P29377 (S100G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	S100G
Synonyms:	CABP9K, CALB3, S100D

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	79 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the S-100 family. Contains 2 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium Metal-binding Vitamin D
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Traceable author statement Ref.1. Source: ProtInc vitamin D binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 79	78	Protein S100-G		PRO_0000144027
Regions
	Domain	13 – 48	36	EF-hand 1
	Domain	45 – 79	35	EF-hand 2
	Calcium binding	18 – 31	14	1; low affinity
	Calcium binding	58 – 69	12	2; high affinity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
Experimental info
	Sequence conflict	79	1	Q → S in AAA35637. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P29377 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 30416A681485B690	FASTA	79	9,016
	10 20 30 40 50 60 MSTKKSPEEL KRIFEKYAAK EGDPDQLSKD ELKLLIQAEF PSLLKGPNTL DDLFQELDKN 70 GDGEVSFEEF QVLVKKISQ

References

	« Hide 'large scale' referencesShow '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] [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].
+	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.
IPI	IPI00303002.
PIR	JN0246.
RefSeq	NP_004048.1. NM_004057.2.
UniGene	Hs.639.
3D structure databases
ProteinModelPortal	P29377.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000369547.
PTM databases
PhosphoSite	P29377.
Polymorphism databases
DMDM	115387.
Proteomic databases
PRIDE	P29377.
Protocols and materials databases
DNASU	795.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380200; ENSP00000369547; ENSG00000169906.
GeneID	795.
KEGG	hsa:795.
UCSC	uc004cxn.1. human.
Organism-specific databases
CTD	795.
GeneCards	GC0XP016668.
HGNC	HGNC:1436. S100G.
HPA	CAB017688.
MIM	302020. gene.
neXtProt	NX_P29377.
PharmGKB	PA26028.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39449.
HOGENOM	HOG000246968.
HOVERGEN	HBG001479.
InParanoid	P29377.
KO	K14734.
OMA	KGPSTLD.
OrthoDB	EOG4NP754.
PhylomeDB	P29377.
Gene expression databases
Bgee	P29377.
CleanEx	HS_S100G.
Genevestigator	P29377.
GermOnline	ENSG00000169906. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR001751. S100/CaBP-9k_CS. IPR013787. S100_Ca-bd_sub. [Graphical view]
Pfam	PF00036. efhand. 1 hit. PF01023. S_100. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS00303. S100_CABP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	795.
NextBio	3230.
SOURCE	Search...

Entry information

Entry name

S100G_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.