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P29377 (S100G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:S100G
Synonyms:CABP9K, CALB3, S100D
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length79 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the S-100 family.

Contains 2 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Vitamin D
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular functioncalcium ion binding

Traceable author statement. Source: ProtInc

vitamin D binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7978Protein S100-G
PRO_0000144027

Regions

Domain13 – 4836EF-hand 1
Domain45 – 7935EF-hand 2
Calcium binding18 – 31141; low affinity
Calcium binding58 – 69122; high affinity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Sequence conflict791Q → S in AAA35637. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P29377 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 30416A681485B690

FASTA799,016
        10         20         30         40         50         60 
MSTKKSPEEL KRIFEKYAAK EGDPDQLSKD ELKLLIQAEF PSLLKGPNTL DDLFQELDKN 

        70 
GDGEVSFEEF QVLVKKISQ 

« Hide

References

« Hide 'large scale' references
[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: 1610358] [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: 1379540] [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: 8308886] [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. expand/collapse author list , 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: 15772651] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00303002.
PIRJN0246.
RefSeqNP_004048.1. NM_004057.2.
UniGeneHs.639.

3D structure databases

ProteinModelPortalP29377.
SMRP29377. Positions 5-79.
ModBaseSearch...

Protein-protein interaction databases

STRINGP29377.

PTM databases

PhosphoSiteP29377.

Polymorphism databases

DMDM115387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380200; ENSP00000369547; ENSG00000169906.
GeneID795.
KEGGhsa:795.
UCSCuc004cxn.1. human.

Organism-specific databases

CTD795.
GeneCardsGC0XP016668.
H-InvDBHIX0056285.
HGNCHGNC:1436. S100G.
HPACAB017688.
MIM302020. gene.
neXtProtNX_P29377.
PharmGKBPA26028.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21178.
GeneTreeENSGT00530000064238.
HOGENOMHBG716817.
HOVERGENHBG001479.
InParanoidP29377.
OMAKGPSTLD.
OrthoDBEOG4NP754.
PhylomeDBP29377.

Gene expression databases

ArrayExpressP29377.
BgeeP29377.
CleanExHS_S100G.
GenevestigatorP29377.
GermOnlineENSG00000169906. Homo sapiens.

Family and domain databases

InterProIPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
KOK14734.
PfamPF00036. efhand. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio3230.
SOURCESearch...

Entry information

Entry nameS100G_HUMAN
AccessionPrimary (citable) accession number: P29377
Secondary accession number(s): Q5JS49
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families