPSCKD 

      1030       1040       1050       1060       1070       1080 
VAPVEKTIKL LPSSHVARLQ IFSVEGQKAI QIKHQDEVNW IAGDIMHNLI FQMYDEGERE 

      1090       1100       1110       1120       1130       1140 
INITSALAEK IKVNWTPEIN KEHLLQGLLP DVQVPTSVKD MRYCQVSFQD DHVSLESAFT 

      1150       1160       1170       1180       1190       1200 
VRPLPDEPKH LKCEMKGGKT VQMGQELQGE VVIIITDQYG NQIQAFSPSS LSSLSIAGVG 

      1210       1220       1230       1240       1250       1260 
LDSSNLKTTF QENTQSISVR GIKFIPGPPG NKDLCFTWRE FSDFIRVQLI SGPPAKLLLI 

      1270       1280       1290       1300       1310       1320 
DWPELKESIP VINGRDLQNP IIVQLCDQWD NPAPVQHVKI SLTKASNLKL MPSNQQHKTD 

      1330       1340       1350       1360       1370       1380 
EKGRANLGVF SVFAPRGEHT LQVKAIYNKS IIEGPIIKLM ILPDPEKPVR LNVKYDKDAS 

      1390       1400       1410       1420       1430       1440 
FLAGGLFTDF MISVISEDDS IIKNINPARI SMKMWKLSTS GNRPPANAET FSCNKIKDND 

      1450       1460       1470       1480       1490       1500 
KEDGCFYFRD KVIPNKVGTY CIQFGFMMDK TNILNSEQVI VEVLPNQPVK LVPKIKPPTP 

      1510       1520       1530       1540       1550       1560 
AVSNVRSVAS RTLVRDLHLS ITDDYDNHTG IDLVGTIIAT IKGSNEEDTD TPLFIGKVRT 

      1570       1580       1590       1600       1610       1620 
LEFPFVNGSA EIMSLVLAES SPGRDSTEYF IVFEPRLPLL SRTLEPYILP FMFYNDVKKQ 

      1630       1640       1650       1660       1670       1680 
QQMAALTKEK DQLSQSIVMY KSLFEASQQL LNEMKCQVEE ARLKEAQLRN ELKIHNIDIP 

      1690       1700       1710       1720       1730       1740 
TTQQVPHIEA LLKRKLSEQE ELKKKPRRSC TLPNYTKGSG DVLGKIAHLA QIEDDRAAMV 

      1750       1760       1770       1780       1790       1800 
ISWHLASDMD CVVTLTTDAA RRIYDETQGR QQVLPLDSIY KKTLPDWKRS LPHFRNGKLY 

      1810       1820       1830       1840       1850       1860 
FKPIGDPVFA RDLLTFPDNV EHCETVFGML LGDTIILDNL DAANHYRKEV VKITHCPTLL 

      1870       1880       1890       1900       1910       1920 
TRDGDRIRSN GKFGGLQNKA PPMDKLRGMV FGAPVPKQCL ILGEQIDLLQ QYRSAVCKLD 

      1930       1940       1950       1960       1970       1980 
SVNKDLNSQL EYLRTPDMRK KKQELDEHEK NLKLIEEKLG MTPIRKCNDS LRHSPKVETT 

      1990       2000 
DCPVPPKRMR REATRQNRII TKTDV 

« Hide

Isoform 2 [UniParc].

Checksum: 1E16E802BA6F7FD7
Show »

FASTA1,917215,745
Isoform 3 [UniParc].

Checksum: 3FD613313D84C89A
Show »

FASTA76285,965

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-2005 (ISOFORM 1).
Tissue: Trachea.
[2]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 530-2005 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1278-2005 (ISOFORM 1).
Tissue: Testis.
[4]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1158-2005 (ISOFORM 1).
Tissue: Brain.
[5]"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 1699-2005 (ISOFORM 1).
Tissue: Eye.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-26; 280-288; 663-671; 826-836; 1208-1220; 1267-1275 AND 1495-1506, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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].
[10]"Digenic inheritance of an SMCHD1 mutation and an FSHD-permissive D4Z4 allele causes facioscapulohumeral muscular dystrophy type 2."
Lemmers R.J., Tawil R., Petek L.M., Balog J., Block G.J., Santen G.W., Amell A.M., van der Vliet P.J., Almomani R., Straasheijm K.R., Krom Y.D., Klooster R., Sun Y., den Dunnen J.T., Helmer Q., Donlin-Smith C.M., Padberg G.W., van Engelen B.G. expand/collapse author list , de Greef J.C., Aartsma-Rus A.M., Frants R.R., de Visser M., Desnuelle C., Sacconi S., Filippova G.N., Bakker B., Bamshad M.J., Tapscott S.J., Miller D.G., van der Maarel S.M.
Nat. Genet. 44:1370-1374(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FSHD2 CYS-353; PRO-479; ARG-492; SER-690; ASN-868 AND SER-1554, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK025646 mRNA. Translation: BAB15202.1. Different initiation.
AK126324 mRNA. Translation: BAC86525.1.
AP001011 Genomic DNA. No translation available.
AP005061 Genomic DNA. No translation available.
AL080138 mRNA. Translation: CAB45732.1.
CR627458 mRNA. Translation: CAH10538.1. Different initiation.
AB014550 mRNA. Translation: BAA31625.1.
BC035774 mRNA. No translation available.
CCDSCCDS45822.1. [A6NHR9-1]
PIRT00372.
RefSeqNP_056110.2. NM_015295.2. [A6NHR9-1]
UniGeneHs.8118.

3D structure databases

ProteinModelPortalA6NHR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116929. 12 interactions.
IntActA6NHR9. 7 interactions.
MINTMINT-5010096.
STRING9606.ENSP00000352119.

PTM databases

PhosphoSiteA6NHR9.

Proteomic databases

MaxQBA6NHR9.
PaxDbA6NHR9.
PeptideAtlasQ6AHX6.
PRIDEA6NHR9.

Protocols and materials databases

DNASU23347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261598; ENSP00000261598; ENSG00000101596. [A6NHR9-2]
ENST00000320876; ENSP00000326603; ENSG00000101596. [A6NHR9-1]
GeneID23347.
KEGGhsa:23347.
UCSCuc002klm.4. human. [A6NHR9-1]

Organism-specific databases

CTD23347.
GeneCardsGC18P002649.
H-InvDBHIX0014298.
HGNCHGNC:29090. SMCHD1.
HPAHPA039441.
MIM158901. phenotype.
614982. gene.
neXtProtNX_A6NHR9.
Orphanet269. Facioscapulohumeral dystrophy.
PharmGKBPA128395776.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73201.
HOGENOMHOG000007754.
HOVERGENHBG108493.
InParanoidA6NHR9.
OMATQQVPHI.
OrthoDBEOG72JWF8.
PhylomeDBA6NHR9.
TreeFamTF329426.

Gene expression databases

ArrayExpressA6NHR9.
BgeeA6NHR9.
CleanExHS_SMCHD1.
GenevestigatorA6NHR9.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
InterProIPR003594. HATPase_ATP-bd.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
[Graphical view]
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF55874. SSF55874. 1 hit.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSMCHD1. human.
GenomeRNAi23347.
NextBio45315.
PROA6NHR9.
SOURCESearch...

Entry information

Entry nameSMHD1_HUMAN
AccessionPrimary (citable) accession number: A6NHR9
Secondary accession number(s): O75141 expand/collapse secondary AC list , Q6AHX6, Q6ZTQ8, Q9H6Q2, Q9UG39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 67 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

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 18

Human chromosome 18: entries, gene names and cross-references to MIM