(data stored in ACNUC32233 zone)

HOGENOM: HS11_PE2113

ID   HS11_PE2113                          STANDARD;      PRT;   2390 AA.
AC   HS11_PE2113; O15020; O14872; O14873;
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=Spectrin beta chain, brain 2;AltName: Full=Beta-III
DE   spectrin;AltName: Full=Spectrin, non-erythroid beta chain 2;
DE   (HS11.PE2113).
GN   Name=SPTBN2; Synonyms=KIAA0302;
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.PE2113.
CC       Homo sapiens chromosome 11 GRCh37  sequence 1..134946516 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:SPTN2_HUMAN
CC   -!- FUNCTION: Probably plays an important role in neuronal membrane
CC       skeleton.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O15020-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15020-2; Sequence=VSP_000722;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, kidney, pancreas,
CC       and liver, and at lower levels in lung and placenta.
CC   -!- DISEASE: Defects in SPTBN2 are the cause of spinocerebellar ataxia
CC       type 5 (SCA5) [MIM:600224]. Spinocerebellar ataxia is a clinically
CC       and genetically heterogeneous group of cerebellar disorders.
CC       Patients show progressive incoordination of gait and often poor
CC       coordination of hands, speech and eye movements, due to
CC       degeneration of the cerebellum with variable involvement of the
CC       brainstem and spinal cord. SCA5 is an autosomal dominant
CC       cerebellar ataxia (ADCA). It is a slowly progressive disorder with
CC       variable age at onset, ranging between 10 and 50 years.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 17 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32700.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/SPTBN2";
CC   -!- GENE_FAMILY: HOG000007281 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000173898;ENST00000309996;ENSP00000311489.
DR   EMBL; AB008567; - ;
DR   EMBL; AF026487; - ;
DR   EMBL; AF026488; - ;
DR   EMBL; AF079569; - ;
DR   EMBL; FJ811850; - ;
DR   UniProtKB/Swiss-Prot; O15020; O14872; O14873; -.
DR   EMBL; AB008567; BAA32700.2; ALT_INIT; mRNA.
DR   EMBL; AP001157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF079569; AAC80006.1; -; mRNA.
DR   EMBL; AF026487; AAC79502.1; -; mRNA.
DR   EMBL; AF026488; AAC79503.1; -; mRNA.
DR   EMBL; AF026488; AAC79504.1; -; mRNA.
DR   IPI; IPI00012645; -.
DR   IPI; IPI00218207; -.
DR   RefSeq; NP_008877.1; NM_006946.2.
DR   UniGene; Hs.26915; -.
DR   PDB; 1WJM; NMR; -; A=2219-2328.
DR   PDB; 1WYQ; NMR; -; A=178-291.
DR   PDBsum; 1WJM; -.
DR   PDBsum; 1WYQ; -.
DR   ProteinModelPortal; O15020; -.
DR   SMR; O15020; 48-291, 300-2082, 2212-2333.
DR   IntAct; O15020; 4.
DR   STRING; O15020; -.
DR   PhosphoSite; O15020; -.
DR   PRIDE; O15020; -.
DR   Ensembl; ENST00000309996; ENSP00000311489; ENSG00000173898.
DR   GeneID; 6712; -.
DR   KEGG; hsa:6712; -.
DR   UCSC; uc001ojd.1; human.
DR   CTD; 6712; -.
DR   GeneCards; GC11M062780; -.
DR   H-InvDB; HIX0021762; -.
DR   HGNC; HGNC:11276; SPTBN2.
DR   HPA; CAB009844; -.
DR   MIM; 600224; phenotype.
DR   MIM; 604985; gene.
DR   neXtProt; NX_O15020; -.
DR   Orphanet; 98766; Spinocerebellar ataxia type 5.
DR   PharmGKB; PA36105; -.
DR   eggNOG; prNOG04562; -.
DR   GeneTree; ENSGT00560000077093; -.
DR   InParanoid; O15020; -.
DR   OMA; MAVREKE; -.
DR   OrthoDB; EOG43FGW0; -.
DR   Reactome; REACT_18266; Axon guidance.
DR   Reactome; REACT_92778; Axon guidance.
DR   NextBio; 26178; -.
DR   ArrayExpress; O15020; -.
DR   Bgee; O15020; -.
DR   CleanEx; HS_SPTBN2; -.
DR   Genevestigator; O15020; -.
DR   GermOnline; ENSG00000173898; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0008091; C:spectrin; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0008219; P:cell death; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   HOGENOMDNA; HS11.PE2113; -.
KW   ENSG000001738981755old_1320000031; ENSP000003114897901old_1320000031;
KW   C1KC08_HUMAN; AB008567; AF026487; AF026488; AF079569; FJ811850;
KW   3D-structure; Actin capping; Actin-binding; Alternative splicing;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
KW   Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Spinocerebellar ataxia.
SQ   SEQUENCE   2390 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK
     KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG EILPKPTKGR MRIHCLENVD
     KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD
     ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA
     FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
     MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
     EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
     EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
     VQAVDAVAAE LAAERYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL
     LYLMDWMEEM KGRLQSQDLG RHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCNP
     GKEYRPCDPQ LVSERVAKLE QSYEALCELA AARRARLEES RRLWRFLWEV GEAEAWVREQ
     QHLLASADTG RDLTGALRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGASQASA
     RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPELGHDEF
     STQALARQHR ALEEEIRSHR PTLDALREQA AALPPTLSRT PEVQSRVPTL ERHYEELQAR
     AGERARALEA ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
     MNTLAAQITA VNDIAEQLLK ANPPGKDRIV NTQEQLNHRW QQFRRLADGK KAALTSALSI
     QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTERDLEA IAARVGELTR
     EANALAAGHP AQAVAINARL REVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW
     LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC
     LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM
     PGTLQAADAA IKKLEDFMST MDANGERIHG LLEAGRQLVS EGNIHADKIR EKADSIERRH
     KKNQDAAQQF LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ
     AFMAELAANK DWLDKVDKEG RELTLEKPEL KALVSEKLRD LHRRWDELET TTQAKARSLF
     DANRAELFAQ SCCALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLEW EMAVREKEVE
     AIQAQAKALA QEDQGAGEVE RTSRAVEEKF RALCQPMRER CRRLQASREQ HQFHRDVEDE
     ILWVTERLPM ASSMEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLRER QRALGAAAAG
     PELAELQEMW KRLGHELELR GKRLEDALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE
     LSAQAEVKKH QVLEQALADY AQTIHQLAAS SQDMIDHEHP ESTRISIRQA QVDKLYAGLK
     ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS
     RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
     YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSPQVQQVQ
     DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM
     LWMDEVNLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG KELLARSHYA
     AEEISEKLSQ LQARRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE
     LGCTVDEVES LIKRHEAFQK SAVAWEERFC ALEKLTALEE REKERKRKRE EEERRKQPPA
     PEPTASVPPG DLVGGQTASD TTWDGTQPRP PPSTQAPSVN GVCTDGEPSQ PLLGQQRLEH
     SSFPEGPGPG SGDEANGPRG ERQTRTRGPA PSAMPQSRST ESAHAATLPP RGPEPSAQEQ
     MEGMLCRKQE MEAFGKKAAN RSWQNVYCVL RRGSLGFYKD AKAASAGVPY HGEVPVSLAR
     AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP
     VVPSTTRGMT RAMTMPPVSP VGAEGPVVLR SKDGRERERE KRFSFFKKNK
//

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