Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein S100-G

Gene

S100G

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi18 – 31141; low affinityAdd
BLAST
Calcium bindingi58 – 69122; high affinityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Vitamin D

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-G
Alternative name(s):
Calbindin-D9k
S100 calcium-binding protein G
Vitamin D-dependent calcium-binding protein, intestinal
Short name:
CABP
Gene namesi
Name:S100G
Synonyms:CALB3, S100D
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 7978Protein S100-GPRO_0000144026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei42 – 421PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP02633.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022630.

Structurei

Secondary structure

1
79
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1812Combined sources
Beta strandi20 – 223Combined sources
Beta strandi26 – 283Combined sources
Helixi29 – 3911Combined sources
Helixi40 – 423Combined sources
Beta strandi45 – 484Combined sources
Helixi50 – 578Combined sources
Beta strandi58 – 603Combined sources
Beta strandi62 – 654Combined sources
Helixi67 – 7711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1GNMR-A5-79[»]
1BOCNMR-A5-79[»]
1BODNMR-A5-79[»]
1CDNNMR-A5-79[»]
1CLBNMR-A5-79[»]
1D1ONMR-A5-79[»]
1HT9X-ray1.76A/B5-79[»]
1IG5X-ray1.50A5-79[»]
1IGVX-ray1.85A5-79[»]
1KCYNMR-A5-79[»]
1KQVNMR-A1-79[»]
1KSMNMR-A1-79[»]
1N65NMR-A5-79[»]
1QX2X-ray1.44A/B5-79[»]
1RT0NMR-A58-69[»]
2BCANMR-A5-79[»]
2BCBNMR-A5-79[»]
2MAZNMR-A5-79[»]
3ICBX-ray2.30A5-79[»]
4ICBX-ray1.60A5-79[»]
ProteinModelPortaliP02633.
SMRiP02633. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02633.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini45 – 7935EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410J1CR. Eukaryota.
ENOG4111C34. LUCA.
GeneTreeiENSGT00530000064238.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP02633.
KOiK14734.
OMAiLLIQTEF.
OrthoDBiEOG7Z3F78.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028489. S100G.
[Graphical view]
PANTHERiPTHR11639:SF73. PTHR11639:SF73. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKKSPEEL KGIFEKYAAK EGDPNQLSKE ELKLLLQTEF PSLLKGPSTL
60 70
DELFEELDKN GDGEVSFEEF QVLVKKISQ
Length:79
Mass (Da):8,918
Last modified:January 23, 2007 - v3
Checksum:i80A5B2AA11D4E74B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18344 mRNA. Translation: AAA30420.1.
BC118480 mRNA. Translation: AAI18481.1.
PIRiA40151. KLBOI.
RefSeqiNP_776682.1. NM_174257.3.
UniGeneiBt.390.

Genome annotation databases

EnsembliENSBTAT00000022630; ENSBTAP00000022630; ENSBTAG00000017020.
GeneIDi281658.
KEGGibta:281658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18344 mRNA. Translation: AAA30420.1.
BC118480 mRNA. Translation: AAI18481.1.
PIRiA40151. KLBOI.
RefSeqiNP_776682.1. NM_174257.3.
UniGeneiBt.390.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1GNMR-A5-79[»]
1BOCNMR-A5-79[»]
1BODNMR-A5-79[»]
1CDNNMR-A5-79[»]
1CLBNMR-A5-79[»]
1D1ONMR-A5-79[»]
1HT9X-ray1.76A/B5-79[»]
1IG5X-ray1.50A5-79[»]
1IGVX-ray1.85A5-79[»]
1KCYNMR-A5-79[»]
1KQVNMR-A1-79[»]
1KSMNMR-A1-79[»]
1N65NMR-A5-79[»]
1QX2X-ray1.44A/B5-79[»]
1RT0NMR-A58-69[»]
2BCANMR-A5-79[»]
2BCBNMR-A5-79[»]
2MAZNMR-A5-79[»]
3ICBX-ray2.30A5-79[»]
4ICBX-ray1.60A5-79[»]
ProteinModelPortaliP02633.
SMRiP02633. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022630.

Proteomic databases

PaxDbiP02633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022630; ENSBTAP00000022630; ENSBTAG00000017020.
GeneIDi281658.
KEGGibta:281658.

Organism-specific databases

CTDi795.

Phylogenomic databases

eggNOGiENOG410J1CR. Eukaryota.
ENOG4111C34. LUCA.
GeneTreeiENSGT00530000064238.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP02633.
KOiK14734.
OMAiLLIQTEF.
OrthoDBiEOG7Z3F78.
TreeFamiTF332727.

Miscellaneous databases

EvolutionaryTraceiP02633.
NextBioi20805589.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028489. S100G.
[Graphical view]
PANTHERiPTHR11639:SF73. PTHR11639:SF73. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The molecular cloning of the complementary deoxyribonucleic acid for bovine vitamin D-dependent calcium-binding protein: structure of the full-length protein and evidence for homologies with other calcium-binding proteins of the troponin-C superfamily of proteins."
    Kumar R., Wieben E., Beecher S.J.
    Mol. Endocrinol. 3:427-432(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Placenta.
  3. "The amino acid sequence of bovine intestinal calcium-binding protein."
    Fullmer C.S., Wasserman R.H.
    J. Biol. Chem. 256:5669-5674(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-79.
  4. "Structure of vitamin D-dependent calcium-binding protein from bovine intestine."
    Szebenyi D.M.E., Obendorf S.K., Moffat K.
    Nature 294:327-332(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  5. "The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins."
    Szebenyi D.M.E., Moffat K.
    J. Biol. Chem. 261:8761-8777(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY STRUCTURE REFINEMENT.
  6. "Structural basis for the negative allostery between Ca(2+)- and Mg(2+)-binding in the intracellular Ca(2+)-receptor calbindin D9k."
    Andersson M., Malmendal A., Linse S., Ivarsson I., Forsen S., Svensson L.A.
    Protein Sci. 6:1139-1147(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  7. "The rate and structural consequences of proline cis-trans isomerization in calbindin D9k: NMR studies of the minor (cis-Pro43) isoform and the Pro43Gly mutant."
    Kordel J., Forsen S., Drakenberg T., Chazin W.J.
    Biochemistry 29:4400-4409(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  8. "1H NMR resonance assignments, secondary structure, and global fold of Apo bovine calbindin D9k."
    Skelton N.J., Forsen S., Chazin W.J.
    Biochemistry 29:5752-5761(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k."
    Akke M., Forsen S., Chazin W.J.
    J. Mol. Biol. 220:173-189(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway."
    Akke M., Forsen S., Chazin W.J.
    J. Mol. Biol. 252:102-121(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "Protein solution structure calculations in solution: solvated molecular dynamics refinement of calbindin D9k."
    Kordel J., Pearlman D.A., Chazin W.J.
    J. Biomol. NMR 10:231-243(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiS100G_BOVIN
AccessioniPrimary (citable) accession number: P02633
Secondary accession number(s): Q17Q94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.