P31949 (S10AB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A11

Alternative name(s):
Calgizzarin
Metastatic lymph node gene 70 protein
Short name=MLN 70
Protein S100-C
S100 calcium-binding protein A11

Gene names

Name:	S100A11
Synonyms:	MLN70, S100C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	105 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Facilitates the differentiation and the cornification of keratinocytes. Ref.16
Subunit structure	Homodimer; disulfide-linked. Ref.16
Subcellular location	Cytoplasm. Nucleus Ref.16.
Post-translational modification	Phosphorylation at Thr-10 by PRKCA significantly suppresses homodimerization and promotes association with NCL/nucleolin which induces nuclear translocation.
Miscellaneous	Binds two calcium ions per molecule with an affinity similar to that of the S-100 proteins By similarity.
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Calcium
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of DNA replication Traceable author statement. Source: ProtInc negative regulation of cell proliferation Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB ruffle Inferred from direct assay. Source: UniProtKB
Molecular function	S100 beta binding Inferred from physical interaction. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent protein binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
S100B	P04271	5	EBI-701862,EBI-458391

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 105

105

Protein S100-A11

PRO_0000144009

Regions

Domain

13 – 49

37

EF-hand 1

Domain

55 – 90

36

EF-hand 2

Calcium binding

25 – 38

14

1; low affinity Potential

Calcium binding

68 – 79

12

2; high affinity Potential

Amino acid modifications

Modified residue

3

1

N6-acetyllysine Ref.14

Modified residue

6

1

Phosphoserine Ref.9 Ref.10 Ref.12

Modified residue

10

1

Phosphothreonine Ref.16

Modified residue

30

1

Phosphotyrosine Ref.11 Ref.13

Modified residue

32

1

Phosphotyrosine Ref.11

Disulfide bond

13

Interchain Ref.16

Secondary structure

1

.

.

.

105

Helix Strand Turn

Details...

Helix

7 – 18

12

Sequences

	Sequence		Length	Mass (Da)
	P31949 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 1729ED680290CFE4	FASTA	105	11,740
	10 20 30 40 50 60 MAKISSPTET ERCIESLIAV FQKYAGKDGY NYTLSKTEFL SFMNTELAAF TKNQKDPGVL 70 80 90 100 DRMMKKLDTN SDGQLDFSEF LNLIGGLAMA CHDSFLKAVP SQKRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human calgizzarin; one colorectal cancer-related gene selected by a large scale random cDNA sequencing and northern blot analysis." Tanaka M., Adzuma K., Iwami M., Yoshimoto K., Monden Y., Itakura M. Cancer Lett. 89:195-200(1995) [PubMed: 7889529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17." Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C. Genomics 28:367-376(1995) [PubMed: 7490069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary carcinoma.
[3]	"Isolation and characterization of cDNA for human S100C protein and a related gene." Nakatani K., Kato A., Sugimoto M., Kumano K., Komada T., Tsunoda H., Ito M., Nakano T., Shima T., Tanaka T. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[4]	"Molecular cloning of a human homologue of the two calcium binding protein, porcine S100 and rabbit calgizzarin." Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S., Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M., Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Placenta and Urinary bladder.
[8]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-12; 43-51 AND 56-62. Tissue: Keratinocyte.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30 AND TYR-32, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, MASS SPECTROMETRY.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"The structure of S100A11 fragment explains a local structural change induced by phosphorylation." Kouno T., Mizuguchi M., Sakaguchi M., Makino E., Mori Y., Shinoda H., Aizawa T., Demura M., Huh N.H., Kawano K. J. Pept. Sci. 14:1129-1138(2008) [PubMed: 18618420] [Abstract] Cited for: STRUCTURE BY NMR OF 1-19, DISULFIDE BOND, PHOSPHORYLATION AT THR-10, FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D38583 mRNA. Translation: BAA07597.1.
X80201 mRNA. Translation: CAA56492.1.
D49355 mRNA. Translation: BAA08354.1.
D50374 mRNA. Translation: BAA23325.1.
BT009912 mRNA. Translation: AAP88914.1.
AL591893 Genomic DNA. Translation: CAH72895.1.
BC001410 mRNA. Translation: AAH01410.1.
BC014354 mRNA. Translation: AAH14354.1.

IPI

IPI00013895.

PIR

I37080.

RefSeq

NP_005611.1. NM_005620.1.

UniGene

Hs.417004.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V4Z	NMR	-	A	1-19	[»]
1V50	NMR	-	A	1-19	[»]

ProteinModelPortal

P31949.

SMR

P31949. Positions 5-104.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31949. 7 interactions.

STRING

P31949.

PTM databases

PhosphoSite

P31949.

Polymorphism databases

DMDM

1710818.

2D gel databases

SWISS-2DPAGE

P31949.

Aarhus/Ghent-2DPAGE

4006. IEF.

DOSAC-COBS-2DPAGE

P31949.

PMMA-2DPAGE

P31949.

Proteomic databases

PeptideAtlas

P31949.

PRIDE

P31949.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000271638; ENSP00000271638; ENSG00000163191.

GeneID

6282.

KEGG

hsa:6282.

UCSC

uc001ezn.1. human.

Organism-specific databases

CTD

6282.

GeneCards

GC01M152004.

H-InvDB

HIX0001073.

HGNC

HGNC:10488. S100A11.

MIM

603114. gene.

neXtProt

NX_P31949.

PharmGKB

PA34900.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20799.

GeneTree

ENSGT00600000084283.

HOGENOM

HBG716817.

HOVERGEN

HBG001479.

InParanoid

P31949.

OMA

MSSPTET.

OrthoDB

EOG4BG8XN.

PhylomeDB

P31949.

Gene expression databases

ArrayExpress

P31949.

Bgee

P31949.

CleanEx

HS_S100A11.

Genevestigator

P31949.

GermOnline

ENSG00000163191. Homo sapiens.

Family and domain databases

InterPro

IPR018248. 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]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

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

NextBio

24385.

SOURCE

Search...

Entry information

Entry name

S10AB_HUMAN

Accession

Primary (citable) accession number: P31949
Secondary accession number(s): Q5VTK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 129 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.