ID SYUB_HUMAN Reviewed; 134 AA. AC Q16143; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-JUL-2008, entry version 73. DE RecName: Full=Beta-synuclein; GN Name=SNCB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Brain; RX MEDLINE=94252398; PubMed=8194594; DOI=10.1016/0014-5793(94)00395-5; RA Jakes R., Spillantini M.G., Goedert M.; RT "Identification of two distinct synucleins from human brain."; RL FEBS Lett. 345:27-32(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99026142; PubMed=9806846; DOI=10.1006/geno.1998.5556; RA Lavedan C., Leroy E., Torres R., Dehejia A., Dutra A., Buchholtz S., RA Nussbaum R.L., Polymeropoulos M.H.; RT "Genomic organization and expression of the human beta-synuclein gene RT (SNCB)."; RL Genomics 54:173-175(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION. RX MEDLINE=20409007; PubMed=10852916; DOI=10.1074/jbc.M003542200; RA Pronin A.N., Morris A.J., Surguchov A., Benovic J.L.; RT "Synucleins are a novel class of substrates for G protein-coupled RT receptor kinases."; RL J. Biol. Chem. 275:26515-26522(2000). CC -!- FUNCTION: Non-amyloid component of senile plaques found in CC Alzheimer disease. Could act as a regulator of SNCA aggregation CC process. Protects neurons from staurosporine and 6 hydroxy CC dopamine (6OHDA)-stimulated caspase activation in a p53-dependent CC manner. Contributes to restore the SNCA anti-apoptotic function CC abolished by 6OHDA. Not found in the Lewy bodies associated with CC Parkinson disease. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain; concentrated CC in presynaptic nerve terminals. CC -!- PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor CC kinases (GRK) is more efficient than phosphorylation by CK1, CK2 CC and CaM-kinase II. CC -!- DISEASE: Brain iron accumulation type 1 (NBIA1, also called CC Hallervorden-Spatz syndrome), a rare neuroaxonal dystrophy, is CC histologically characterized by axonal spheroids, iron deposition, CC Lewy body (LB)-like intraneuronal inclusions, glial inclusions and CC neurofibrillary tangles. SNCB is found in spheroids but not in CC inclusions. CC -!- SIMILARITY: Belongs to the synuclein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S69965; AAB30860.1; -; mRNA. DR EMBL; AF053136; AAC80286.1; -; Genomic_DNA. DR EMBL; AF053134; AAC80286.1; JOINED; Genomic_DNA. DR EMBL; AF053135; AAC80286.1; JOINED; Genomic_DNA. DR EMBL; BT006627; AAP35273.1; -; mRNA. DR EMBL; BC002902; AAH02902.1; -; mRNA. DR PIR; S44430; S44430. DR RefSeq; NP_001001502.1; -. DR RefSeq; NP_003076.1; -. DR UniGene; Hs.90297; -. DR PhosphoSite; Q16143; -. DR Ensembl; ENSG00000074317; Homo sapiens. DR GeneID; 6620; -. DR KEGG; hsa:6620; -. DR H-InvDB; HIX0005445; -. DR HGNC; HGNC:11140; SNCB. DR HPA; CAB002681; -. DR MIM; 602569; gene. DR PharmGKB; PA35988; -. DR HOGENOM; Q16143; -. DR HOVERGEN; Q16143; -. DR ArrayExpress; Q16143; -. DR CleanEx; HS_SNCB; -. DR GermOnline; ENSG00000074317; Homo sapiens. DR GO; GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc. DR InterPro; IPR001058; Synuclein. DR InterPro; IPR002461; Synuclein_beta. DR Gene3D; G3DSA:1.10.287.700; Synuclein; 1. DR PANTHER; PTHR13820; Synuclein; 1. DR PANTHER; PTHR13820:SF4; Synuclein_beta; 1. DR Pfam; PF01387; Synuclein; 1. DR PRINTS; PR01213; BSYNUCLEIN. DR PRINTS; PR01211; SYNUCLEIN. DR ProDom; PD010631; Synuclein; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Repeat. FT CHAIN 1 134 Beta-synuclein. FT /FTId=PRO_0000184035. FT REPEAT 20 30 1. FT REPEAT 31 41 2. FT REPEAT 42 56 3; approximate. FT REPEAT 57 67 4. FT REGION 20 67 4 X 11 AA tandem repeats of [EGS]-K-T-K- FT [EQ]-[GQ]-V-X(4). FT MOD_RES 118 118 Phosphoserine; by BARK1, CK2 and GRK5. SQ SEQUENCE 134 AA; 14288 MW; 5BCA9FCA615AC4EF CRC64; MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTREGVVQ GVASVAEKTK EQASHLGGAV FSGAGNIAAA TGLVKREEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE DPPQEEYQEY EPEA //