(data stored in ACNUC27670 zone)

HOGENOM: HS1_PE4673

ID   HS1_PE4673                           STANDARD;      PRT;   98 AA.
AC   HS1_PE4673; Q99584; Q52PI9; Q6FGF8;
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=Protein S100-A13;AltName: Full=S100 calcium-binding protein
DE   A13; (HS1.PE4673).
GN   Name=S100A13;
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 HS1.PE4673.
CC       Homo sapiens chromosome 1 GRCh37  sequence 1..249240621 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:S10AD_HUMAN
CC   -!- FUNCTION: Plays a role in the export of proteins that lack a
CC       signal peptide and are secreted by an alternative pathway. Binds
CC       two calcium ions per subunit. Binds one copper ion. Binding of one
CC       copper ion does not interfere with calcium binding. Required for
CC       the copper-dependent stress-induced export of IL1A and FGF1. The
CC       calcium-free protein binds to lipid vesicles containing
CC       phosphatidylserine, but not to vesicles containing
CC       phosphatidylcholine (By similarity).
CC   -!- SUBUNIT: Homodimer. Part of a copper-dependent multiprotein
CC       complex containing S100A13, FGF1 and SYT1. Interacts with FGF1 and
CC       SYT1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is
CC       mediated by exposure to stress and requires copper ions.
CC   -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.
CC   -!- SIMILARITY: Belongs to the S-100 family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- GENE_FAMILY: HOG000246968 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000189171;ENST00000368699;ENSP00000357688.
DR   EMBL; AY987392; - ;
DR   EMBL; BC000632; - ;
DR   EMBL; BC068064; - ;
DR   EMBL; BC070291; - ;
DR   EMBL; BT006724; - ;
DR   EMBL; BX470102; - ;
DR   EMBL; CH471121; - ;
DR   EMBL; CR542149; - ;
DR   EMBL; X99920; - ;
DR   UniProtKB/Swiss-Prot; Q99584; Q52PI9; Q6FGF8; -.
DR   EMBL; X99920; CAA68188.1; -; mRNA.
DR   EMBL; CR542149; CAG46946.1; -; mRNA.
DR   EMBL; BT006724; AAP35370.1; -; mRNA.
DR   EMBL; BX470102; CAI14760.1; -; Genomic_DNA.
DR   EMBL; BC000632; AAH00632.1; -; mRNA.
DR   EMBL; BC068064; AAH68064.1; -; mRNA.
DR   EMBL; BC070291; AAH70291.1; -; mRNA.
DR   EMBL; AY987392; AAX89402.1; -; mRNA.
DR   IPI; IPI00016179; -.
DR   PIR; JC5064; JC5064.
DR   RefSeq; NP_001019381.1; NM_001024210.1.
DR   RefSeq; NP_001019382.1; NM_001024211.1.
DR   RefSeq; NP_001019383.1; NM_001024212.1.
DR   RefSeq; NP_001019384.1; NM_001024213.1.
DR   RefSeq; NP_005970.1; NM_005979.2.
DR   UniGene; Hs.516505; -.
DR   PDB; 1YUR; NMR; -; A/B=1-98.
DR   PDB; 1YUS; NMR; -; A/B=1-98.
DR   PDB; 1YUT; NMR; -; A/B=1-98.
DR   PDB; 1YUU; NMR; -; A/B=1-98.
DR   PDB; 2EGD; X-ray; 1.80 A; A/B=1-98.
DR   PDB; 2H2K; X-ray; 2.00 A; A/B=1-98.
DR   PDB; 2K8M; NMR; -; B/C=1-98.
DR   PDB; 2KI4; NMR; -; B/C=1-98.
DR   PDB; 2KI6; NMR; -; C/D=1-98.
DR   PDB; 2KOT; NMR; -; A/B=1-98.
DR   PDB; 2L5X; NMR; -; B/C=1-98.
DR   PDBsum; 1YUR; -.
DR   PDBsum; 1YUS; -.
DR   PDBsum; 1YUT; -.
DR   PDBsum; 1YUU; -.
DR   PDBsum; 2EGD; -.
DR   PDBsum; 2H2K; -.
DR   PDBsum; 2K8M; -.
DR   PDBsum; 2KI4; -.
DR   PDBsum; 2KI6; -.
DR   PDBsum; 2KOT; -.
DR   PDBsum; 2L5X; -.
DR   ProteinModelPortal; Q99584; -.
DR   SMR; Q99584; 5-90.
DR   IntAct; Q99584; 2.
DR   STRING; Q99584; -.
DR   PhosphoSite; Q99584; -.
DR   PeptideAtlas; Q99584; -.
DR   PRIDE; Q99584; -.
DR   Ensembl; ENST00000339556; ENSP00000344822; ENSG00000189171.
DR   Ensembl; ENST00000368699; ENSP00000357688; ENSG00000189171.
DR   Ensembl; ENST00000392622; ENSP00000376398; ENSG00000189171.
DR   Ensembl; ENST00000392623; ENSP00000376399; ENSG00000189171.
DR   Ensembl; ENST00000440685; ENSP00000392767; ENSG00000189171.
DR   GeneID; 6284; -.
DR   KEGG; hsa:6284; -.
DR   NMPDR; fig|9606.3.peg.2109; -.
DR   UCSC; uc001fcf.2; human.
DR   CTD; 6284; -.
DR   GeneCards; GC01M124954; -.
DR   H-InvDB; HIX0001084; -.
DR   HGNC; HGNC:10490; S100A13.
DR   HPA; CAB025494; -.
DR   HPA; HPA019592; -.
DR   MIM; 601989; gene.
DR   neXtProt; NX_Q99584; -.
DR   PharmGKB; PA34902; -.
DR   eggNOG; prNOG21774; -.
DR   GeneTree; ENSGT00530000063972; -.
DR   InParanoid; Q99584; -.
DR   OMA; FTFAGRE; -.
DR   OrthoDB; EOG4G1MJ0; -.
DR   PhylomeDB; Q99584; -.
DR   DrugBank; DB01025; Amlexanox.
DR   NextBio; 24393; -.
DR   ArrayExpress; Q99584; -.
DR   Bgee; Q99584; -.
DR   CleanEx; HS_S100A13; -.
DR   Genevestigator; Q99584; -.
DR   GermOnline; ENSG00000189171; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0048602; F:fibroblast growth factor 1 binding; IPI:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0050703; P:interleukin-1 alpha secretion; IDA:UniProtKB.
DR   GO; GO:0043303; P:mast cell degranulation; NAS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF01023; S_100; 1.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS00303; S100_CABP; FALSE_NEG.
DR   HOGENOMDNA; HS1.PE4673; -.
KW   ENSG000001891711755old_1320000031; ENSP000003576887901old_1320000031;
KW   D3DV53_HUMAN; AY987392; BC000632; BC068064; BC070291; BT006724; BX470102;
KW   CR542149; X99920;
KW   3D-structure; Calcium; Complete proteome; Copper; Cytoplasm;
KW   Lipid-binding; Metal-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Secreted; Transport.
SQ   SEQUENCE   98 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAAEPLTELE ESIETVVTTF FTFARQEGRK DSLSVNEFKE LVTQQLPHLL KDVGSLDEKM
     KSLDVNQDSE LKFNEYWRLI GELAKEIRKK KDLKIRKK
//

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