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Protein

Protein S100-G

Gene

S100G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Regions

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

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. vitamin D binding Source: UniProtKB-KW
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:CABP9K, CALB3, S100D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:1436. S100G.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. basolateral plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26028.

Polymorphism and mutation databases

BioMutaiS100G.
DMDMi115387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7978Protein S100-GPRO_0000144027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP29377.

PTM databases

PhosphoSiteiP29377.

Expressioni

Gene expression databases

BgeeiP29377.
CleanExiHS_S100G.
GenevestigatoriP29377.

Organism-specific databases

HPAiCAB017688.
HPA055873.

Interactioni

Protein-protein interaction databases

BioGridi107246. 1 interaction.
STRINGi9606.ENSP00000369547.

Structurei

3D structure databases

ProteinModelPortaliP29377.
SMRiP29377. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiNOG39449.
GeneTreeiENSGT00530000064238.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP29377.
KOiK14734.
OMAiLLIQTEF.
OrthoDBiEOG7Z3F78.
PhylomeDBiP29377.
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:SF67. PTHR11639:SF67. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
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.

P29377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKKSPEEL KRIFEKYAAK EGDPDQLSKD ELKLLIQAEF PSLLKGPNTL
60 70
DDLFQELDKN GDGEVSFEEF QVLVKKISQ
Length:79
Mass (Da):9,016
Last modified:January 23, 2007 - v2
Checksum:i30416A681485B690
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791Q → S in AAA35637 (PubMed:8308886).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65869 mRNA. Translation: CAA46699.1.
L13220 mRNA. Translation: AAA35638.1.
L13042 Genomic DNA. Translation: AAA35637.1.
AL445467 Genomic DNA. Translation: CAI40084.1.
BC112174 mRNA. Translation: AAI12175.1.
CCDSiCCDS14176.1.
PIRiJN0246.
RefSeqiNP_004048.1. NM_004057.2.
UniGeneiHs.639.

Genome annotation databases

EnsembliENST00000380200; ENSP00000369547; ENSG00000169906.
GeneIDi795.
KEGGihsa:795.
UCSCiuc004cxn.1. human.

Polymorphism and mutation databases

BioMutaiS100G.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65869 mRNA. Translation: CAA46699.1.
L13220 mRNA. Translation: AAA35638.1.
L13042 Genomic DNA. Translation: AAA35637.1.
AL445467 Genomic DNA. Translation: CAI40084.1.
BC112174 mRNA. Translation: AAI12175.1.
CCDSiCCDS14176.1.
PIRiJN0246.
RefSeqiNP_004048.1. NM_004057.2.
UniGeneiHs.639.

3D structure databases

ProteinModelPortaliP29377.
SMRiP29377. Positions 5-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107246. 1 interaction.
STRINGi9606.ENSP00000369547.

PTM databases

PhosphoSiteiP29377.

Polymorphism and mutation databases

BioMutaiS100G.
DMDMi115387.

Proteomic databases

PRIDEiP29377.

Protocols and materials databases

DNASUi795.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380200; ENSP00000369547; ENSG00000169906.
GeneIDi795.
KEGGihsa:795.
UCSCiuc004cxn.1. human.

Organism-specific databases

CTDi795.
GeneCardsiGC0XP016668.
HGNCiHGNC:1436. S100G.
HPAiCAB017688.
HPA055873.
MIMi302020. gene.
neXtProtiNX_P29377.
PharmGKBiPA26028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39449.
GeneTreeiENSGT00530000064238.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP29377.
KOiK14734.
OMAiLLIQTEF.
OrthoDBiEOG7Z3F78.
PhylomeDBiP29377.
TreeFamiTF332727.

Miscellaneous databases

GeneWikiiS100G.
GenomeRNAii795.
NextBioi3230.
PROiP29377.
SOURCEiSearch...

Gene expression databases

BgeeiP29377.
CleanExiHS_S100G.
GenevestigatoriP29377.

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:SF67. PTHR11639:SF67. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
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. "Molecular cloning and chromosomal assignment of human calbindin-D9k."
    Howard A., Legon S., Spurr N.K., Walters J.R.I.
    Biochem. Biophys. Res. Commun. 185:663-669(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of the full-length cDNA encoding the human calbindin-D9k."
    Jeung E.B., Krisinger J., Dann J.L., Leung P.C.K.
    FEBS Lett. 307:224-228(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The human calbindin-D9k gene. Complete structure and implications on steroid hormone regulation."
    Jeung E.B., Leung P.C.K., Krisinger J.
    J. Mol. Biol. 235:1231-1238(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiS100G_HUMAN
AccessioniPrimary (citable) accession number: P29377
Secondary accession number(s): Q5JS49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.