(data stored in ACNUC27670 zone)

HOGENOM: HS1_PE4557

ID   HS1_PE4557                           STANDARD;      PRT;   105 AA.
AC   HS1_PE4557; P31949; Q5VTK0;
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-A11;AltName: Full=Calgizzarin;AltName:
DE   Full=Metastatic lymph node gene 70 protein; Short=MLN 70;AltName:
DE   Full=Protein S100-C;AltName: Full=S100 calcium-binding protein A11;
DE   (HS1.PE4557).
GN   Name=S100A11; Synonyms=MLN70, S100C;
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.PE4557.
CC       Homo sapiens chromosome 1 GRCh37  sequence 1..249240621 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:S10AB_HUMAN
CC   -!- FUNCTION: Facilitates the differentiation and the cornification of
CC       keratinocytes.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- INTERACTION:
CC       P04271:S100B; NbExp=5; IntAct=EBI-701862, EBI-458391;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: Phosphorylation at Thr-10 by PRKCA significantly suppresses
CC       homodimerization and promotes association with NCL/nucleolin which
CC       induces nuclear translocation.
CC   -!- MISCELLANEOUS: Binds two calcium ions per molecule with an
CC       affinity similar to that of the S-100 proteins (By similarity).
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;ENSG00000163191;ENST00000271638;ENSP00000271638.
DR   EMBL; AK312184; - ;
DR   EMBL; AL591893; - ;
DR   EMBL; BC001410; - ;
DR   EMBL; BC014354; - ;
DR   EMBL; BT009912; - ;
DR   EMBL; D38583; - ;
DR   EMBL; D49355; - ;
DR   EMBL; D50374; - ;
DR   EMBL; X80201; - ;
DR   UniProtKB/Swiss-Prot; P31949; Q5VTK0; -.
DR   EMBL; D38583; BAA07597.1; -; mRNA.
DR   EMBL; X80201; CAA56492.1; -; mRNA.
DR   EMBL; D49355; BAA08354.1; -; mRNA.
DR   EMBL; D50374; BAA23325.1; -; mRNA.
DR   EMBL; BT009912; AAP88914.1; -; mRNA.
DR   EMBL; AL591893; CAH72895.1; -; Genomic_DNA.
DR   EMBL; BC001410; AAH01410.1; -; mRNA.
DR   EMBL; BC014354; AAH14354.1; -; mRNA.
DR   IPI; IPI00013895; -.
DR   PIR; I37080; I37080.
DR   RefSeq; NP_005611.1; NM_005620.1.
DR   UniGene; Hs.417004; -.
DR   PDB; 1V4Z; NMR; -; A=1-19.
DR   PDB; 1V50; NMR; -; A=1-19.
DR   PDBsum; 1V4Z; -.
DR   PDBsum; 1V50; -.
DR   ProteinModelPortal; P31949; -.
DR   SMR; P31949; 5-104.
DR   IntAct; P31949; 6.
DR   STRING; P31949; -.
DR   PhosphoSite; P31949; -.
DR   SWISS-2DPAGE; P31949; -.
DR   Aarhus/Ghent-2DPAGE; 4006; IEF.
DR   DOSAC-COBS-2DPAGE; P31949; -.
DR   PMMA-2DPAGE; P31949; -.
DR   PeptideAtlas; P31949; -.
DR   PRIDE; P31949; -.
DR   Ensembl; ENST00000271638; ENSP00000271638; ENSG00000163191.
DR   GeneID; 6282; -.
DR   KEGG; hsa:6282; -.
DR   UCSC; uc001ezn.1; human.
DR   CTD; 6282; -.
DR   GeneCards; GC01M123382; -.
DR   H-InvDB; HIX0001073; -.
DR   HGNC; HGNC:10488; S100A11.
DR   MIM; 603114; gene.
DR   neXtProt; NX_P31949; -.
DR   PharmGKB; PA34900; -.
DR   eggNOG; prNOG20799; -.
DR   GeneTree; ENSGT00600000084283; -.
DR   InParanoid; P31949; -.
DR   OMA; MSSPTET; -.
DR   OrthoDB; EOG4BG8XN; -.
DR   PhylomeDB; P31949; -.
DR   NextBio; 24385; -.
DR   ArrayExpress; P31949; -.
DR   Bgee; P31949; -.
DR   CleanEx; HS_S100A11; -.
DR   Genevestigator; P31949; -.
DR   GermOnline; ENSG00000163191; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0048154; F:S100 beta binding; IPI:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR   GO; GO:0008156; P:negative regulation of DNA replication; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR001751; S100/CaBP-9k_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 1.
DR   Pfam; PF01023; S_100; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   HOGENOMDNA; HS1.PE4557; -.
KW   ENSG000001631911755old_1320000031; ENSP000002716387901old_1320000031;
KW   B2R5H0_HUMAN; AK312184; AL591893; BC001410; BC014354; BT009912; D38583;
KW   D50374; X80201;
KW   3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
SQ   SEQUENCE   105 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKISSPTET ERCIESLIAV FQKYAGKDGY NYTLSKTEFL SFMNTELAAF TKNQKDPGVL
     DRMMKKLDTN SDGQLDFSEF LNLIGGLAMA CHDSFLKAVP SQKRT
//

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