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O95278 (EPM2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laforin

EC=3.1.3.-
EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Glucan phosphatase
Lafora PTPase
Short name=LAFPTPase
Gene names
Name:EPM2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1. Ref.1 Ref.2 Ref.10 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with itself; however no biological function has been identified for the dimer. Interacts with PPP1R3B, PPP1R3C, HIRIP5, and EPM2AIP1. Binds glycogen and Lafora bodies. Interacts with NHLRC1/malin (via the NHL repeats). Forms a complex with NHLRC1/malin and HSP70. Interacts with PPP1R3D; in the presence of NHLC1/malin the interaction leads to ubiquitination and autophagic degradation of PPP1R3D. Interacts (via the phosphatase domain) with MAPT/Tau; the interaction dephosphorylates MAPT. Isoform 2 does not bind glycogen. Isoform 1 and isoform 2 interact to form a heterodimeric complex inactive as phosphatase in vitro. Active phosphatase isoform 7 interacts with isoform 1 or isoform 2 to form a heterodimeric complex inactive as phosphatase in vitro. Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.27

Subcellular location

Cytoplasm Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20. Note: Under glycogenolytic conditions localizes to the nucleus. Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20

Isoform 1: Endoplasmic reticulum. Cell membrane. Note: Primarily associated with polyribosomes at the endoplasmic reticulum, also found at the plasma membrane. Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20

Isoform 2: Endoplasmic reticulum. Cell membrane. Nucleus Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20. Note: Also found in the nucleus. Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20

Isoform 4: Cytoplasm Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20. Nucleus Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20.

Isoform 5: Cytoplasm Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20. Nucleus Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20.

Isoform 7: Cytoplasm Ref.2 Ref.10 Ref.11 Ref.12 Ref.19 Ref.20.

Tissue specificity

Expressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta. Ref.1

Post-translational modification

Polyubiquitinated by NHLRC1/malin.

Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2.

Involvement in disease

Epilepsy, progressive myoclonic 2 (EPM2) [MIM:254780]: An autosomal recessive and severe form of adolescent-onset progressive epilepsy. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. EPM2 occurs worldwide, but it is particularly common in the mediterranean countries of southern Europe and northern Africa, in southern India and in the Middle East. At the cellular level, it is characterized by accumulation of starch-like polyglucosans called Lafora bodies (LBs) that are most abundant in organs with the highest glucose metabolism: brain, heart, liver and skeletal muscle. Among other conditions involving polyglucosans, EPM2 is unique in that the inclusions are in neuronal dendrites but not axons and the forming polyglucosan fibrils are associated with the endoplasmic reticulum.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.29 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence BAG51107.1 differs from that shown. Reason: Frameshift at position 223.

Ontologies

Keywords
   Biological processAutophagy
Carbohydrate metabolism
Glycogen metabolism
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen biosynthetic process

Traceable author statement. Source: Reactome

glycogen metabolic process

Non-traceable author statement Ref.9. Source: UniProtKB

habituation

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.2Ref.14. Source: GOC

protein dephosphorylation

Inferred from direct assay Ref.2Ref.14. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.19. Source: UniProtKB

cytosol

Inferred from direct assay Ref.14. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

polysome

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functioncarbohydrate phosphatase activity

Inferred from experiment. Source: Reactome

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.14. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.2Ref.14. Source: UniProtKB

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1R3CQ9UQK15EBI-2506661,EBI-2506727

Alternative products

This entry describes 9 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: O95278-1)

Also known as: A; LDH1; Laf331;

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: O95278-2)

Also known as: B; C-terISO; Laf317;

The sequence of this isoform differs from the canonical sequence as follows:
     310-320: LARAQEDFFQK → ASQDTFPL
     321-331: Missing.
Note: Produced by alternative splicing.
Isoform 3 (identifier: O95278-3)

The sequence of this isoform differs from the canonical sequence as follows:
     75-100: GAEPGRVDTFWYKFLKREPGGELSWE → LVKIGSAPETRSKIFPRFTIRRRLSR
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 4 (identifier: O95278-4)

Also known as: Laf152;

The sequence of this isoform differs from the canonical sequence as follows:
     102-199: NGPHHDRCCT...MNFQTEWDIV → IASRRLPPAQ...VPAHSPGDLG
     200-331: Missing.
Note: Produced by alternative splicing.
Isoform 5 (identifier: O95278-5)

Also known as: Laf224;

The sequence of this isoform differs from the canonical sequence as follows:
     160-293: Missing.
     294-331: YFLMAKRPAV...GKVRSSVCSL → PSTDAAPGGV...PHGQEAGCLH
Note: Produced by alternative splicing.
Isoform 6 (identifier: O95278-6)

Also known as: Laf88;

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.
Note: Produced by alternative initiation at Met-244 of isoform 1. Transcript amplified but protein not detected.
Isoform 7 (identifier: O95278-7)

Also known as: Laf177;

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: MRFRFGVVVP...AGHQAMHYSR → MIFNK
Note: Produced by alternative splicing. Active phosphatase.
Isoform 8 (identifier: O95278-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 9 (identifier: B3EWF7-1)

Also known as: POCR;

The sequence of this isoform can be found in the external entry B3EWF7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by alternative initiation. Arises due to the use of an alternative initiation codon in exon 1 out of frame with isoform 1 and results in a completely different isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Laforin
PRO_0000094838

Regions

Domain1 – 124124CBM20
Domain243 – 31169Tyrosine-protein phosphatase

Sites

Active site2661Phosphocysteine intermediate Ref.12
Site3291Required for homodimerization

Amino acid modifications

Modified residue251Phosphoserine; by AMPK Ref.25

Natural variations

Alternative sequence1 – 243243Missing in isoform 6.
VSP_042494
Alternative sequence1 – 159159MRFRF…MHYSR → MIFNK in isoform 7.
VSP_042495
Alternative sequence1 – 138138Missing in isoform 8.
VSP_042493
Alternative sequence75 – 10026GAEPG…ELSWE → LVKIGSAPETRSKIFPRFTI RRRLSR in isoform 3.
VSP_011014
Alternative sequence102 – 19998NGPHH…EWDIV → IASRRLPPAQSGSSGPHPQP GPRPRAGPAGPGGARPGLFA RVPAHSPGDLG in isoform 4.
VSP_011015
Alternative sequence160 – 293134Missing in isoform 5.
VSP_042496
Alternative sequence200 – 331132Missing in isoform 4.
VSP_011016
Alternative sequence294 – 33138YFLMA…SVCSL → PSTDAAPGGVPAACAAGEGT HRVRALQRWGGPLHRGCLRL APVCDGLESEEGAVFPHGQE AGCLH in isoform 5.
VSP_042497
Alternative sequence310 – 32011LARAQEDFFQK → ASQDTFPL in isoform 2.
VSP_011017
Alternative sequence321 – 33111Missing in isoform 2.
VSP_011018
Natural variant251S → P in EPM2; atypical form; does not affect glycogen binding. Ref.16 Ref.31
VAR_019465
Natural variant281E → K in EPM2; does not affect glycogen binding. Ref.16
VAR_019466
Natural variant321W → G in EPM2; affects phosphatase activity; abolishes glycogen binding; reduced binding to Lafora bodies; disrupts the interaction with PPP1R3C; significant protein amount targeted to the nucleus. Ref.12 Ref.15 Ref.16 Ref.31
VAR_019467
Natural variant461A → P Does not affect glycogen binding. Ref.16 Ref.30 Ref.35
VAR_019468
Natural variant841F → L in EPM2; affects phosphatase activity and glycogen binding; disrupts the interaction with PPP1R3C. Ref.15 Ref.29
VAR_019469
Natural variant881F → L in EPM2; does not affect glycogen binding. Ref.16
VAR_019470
Natural variant911R → P in EPM2; atypical form; learning difficuties with childhood-onset. Ref.33 Ref.34
VAR_019471
Natural variant1081R → C in EPM2; loss of phosphatase activity; reduced self-interaction capacity; disrupts the interaction with PPP1R3C. Ref.1 Ref.15 Ref.31
VAR_019472
Natural variant1141E → D. Ref.1
VAR_019473
Natural variant1401K → N in EPM2. Ref.36
VAR_046383
Natural variant1481N → Y in EPM2. Ref.36
VAR_046384
Natural variant1711R → H in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding. Ref.2 Ref.9 Ref.31 Ref.34
VAR_019474
Natural variant1871T → A in EPM2; abolishes interaction with NHLRC1. Ref.32
VAR_019475
Natural variant1941T → I in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; reduced self-interaction capacity; abolishes interaction with NHLRC1, PPP1R3C and PRKAA2; no effect on phosphorylation of protein. Ref.9 Ref.15 Ref.31
VAR_019476
Natural variant2101E → K in EPM2. Ref.36
VAR_046385
Natural variant2401G → S in EPM2; very slight loss of phosphatase activity; does not affect glycogen binding; disrupts the interaction with PPP1R3C. Ref.15 Ref.29
VAR_019477
Natural variant2791G → S in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. Ref.1 Ref.9 Ref.15 Ref.31 Ref.34
VAR_019478
Natural variant2931Q → L in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. Ref.1 Ref.2 Ref.15 Ref.31
VAR_019479
Natural variant2941Y → N in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. Ref.9 Ref.15 Ref.31
VAR_019480
Natural variant3011P → L in EPM2; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. Ref.15 Ref.29
VAR_019481
Natural variant3101L → W in EPM2; alters the subcellular localization of isoform 1; does not affect homodimerization of isoform 1 but prevents heterodimerization of isoform 1 and isoform 2. Ref.36
VAR_046386

Experimental info

Mutagenesis251S → A: Partial loss of phosphatase activity. Abolishes homodimerization. Abolishes interaction with NHLRC1, PPP1R3C and PRKAA2. Does not affect glycogen binding. Reduces stability of the protein. Ref.25
Mutagenesis251S → D: Partial loss of phosphatase activity. Increases interaction with NHLRC1. Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. Does not affect binding to carbohydrate. Does not affect homodimerization. Ref.25
Mutagenesis871K → A: Partial loss of phosphatase activity. Abolishes glycogen binding. Ref.12
Mutagenesis109 – 1102CC → SS: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.
Mutagenesis1231C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. Ref.28
Mutagenesis1681S → A or D: Abolishes interaction with NHLRC1. Ref.25
Mutagenesis1691C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. Ref.28
Mutagenesis1871T → D: Abolishes interaction with NHLRC1. Ref.25
Mutagenesis1941T → D: Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. Ref.25
Mutagenesis2051C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. Ref.28
Mutagenesis2351D → A: Loss of phosphatase activity. Does not affect glycogen binding. Ref.15
Mutagenesis2501C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. Ref.28
Mutagenesis2661C → S: Complete loss of phosphatase activity. Does not affect glycogen binding. Does not affect self-interaction. Increases the interaction with PPP1R3C. Ref.12 Ref.15 Ref.28
Mutagenesis329 – 3313Missing: Fails to homodimerize. Does not affect carbohydrate binding or phosphatase activity. Ref.28
Mutagenesis3291C → S: Fails to homodimerize. Does not affect carbohydrate binding, interaction with NHLRC1, phosphatase activity, or ubiquitination by NHLRC1. Ref.28
Sequence conflict1931Q → K in AAH70047. Ref.8
Sequence conflict2481A → P in AAO15523. Ref.4
Sequence conflict2581K → E in BAG61454. Ref.5
Sequence conflict2941Y → H in BAG61454. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (LDH1) (Laf331) [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: DD79F917262AB458

FASTA33137,158
        10         20         30         40         50         60 
MRFRFGVVVP PAVAGARPEL LVVGSRPELG RWEPRGAVRL RPAGTAAGDG ALALQEPGLW 

        70         80         90        100        110        120 
LGEVELAAEE AAQDGAEPGR VDTFWYKFLK REPGGELSWE GNGPHHDRCC TYNENNLVDG 

       130        140        150        160        170        180 
VYCLPIGHWI EATGHTNEMK HTTDFYFNIA GHQAMHYSRI LPNIWLGSCP RQVEHVTIKL 

       190        200        210        220        230        240 
KHELGITAVM NFQTEWDIVQ NSSGCNRYPE PMTPDTMIKL YREEGLAYIW MPTPDMSTEG 

       250        260        270        280        290        300 
RVQMLPQAVC LLHALLEKGH IVYVHCNAGV GRSTAAVCGW LQYVMGWNLR KVQYFLMAKR 

       310        320        330 
PAVYIDEEAL ARAQEDFFQK FGKVRSSVCS L 

« Hide

Isoform 2 (B) (C-terISO) (Laf317) [UniParc].

Checksum: 5646A039398AC24D
Show »

FASTA31735,519
Isoform 3 [UniParc].

Checksum: 65E7EC44AE20B083
Show »

FASTA33137,188
Isoform 4 (Laf152) [UniParc].

Checksum: 60CD9293F2267EC4
Show »

FASTA15215,804
Isoform 5 (Laf224) [UniParc].

Checksum: 66ECE43870086B2A
Show »

FASTA22424,134
Isoform 6 (Laf88) [UniParc].

Checksum: D28FAB18CC285D07
Show »

FASTA889,933
Isoform 7 (Laf177) [UniParc].

Checksum: 5AE29B26B72E7BF7
Show »

FASTA17720,256
Isoform 8 [UniParc].

Checksum: 3DC9436A9885B915
Show »

FASTA19322,160
Isoform 9 (POCR) [UniParc].

See B3EWF7.

References

« Hide 'large scale' references
[1]"Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy."
Minassian B.A., Lee J.R., Herbrick J.-A., Huizenga J., Soder S., Mungall A.J., Dunham I., Gardner R., Fong C.G., Carpenter S., Jardim L., Satishchandra P., Andermann E., Snead O.C. III, Lopes-Cendes I., Tsui L.-C., Delgado-Escueta A.V., Rouleau G.A., Scherer S.W.
Nat. Genet. 20:171-174(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, PROBABLE FUNCTION, TISSUE SPECIFICITY, VARIANTS EPM2 CYS-108; SER-279 AND LEU-293, VARIANT ASP-114.
[2]"Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes."
Ganesh S., Agarwala K.L., Ueda K., Akagi T., Shoda K., Usui T., Hashikawa T., Osada H., Delgado-Escueta A.V., Yamakawa K.
Hum. Mol. Genet. 9:2251-2261(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTIONAL CHARACTERIZATION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS EPM2 HIS-171 AND LEU-293.
Tissue: Fetal brain.
[3]Lee J.R., Scherer S.W.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Cloning of differentially spliced transcripts of the EPM2A gene."
Ganesh S., Yamakawa K.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [MRNA] OF 25-331 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 75-331 (ISOFORM 3).
Tissue: Cerebellum and Fetal brain.
[5]"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] (ISOFORMS 7 AND 8).
Tissue: Fetal brain and Teratocarcinoma.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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 1 AND 6).
Tissue: Hypothalamus and Kidney.
[9]"A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)."
Serratosa J.M., Gomez-Garre P., Gallardo M.E., Anta B., de Bernabe D.B., Lindhout D., Augustijn P.B., Tassinari C.A., Malafosse R.M., Topcu M., Grid D., Dravet C., Berkovic S.F., de Cordoba S.R.
Hum. Mol. Genet. 8:345-352(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-331 (ISOFORMS 1 AND 2), VARIANTS EPM2 HIS-171; ILE-194; SER-279 AND ASN-294.
[10]"Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase."
Minassian B.A., Andrade D.M., Ianzano L., Young E.J., Chan E., Ackerley C.A., Scherer S.W.
Ann. Neurol. 49:271-275(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Alternative splicing modulates subcellular localization of laforin."
Ganesh S., Suzuki T., Yamakawa K.
Biochem. Biophys. Res. Commun. 291:1134-1137(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORM 2).
[12]"A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen."
Wang J., Stuckey J.A., Wishart M.J., Dixon J.E.
J. Biol. Chem. 277:2377-2380(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOGEN-BINDING, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT EPM2 GLY-32, ACTIVE SITE, MUTAGENESIS OF LYS-87 AND CYS-266.
[13]"Identification of a novel protein interacting with laforin, the EPM2A progressive myoclonus epilepsy gene product."
Ianzano L., Zhao X.C., Minassian B.A., Scherer S.W.
Genomics 81:579-587(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPM2AIP1.
[14]"The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain."
Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H., Delgado-Escueta A.V., Yamakawa K.
Hum. Mol. Genet. 12:2359-2368(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIRIP5.
[15]"Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation."
Fernandez-Sanchez M.E., Criado-Garcia O., Heath K.E., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa J.M., Rodriguez de Cordoba S.
Hum. Mol. Genet. 12:3161-3171(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-INTERACTION, INTERACTION WITH PPP1R3C, MUTAGENESIS OF ASP-235 AND CYS-266, CHARACTERIZATION OF VARIANTS EPM2 GLY-32; LEU-84; CYS-108; ILE-194; SER-240; SER-279; LEU-293; ASN-294 AND LEU-301.
[16]"The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies."
Ganesh S., Tsurutani N., Suzuki T., Hoshii Y., Ishihara T., Delgado-Escueta A.V., Yamakawa K.
Biochem. Biophys. Res. Commun. 313:1101-1109(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO LAFORA BODIES, CHARACTERIZATION OF VARIANTS EPM2 PRO-25; LYS-28; GLY-32 AND LEU-88, CHARACTERIZATION OF VARIANT PRO-46.
[17]"Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin."
Gentry M.S., Worby C.A., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 102:8501-8506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NHLRC1, POLYUBIQUITINATION.
[18]"Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates."
Worby C.A., Gentry M.S., Dixon J.E.
J. Biol. Chem. 281:30412-30418(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GLUCAN PHOSPHATASE, INTERACTION WITH PPP1R3B; PPP1R3C AND PPP1R3D.
[19]"A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease."
Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.
Genes Dev. 21:2399-2409(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Modulation of functional properties of laforin phosphatase by alternative splicing reveals a novel mechanism for the EPM2A gene in Lafora progressive myoclonus epilepsy."
Dubey D., Ganesh S.
Hum. Mol. Genet. 17:3010-3020(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, HETERODIMERIZATION, SUBCELLULAR LOCATION.
[21]"Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)."
Worby C.A., Gentry M.S., Dixon J.E.
J. Biol. Chem. 283:4069-4076(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP1R3C.
[22]"The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system."
Garyali P., Siwach P., Singh P.K., Puri R., Mittal S., Sengupta S., Parihar R., Ganesh S.
Hum. Mol. Genet. 18:688-700(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPLEX FORMATION WITH NHLRC1 AND HSP70.
[23]"Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease."
Puri R., Suzuki T., Yamakawa K., Ganesh S.
J. Biol. Chem. 284:22657-22663(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPT.
[24]"Laforin, the most common protein mutated in Lafora disease, regulates autophagy."
Aguado C., Sarkar S., Korolchuk V.I., Criado O., Vernia S., Boya P., Sanz P., de Cordoba S.R., Knecht E., Rubinsztein D.C.
Hum. Mol. Genet. 19:2867-2876(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase."
Roma-Mateo C., Solaz-Fuster Mdel C., Gimeno-Alcaniz J.V., Dukhande V.V., Donderis J., Worby C.A., Marina A., Criado O., Koller A., Rodriguez De Cordoba S., Gentry M.S., Sanz P.
Biochem. J. 439:265-275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-25 (ISOFORM 1), MUTAGENESIS OF SER-25; SER-168; THR-187 AND THR-194.
[26]"Identification and characterization of novel splice variants of the human EPM2A gene mutated in Lafora progressive myoclonus epilepsy."
Dubey D., Parihar R., Ganesh S.
Genomics 99:36-43(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 4; 5; 6; 7 AND 9).
[27]"Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex."
Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.
Int. J. Biochem. Cell Biol. 45:1479-1488(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP1R3D.
[28]"Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329."
Sanchez-Martin P., Raththagala M., Bridges T.M., Husodo S., Gentry M.S., Sanz P., Roma-Mateo C.
PLoS ONE 8:E69523-E69523(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 109-CYS-CYS-110; CYS-123; CYS-169; CYS-205; CYS-250; CYS-266; CYS-329 AND 329-CYS--CYS-331.
[29]"Mutational spectrum of the EPM2A gene in progressive myoclonus epilepsy of Lafora: high degree of allelic heterogeneity and prevalence of deletions."
Gomez-Garre P., Sanz Y., Rodriguez de Cordoba S.R., Serratosa J.M.
Eur. J. Hum. Genet. 8:946-954(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPM2 LEU-84; SER-240 AND LEU-301.
[30]"Mutation screening for Japanese Lafora's disease patients: identification of novel sequence variants in the coding and upstream regulatory regions of EPM2A gene."
Ganesh S., Shoda K., Amano K., Uchiyama A., Kumada S., Moriyama N., Hirose S., Yamakawa K.
Mol. Cell. Probes 15:281-289(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-46.
[31]"Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype."
Ganesh S., Delgado-Escueta A.V., Suzuki T., Francheschetti S., Riggio C., Avanzini G., Rabinowicz A., Bohlega S., Bailey J., Alonso M.E., Rasmussen A., Thomson A.E., Ochoa A., Prado A.J., Medina M.T., Yamakawa K.
Hum. Mol. Genet. 11:1263-1271(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPM2 PRO-25; CYS-108; HIS-171 AND LEU-293, CHARACTERIZATION OF VARIANTS EPM2 GLY-32; CYS-108; ILE-194; SER-279 AND ASN-294.
[32]"Two novel mutations in the EPM2A gene in a Korean patient with Lafora's progressive myoclonus epilepsy."
Ki C.S., Kong S.Y., Seo D.W., Hong S.B., Kim H.J., Kim J.W.
J. Hum. Genet. 48:51-54(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPM2 ALA-187.
[33]"A novel exon 1 mutation in a patient with atypical Lafora progressive myoclonus epilepsy seen as childhood-onset cognitive deficit."
Annesi G., Sofia V., Gambardella A., Ciro Candiano I.C., Spadafora P., Annesi F., Cutuli N., De Marco E.V., Civitelli D., Carrideo S., Tarantino P., Barone R., Zappia M., Quattrone A.
Epilepsia 45:294-295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPM2 PRO-91.
[34]"Loss of function of the cytoplasmic isoform of the protein laforin (EPM2A) causes Lafora progressive myoclonus epilepsy."
Ianzano L., Young E.J., Zhao X.C., Chan E.M., Rodriguez M.T., Torrado M.V., Scherer S.W., Minassian B.A.
Hum. Mutat. 23:170-176(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPM2 PRO-91; HIS-171 AND SER-279.
[35]"Mutations in the NHLRC1 gene are the common cause for Lafora disease in the Japanese population."
Singh S., Suzuki T., Uchiyama A., Kumada S., Moriyama N., Hirose S., Takahashi Y., Sugie H., Mizoguchi K., Inoue Y., Kimura K., Sawaishi Y., Yamakawa K., Ganesh S.
J. Hum. Genet. 50:347-352(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-46.
[36]"Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin."
Singh S., Satishchandra P., Shankar S.K., Ganesh S.
Hum. Mutat. 29:E1-12(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPM2 ASN-140; TYR-148; LYS-210 AND TRP-310, CHARACTERIZATION OF VARIANT EPM2 TRP-310.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084535 mRNA. Translation: AAC83347.2.
AF284580 mRNA. Translation: AAG18377.1.
AF454491 mRNA. Translation: AAO15523.1.
AF454492 mRNA. Translation: AAO15524.1.
AF454493 mRNA. Translation: AAO15525.1.
AF454494 mRNA. Translation: AAO15526.1.
AK022721 mRNA. Translation: BAG51107.1. Frameshift.
AK299497 mRNA. Translation: BAG61454.1.
AL023806, AL365193 Genomic DNA. Translation: CAI21419.1.
AL365193, AL023806 Genomic DNA. Translation: CAI21675.1.
CH471051 Genomic DNA. Translation: EAW47844.1.
BC005286 mRNA. Translation: AAH05286.1.
BC070047 mRNA. Translation: AAH70047.1.
AJ130763 mRNA. Translation: CAA10199.1.
AJ130764 mRNA. Translation: CAA10200.1.
RefSeqNP_001018051.1. NM_001018041.1.
NP_005661.1. NM_005670.3.
UniGeneHs.486696.

3D structure databases

ProteinModelPortalO95278.
SMRO95278. Positions 8-105, 154-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113679. 13 interactions.
IntActO95278. 2 interactions.
STRING9606.ENSP00000356489.

Chemistry

ChEMBLCHEMBL2311242.

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.

PTM databases

PhosphoSiteO95278.

Proteomic databases

PaxDbO95278.
PRIDEO95278.

Protocols and materials databases

DNASU7957.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367519; ENSP00000356489; ENSG00000112425. [O95278-1]
GeneID7957.
KEGGhsa:7957.
UCSCuc003qku.3. human. [O95278-7]
uc003qkv.3. human. [O95278-2]
uc003qkw.3. human. [O95278-1]
uc010khr.3. human. [O95278-5]

Organism-specific databases

CTD7957.
GeneCardsGC06M145822.
HGNCHGNC:3413. EPM2A.
HPAHPA053643.
HPA055468.
MIM254780. phenotype.
607566. gene.
neXtProtNX_O95278.
Orphanet501. Lafora disease.
PharmGKBPA27832.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243912.
HOGENOMHOG000285975.
HOVERGENHBG051493.
InParanoidO95278.
KOK14165.
OMARKVQYFV.
PhylomeDBO95278.
TreeFamTF332841.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO95278.
BgeeO95278.
CleanExHS_EPM2A.
GenevestigatorO95278.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00686. CBM_20. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF49452. SSF49452. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi7957.
NextBio30475.
PROO95278.
SOURCESearch...

Entry information

Entry nameEPM2A_HUMAN
AccessionPrimary (citable) accession number: O95278
Secondary accession number(s): B3KMU5 expand/collapse secondary AC list , B4DRZ2, O95483, Q5T3F5, Q6IS15, Q8IU96, Q8IX24, Q8IX25, Q9BS66, Q9UEN2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 121 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM