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O95248 (MTMR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Myotubularin-related protein 5
Alternative name(s):
SET-binding factor 1
Short name=Sbf1
Gene names
Name:SBF1
Synonyms:MTMR5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1867 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable pseudophosphatase. Lacks several amino acids in the catalytic pocket which renders it catalytically inactive as a phosphatase. The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts. According to Ref.9, may function as a guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Ref.4 Ref.9

Subunit structure

Interacts with the SET domain of KMT2A/MLL1. Interacts with SUV39H1. Ref.4 Ref.6

Subcellular location

Nucleus Ref.4.

Involvement in disease

Charcot-Marie-Tooth disease 4B3 (CMT4B3) [MIM:615284]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.

Contains 1 dDENN domain.

Contains 1 DENN domain.

Contains 1 GRAM domain.

Contains 1 myotubularin phosphatase domain.

Contains 1 PH domain.

Contains 1 uDENN domain.

Sequence caution

The sequence AAC39675.1 differs from that shown. Reason: Frameshift at positions 1603, 1627, 1631 and 1864.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95248-1)

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 4 (identifier: O95248-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1275-1275: H → HVPSPRARVTTLSNPMAASASRRTAPR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18671867Myotubularin-related protein 5
PRO_0000094938

Regions

Domain18 – 8669UDENN
Domain128 – 310183DENN
Domain363 – 43270dDENN
Domain880 – 96889GRAM
Domain1120 – 1596477Myotubularin phosphatase
Domain1761 – 1865105PH

Amino acid modifications

Modified residue11371Phosphothreonine Ref.7

Natural variations

Alternative sequence12751H → HVPSPRARVTTLSNPMAASA SRRTAPR in isoform 4.
VSP_015158
Natural variant4171M → V in CMT4B3. Ref.12
VAR_070046
Natural variant15641T → A in CMT4B3. Ref.12
VAR_070047

Experimental info

Sequence conflict5961A → V in AAC39675. Ref.4
Sequence conflict11721P → R in AAC39675. Ref.4
Sequence conflict13761A → P in AAC78842. Ref.5
Sequence conflict15561Y → H in AAC78842. Ref.5

Sequences

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

Last modified September 11, 2007. Version 3.
Checksum: AAC0E04B27E5BE33

FASTA1,867208,315
        10         20         30         40         50         60 
MARLADYFVL VAFGPHPRGS GEGQGQILQR FPEKDWEDNP FPQGIELFCQ PSGWQLCPER 

        70         80         90        100        110        120 
NPPTFFVAVL TDINSERHYC ACLTFWEPAE PSQETTRVED ATEREEEGDE GGQTHLSPTA 

       130        140        150        160        170        180 
PAPSAQLFAP KTLVLVSRLD HTEVFRNSLG LIYAIHVEGL NVCLENVIGN LLTCTVPLAG 

       190        200        210        220        230        240 
GSQRTISLGA GDRQVIQTPL ADSLPVSRCS VALLFRQLGI TNVLSLFCAA LTEHKVLFLS 

       250        260        270        280        290        300 
RSYQRLADAC RGLLALLFPL RYSFTYVPIL PAQLLEVLST PTPFIIGVNA AFQAETQELL 

       310        320        330        340        350        360 
DVIVADLDGG TVTIPECVHI PPLPEPLQSQ THSVLSMVLD PELELADLAF PPPTTSTSSL 

       370        380        390        400        410        420 
KMQDKELRAV FLRLFAQLLQ GYRWCLHVVR IHPEPVIRFH KAAFLGQRGL VEDDFLMKVL 

       430        440        450        460        470        480 
EGMAFAGFVS ERGVPYRPTD LFDELVAHEV ARMRADENHP QRVLRHVQEL AEQLYKNENP 

       490        500        510        520        530        540 
YPAVAMHKVQ RPGESSHLRR VPRPFPRLDE GTVQWIVDQA AAKMQGAPPA VKAERRTTVP 

       550        560        570        580        590        600 
SGPPMTAILE RCSGLHVNSA RRLEVVRNCI SYVFEGKMLE AKKLLPAVLR ALKGRAARRC 

       610        620        630        640        650        660 
LAQELHLHVQ QNRAVLDHQQ FDFVVRMMNC CLQDCTSLDE HGIAAALLPL VTAFCRKLSP 

       670        680        690        700        710        720 
GVTQFAYSCV QEHVVWSTPQ FWEAMFYGDV QTHIRALYLE PTEDLAPAQE VGEAPSQEDE 

       730        740        750        760        770        780 
RSALDVASEQ RRLWPTLSRE KQQELVQKEE STVFSQAIHY ANRMSYLLLP LDSSKSRLLR 

       790        800        810        820        830        840 
ERAGLGDLES ASNSLVTNSM AGSVAESYDT ESGFEDAETC DVAGAVVRFI NRFVDKVCTE 

       850        860        870        880        890        900 
SGVTSDHLKG LHVMVPDIVQ MHIETLEAVQ RESRRLPPIQ KPKLLRPRLL PGEECVLDGL 

       910        920        930        940        950        960 
RVYLLPDGRE EGAGGSAGGP ALLPAEGAVF LTTYRVIFTG MPTDPLVGEQ VVVRSFPVAA 

       970        980        990       1000       1010       1020 
LTKEKRISVQ TPVDQLLQDG LQLRSCTFQL LKMAFDEEVG SDSAELFRKQ LHKLRYPPDI 

      1030       1040       1050       1060       1070       1080 
RATFAFTLGS AHTPGRPPRV TKDKGPSLRT LSRNLVKNAK KTIGRQHVTR KKYNPPSWEH 

      1090       1100       1110       1120       1130       1140 
RGQPPPEDQE DEISVSEELE PSTLTPSSAL KPSDRMTMSS LVERACCRDY QRLGLGTLSS 

      1150       1160       1170       1180       1190       1200 
SLSRAKSEPF RISPVNRMYA ICRSYPGLLI VPQSVQDNAL QRVSRCYRQN RFPVVCWRSG 

      1210       1220       1230       1240       1250       1260 
RSKAVLLRSG GLHGKGVVGL FKAQNAPSPG QSQADSSSLE QEKYLQAVVS SMPRYADASG 

      1270       1280       1290       1300       1310       1320 
RNTLSGFSSA HMGSHGKWGS VRTSGRSSGL GTDVGSRLAG RDALAPPQAN GGPPDPGFLR 

      1330       1340       1350       1360       1370       1380 
PQRAALYILG DKAQLKGVRS DPLQQWELVP IEVFEARQVK ASFKKLLKAC VPGCPAAEPS 

      1390       1400       1410       1420       1430       1440 
PASFLRSLED SEWLIQIHKL LQVSVLVVEL LDSGSSVLVG LEDGWDITTQ VVSLVQLLSD 

      1450       1460       1470       1480       1490       1500 
PFYRTLEGFR LLVEKEWLSF GHRFSHRGAH TLAGQSSGFT PVFLQFLDCV HQVHLQFPME 

      1510       1520       1530       1540       1550       1560 
FEFSQFYLKF LGYHHVSRRF RTFLLDSDYE RIELGLLYEE KGERRGQVPC RSVWEYVDRL 

      1570       1580       1590       1600       1610       1620 
SKRTPVFHNY MYAPEDAEVL RPYSNVSNLK VWDFYTEETL AEGPPYDWEL AQGPPEPPEE 

      1630       1640       1650       1660       1670       1680 
ERSDGGAPQS RRRVVWPCYD SCPRAQPDAI SRLLEELQRL ETELGQPAER WKDTWDRVKA 

      1690       1700       1710       1720       1730       1740 
AQRLEGRPDG RGTPSSLLVS TAPHHRRSLG VYLQEGPVGS TLSLSLDSDQ SSGSTTSGSR 

      1750       1760       1770       1780       1790       1800 
QAARRSTSTL YSQFQTAESE NRSYEGTLYK KGAFMKPWKA RWFVLDKTKH QLRYYDHRVD 

      1810       1820       1830       1840       1850       1860 
TECKGVIDLA EVEAVAPGTP TMGAPKTVDE KAFFDVKTTR RVYNFCAQDV PSAQQWVDRI 


QSCLSDA 

« Hide

Isoform 4 [UniParc].

Checksum: 36865405984F1AFA
Show »

FASTA1,893211,048

References

« Hide 'large scale' references
[1]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 938-1866 (ISOFORM 1).
Tissue: Muscle and Ovary.
[4]"Association of SET domain and myotubularin-related proteins modulates growth control."
Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.
Nat. Genet. 18:331-337(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-1867 (ISOFORM 1), FUNCTION, INTERACTION WITH KMT2A/MLL1, SUBCELLULAR LOCATION.
Tissue: Lymphoblast.
[5]"Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human."
Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., Mandel J.-L.
Hum. Mol. Genet. 7:1703-1712(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1362-1602.
[6]"Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9."
Firestein R., Cui X., Huie P., Cleary M.L.
Mol. Cell. Biol. 20:4900-4909(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUV39H1.
[7]"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 THR-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
[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]"SET binding factor 1 (SBF1) mutation causes Charcot-Marie-Tooth disease type 4B3."
Nakhro K., Park J.M., Hong Y.B., Park J.H., Nam S.H., Yoon B.R., Yoo J.H., Koo H., Jung S.C., Kim H.L., Kim J.Y., Choi K.G., Choi B.O., Chung K.W.
Neurology 81:165-173(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMT4B3 VAL-417 AND ALA-1564.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL096767 Genomic DNA. Translation: CAO03462.1.
CH471138 Genomic DNA. Translation: EAW73536.1.
BC009268 mRNA. Translation: AAH09268.2.
BC087612 mRNA. Translation: AAH87612.1.
U93181 mRNA. Translation: AAC39675.1. Frameshift.
AF072929 mRNA. Translation: AAC78842.1.
CCDSCCDS14091.2. [O95248-4]
RefSeqNP_002963.2. NM_002972.2. [O95248-4]
XP_005261992.1. XM_005261935.1. [O95248-1]
UniGeneHs.589924.

3D structure databases

ProteinModelPortalO95248.
SMRO95248. Positions 203-432, 1147-1251, 1318-1595, 1764-1865.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112212. 12 interactions.
IntActO95248. 5 interactions.
MINTMINT-7034529.
STRING9606.ENSP00000375097.

PTM databases

PhosphoSiteO95248.

Proteomic databases

MaxQBO95248.
PaxDbO95248.
PRIDEO95248.

Protocols and materials databases

DNASU6305.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380817; ENSP00000370196; ENSG00000100241. [O95248-4]
ENST00000390679; ENSP00000375097; ENSG00000100241. [O95248-1]
GeneID6305.
KEGGhsa:6305.
UCSCuc003blh.3. human. [O95248-4]
uc011arx.2. human. [O95248-1]

Organism-specific databases

CTD6305.
GeneCardsGC22M050885.
GeneReviewsSBF1.
HGNCHGNC:10542. SBF1.
MIM603560. gene.
615284. phenotype.
neXtProtNX_O95248.
Orphanet363981. Charcot-Marie-Tooth disease type 4B3.
PharmGKBPA34953.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315534.
HOVERGENHBG052527.
KOK18061.
OMASEWLIQI.
OrthoDBEOG747PKH.
PhylomeDBO95248.
TreeFamTF318583.

Gene expression databases

ArrayExpressO95248.
BgeeO95248.
CleanExHS_SBF1.
GenevestigatorO95248.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR005112. dDENN_dom.
IPR001194. DENN_dom.
IPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR022096. SBF2.
IPR005113. uDENN_dom.
[Graphical view]
PfamPF03455. dDENN. 1 hit.
PF02141. DENN. 1 hit.
PF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
PF00169. PH. 1 hit.
PF12335. SBF2. 1 hit.
PF03456. uDENN. 1 hit.
[Graphical view]
SMARTSM00801. dDENN. 1 hit.
SM00799. DENN. 1 hit.
SM00568. GRAM. 1 hit.
SM00233. PH. 1 hit.
SM00800. uDENN. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
PROSITEPS50947. DDENN. 1 hit.
PS50211. DENN. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS51339. PPASE_MYOTUBULARIN. 1 hit.
PS50946. UDENN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSBF1. human.
GeneWikiSBF1.
GenomeRNAi6305.
NextBio24479.
PROO95248.
SOURCESearch...

Entry information

Entry nameMTMR5_HUMAN
AccessionPrimary (citable) accession number: O95248
Secondary accession number(s): A6PVG9 expand/collapse secondary AC list , O60228, Q5JXD8, Q5PPM2, Q96GR9, Q9UGB8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 132 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

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 22

Human chromosome 22: entries, gene names and cross-references to MIM