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Reviewed, UniProtKB/Swiss-Prot P29377 (S100G_HUMAN)

Last modified March 2, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Protein S100-G
Alternative name(s):
S100 calcium-binding protein G
Vitamin D-dependent calcium-binding protein, intestinal
Short name=CABP
Calbindin-D9k
Gene names
Name:S100G
Synonyms:CABP9K, CALB3, S100D
OrganismHomo sapiens (Human) [Complete proteome]
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
Gene Ontology (GO)
   Molecular functioncalcium ion binding Ref.1

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
P29377-1 [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.
UniGeneHs.639

3D structure databases

SMRP29377. Positions 2-79.
ModBaseSearch...

Protein-protein interaction databases

STRINGP29377.

Genome annotation databases

EnsemblENST00000380200; ENSP00000369547; ENSG00000169906; Homo sapiens. [Genome view]
GeneID795.
KEGGhsa:795.
UCSCuc004cxn.1. human.

Organism-specific databases

CTD795.
GeneCardsGC0XP016578.
HGNCHGNC:1436. S100G.
HPACAB017688.
MIM302020. gene.
PharmGKBPA26028.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21178.
HOGENOMHBG716817.
HOVERGENHBG001479.
InParanoidP29377.
OMAKGPSTLD.
OrthoDBEOG9RV59H.
PhylomeDBP29377.

Gene expression databases

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

Family and domain databases

InterProIPR011992. 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.
PfamPF01023. 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 Resources

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: March 2, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents