(data stored in ACNUC9435 zone)

HOGENOM: HS11_PE652

ID   HS11_PE652                           STANDARD;      PRT;   1849 AA.
AC   HS11_PE652;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Myotubularin-related protein 13;AltName: Full=SET-binding
DE   factor 2; (HS11.PE652).
GN   Name=SBF2; Synonyms=CMT4B2, KIAA1766, MTMR13;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS11.PE652.
CC       Homo sapiens chromosome 11 GRCh37  sequence 1..134946516 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:MTMRD_HUMAN
CC   -!- SUBUNIT: Interacts with MTMR2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Associated with membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86WG5-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q86WG5-3; Sequence=VSP_017157, VSP_017158;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in spinal cord.
CC   -!- DISEASE: Defects in SBF2 are the cause of Charcot-Marie-Tooth
CC       disease type 4B2 (CMT4B2) [MIM:604563]. CMT4B2 is a recessive form
CC       of Charcot-Marie-Tooth disease, the most common inherited disorder
CC       of the peripheral nervous system. Charcot-Marie-Tooth disease is
CC       classified in two main groups on the basis of electrophysiologic
CC       properties and histopathology: primary peripheral demyelinating
CC       neuropathy and primary peripheral axonal neuropathy. Demyelinating
CC       CMT neuropathies are characterized by severely reduced nerve
CC       conduction velocities (less than 38 m/sec), segmental
CC       demyelination and remyelination with onion bulb formations on
CC       nerve biopsy, slowly progressive distal muscle atrophy and
CC       weakness, absent deep tendon reflexes, and hollow feet. By
CC       convention, autosomal recessive forms of demyelinating Charcot-
CC       Marie-Tooth disease are designated CMT4. CMT4B2 is characterized
CC       by abnormal folding of myelin sheaths.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- CAUTION: In contrast to other members of the family, it lacks a
CC       canonical protein-tyrosine phosphatase domain and lacks the
CC       conserved Cys residue in position 1410 which is replaced by a Leu
CC       residue. It therefore probably does not have phosphatase activity.
CC   -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC       URL="http://www.molgen.ua.ac.be/CMTMutations/";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/SBF2";
CC   -!- GENE_FAMILY: HOG000044360 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000133812;ENST00000256190;ENSP00000256190.
DR   EMBL; AB051553; - ;
DR   EMBL; AK091362; - ;
DR   EMBL; AK123621; - ;
DR   EMBL; AL512756; - ;
DR   EMBL; AY234241; - ;
DR   EMBL; BC011143; - ;
DR   EMBL; BC043389; - ;
DR   EMBL; BC053867; - ;
DR   EMBL; BC063656; - ;
DR   EMBL; BC101466; - ;
DR   EMBL; BX538184; - ;
DR   EMBL; CR749312; - ;
DR   UniProtKB/Swiss-Prot; Q86WG5; Q3MJF0; Q68DQ3; Q6P459; Q6PJD1; Q7Z325; Q7Z621; Q86VE2; -.
DR   UniProtKB/Swiss-Prot; Q96FE2; Q9C097; -.
DR   EMBL; AY234241; AAO62733.1; -; mRNA.
DR   EMBL; BC011143; AAH11143.1; -; mRNA.
DR   EMBL; BC043389; AAH43389.1; -; mRNA.
DR   EMBL; BC053867; AAH53867.1; -; mRNA.
DR   EMBL; BC063656; AAH63656.1; -; mRNA.
DR   EMBL; BC101466; AAI01467.1; -; mRNA.
DR   EMBL; AB051553; BAB21857.1; -; mRNA.
DR   EMBL; BX538184; CAD98056.1; -; mRNA.
DR   EMBL; CR749312; CAH18167.1; -; mRNA.
DR   IPI; IPI00654703; -.
DR   IPI; IPI00719299; -.
DR   RefSeq; NP_112224.1; NM_030962.3.
DR   UniGene; Hs.577252; -.
DR   ProteinModelPortal; Q86WG5; -.
DR   SMR; Q86WG5; 874-1585, 1746-1847.
DR   IntAct; Q86WG5; 1.
DR   STRING; Q86WG5; -.
DR   PhosphoSite; Q86WG5; -.
DR   PRIDE; Q86WG5; -.
DR   Ensembl; ENST00000256190; ENSP00000256190; ENSG00000133812.
DR   GeneID; 81846; -.
DR   KEGG; hsa:81846; -.
DR   NMPDR; fig|9606.3.peg.5252; -.
DR   UCSC; uc001mib.2; human.
DR   UCSC; uc001mif.2; human.
DR   CTD; 81846; -.
DR   GeneCards; GC11M009472; -.
DR   H-InvDB; HIX0009438; -.
DR   HGNC; HGNC:2135; SBF2.
DR   MIM; 604563; phenotype.
DR   MIM; 607697; gene.
DR   neXtProt; NX_Q86WG5; -.
DR   Orphanet; 99956; Charcot-Marie-Tooth disease type 4B2.
DR   PharmGKB; PA26649; -.
DR   eggNOG; prNOG14178; -.
DR   InParanoid; Q86WG5; -.
DR   OMA; CQGSGFA; -.
DR   OrthoDB; EOG48D0TF; -.
DR   PhylomeDB; Q86WG5; -.
DR   NextBio; 72146; -.
DR   ArrayExpress; Q86WG5; -.
DR   Bgee; Q86WG5; -.
DR   Genevestigator; Q86WG5; -.
DR   GermOnline; ENSG00000133812; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0042552; P:myelination; NAS:UniProtKB.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR022096; SBF2.
DR   InterPro; IPR005113; uDENN.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF12335; SBF2; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50946; UDENN; 1.
DR   HOGENOMDNA; HS11.PE652; -.
KW   ENSG000001338121755old_1320000031; ENSP000002561907901old_1320000031;
KW   B3KRC9_HUMAN; B3KVW2_HUMAN; Q9H032_HUMAN; AB051553; AK091362; AK123621;
KW   AY234241; BC011143; BC043389; BC053867; BC063656; BC101466; BX538184;
KW   CR749312;
KW   Alternative splicing; Charcot-Marie-Tooth disease; Complete proteome;
KW   Cytoplasm; Membrane; Neuropathy; Polymorphism; Reference proteome.
SQ   SEQUENCE   1849 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MARLADYFIV VGYDHEKPGS GEGLGKIIQR FPQKDWDDTP FPQGIELFCQ PGGWQLSRER
     KQPTFFVVVL TDIDSDRHYC SCLTFYEAEI NLQGTKKEEI EGEAKVSGLI QPAEVFAPKS
     LVLVSRLYYP EIFRACLGLI YTVYVDSLNV SLESLIANLC ACLVPAAGGS QKLFSLGAGD
     RQLIQTPLHD SLPITGTSVA LLFQQLGIQN VLSLFCAVLT ENKVLFHSAS FQRLSDACRA
     LESLMFPLKY SYPYIPILPA QLLEVLSSPT PFIIGVHSVF KTDVHELLDV IIADLDGGTI
     KIPECIHLSS LPEPLLHQTQ SALSLILHPD LEVADHAFPP PRTALSHSKM LDKEVRAVFL
     RLFAQLFQGY RSCLQLIRIH AEPVIHFHKT AFLGQRGLVE NDFLTKVLSG MAFAGFVSER
     GPPYRSCDLF DELVAFEVER IKVEENNPVK MIKHVRELAE QLFKNENPNP HMAFQKVPRP
     TEGSHLRVHI LPFPEINEAR VQELIQENVA KNQNAPPATR IEKKCVVPAG PPVVSIMDKV
     TTVFNSAQRL EVVRNCISFI FENKILETEK TLPAALRALK GKAARQCLTD ELGLHVQQNR
     AILDHQQFDY IIRMMNCTLQ DCSSLEEYNI AAALLPLTSA FYRKLAPGVS QFAYTCVQDH
     PIWTNQQFWE TTFYNAVQEQ VRSLYLSAKE DNHAPHLKQK DKLPDDHYQE KTAMDLAAEQ
     LRLWPTLSKS TQQELVQHEE STVFSQAIHF ANLMVNLLVP LDTSKNKLLR TSAPGDWESG
     SNSIVTNSIA GSVAESYDTE SGFEDSENTD IANSVVRFIT RFIDKVCTES GVTQDHIKSL
     HCMIPGIVAM HIETLEAVHR ESRRLPPIQK PKILRPALLP GEEIVCEGLR VLLDPDGREE
     ATGGLLGGPQ LLPAEGALFL TTYRILFRGT PHDQLVGEQT VVRSFPIASI TKEKKITMQN
     QLQQNMQEGL QITSASFQLI KVAFDEEVSP EVVEIFKKQL MKFRYPQSIF STFAFAAGQT
     TPQIILPKQK EKNTSFRTFS KTIVKGAKRA GKMTIGRQYL LKKKTGTIVE ERVNRPGWNE
     DDDVSVSDES ELPTSTTLKA SEKSTMEQLV EKACFRDYQR LGLGTISGSS SRSRPEYFRI
     TASNRMYSLC RSYPGLLVVP QAVQDSSLPR VARCYRHNRL PVVCWKNSRS GTLLLRSGGF
     HGKGVVGLFK SQNSPQAAPT SSLESSSSIE QEKYLQALLN AVSVHQKLRG NSTLTVRPAF
     ALSPGVWASL RSSTRLISSP TSFIDVGARL AGKDHSASFS NSSYLQNQLL KRQAALYIFG
     EKSQLRNFKV EFALNCEFVP VEFHEIRQVK ASFKKLMRAC IPSTIPTDSE VTFLKALGDS
     EWFPQLHRIM QLAVVVSEVL ENGSSVLVCL EEGWDITAQV TSLVQLLSDP FYRTLEGFQM
     LVEKEWLSFG HKFSQRSSLT LNCQGSGFAP VFLQFLDCVH QVHNQYPTEF EFNLYYLKFL
     AFHYVSNRFK TFLLDSDYER LEHGTLFDDK GEKHAKKGVC IWECIDRMHK RSPIFFNYLY
     SPLEIEALKP NVNVSSLKKW DYYIEETLST GPSYDWMMLT PKHFPSEDSD LAGEAGPRSQ
     RRTVWPCYDD VSCTQPDALT SLFSEIEKLE HKLNQAPEKW QQLWERVTVD LKEEPRTDRS
     QRHLSRSPGI VSTNLPSYQK RSLLHLPDSS MGEEQNSSIS PSNGVERRAA TLYSQYTSKN
     DENRSFEGTL YKRGALLKGW KPRWFVLDVT KHQLRYYDSG EDTSCKGHID LAEVEMVIPA
     GPSMGAPKHT SDKAFFDLKT SKRVYNFCAQ DGQSAQQWMD KIQSCISDA
//

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