P60903 (S10AA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A10

Alternative name(s):
Calpactin I light chain
Calpactin-1 light chain
Cellular ligand of annexin II
S100 calcium-binding protein A10
p10 protein
p11

Gene names

Name:	S100A10
Synonyms:	ANX2LG, CAL1L, CLP11

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	97 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)

Function	Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.
Subunit structure	Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with SCN10A By similarity.
Miscellaneous	Does not appear to bind calcium. Contains 2 ancestral calcium site related to EF-hand domains that have lost their ability to bind calcium.
Sequence similarities	Belongs to the S-100 family.

Ontologies

Keywords
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to acid Inferred from electronic annotation. Source: Compara positive regulation of binding Inferred from electronic annotation. Source: Compara signal transduction Non-traceable author statement Ref.1. Source: ProtInc
Cellular_component	extrinsic to plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro receptor binding Non-traceable author statement Ref.1. Source: ProtInc
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 – 97

96

Protein S100-A10

PRO_0000144002

Regions

Region

60 – 71

12

Ancestral calcium site

Amino acid modifications

Modified residue

23

1

N6-acetyllysine Ref.7

Modified residue

28

1

N6-acetyllysine Ref.7

Modified residue

37

1

N6-acetyllysine Ref.7

Modified residue

54

1

N6-acetyllysine Ref.7

Modified residue

57

1

N6-acetyllysine Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

97

Helix Strand Turn

Details...

Helix

4 – 20

17

Helix

21 – 23

3

Helix

28 – 38

11

Helix

40 – 45

6

Helix

51 – 59

9

Beta strand

63 – 65

3

Helix

69 – 90

22

Sequences

	Sequence		Length	Mass (Da)
	P60903 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3E8E03A6E7DD7A8D	FASTA	97	11,203
	10 20 30 40 50 60 MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD 70 80 90 QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II." Kube E., Weber K., Gerke V. Gene 102:255-259(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family." Harder T., Kube E., Gerke V. Gene 113:269-274(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"cDNA sequence of human p11 calpactin I light chain." Dooley T.P., Weiland K.L., Simon M. Genomics 13:866-868(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Brain.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-28; LYS-37; LYS-54 AND LYS-57, MASS SPECTROMETRY.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"The crystal structure of a complex of p11 with the annexin II N-terminal peptide." Rety S., Sopkova J., Renouard M., Osterloh D., Gerke V., Tabaries S., Russo-Marie F., Lewit-Bentley A. Nat. Struct. Biol. 6:89-95(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M81457 mRNA. Translation: AAA58404.1.
M38591 mRNA. Translation: AAA58426.1.
M77483 Genomic DNA. No translation available.
AK291073 mRNA. Translation: BAF83762.1.
AL450992 Genomic DNA. Translation: CAI12164.1.
BC015973 mRNA. Translation: AAH15973.1.
BC105786 mRNA. Translation: AAI05787.1.

IPI

IPI00183695.

PIR

JC1139.

RefSeq

NP_002957.1. NM_002966.2.

UniGene

Hs.143873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4P	X-ray	2.25	A/B	2-97	[»]
1BT6	X-ray	2.40	A/B	2-97	[»]
4DRW	X-ray	3.50	A/B/C/D	1-93	[»]
4FTG	X-ray	2.51	A/B	2-97	[»]
4HRE	X-ray	2.79	E/F/I/J	2-97	[»]
4HRG	X-ray	2.00	A/B	1-93	[»]
4HRH	X-ray	3.00	A/B	1-93	[»]

ProteinModelPortal

P60903.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60903. 3 interactions.

MINT

MINT-1178035.

STRING

9606.ENSP00000357799.

PTM databases

PhosphoSite

P60903.

Polymorphism databases

DMDM

46397706.

2D gel databases

SWISS-2DPAGE

P60903.

Proteomic databases

PaxDb

P60903.

PeptideAtlas

P60903.

PRIDE

P60903.

Protocols and materials databases

DNASU

6281.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368809; ENSP00000357799; ENSG00000197747.
ENST00000368811; ENSP00000357801; ENSG00000197747.

GeneID

6281.

KEGG

hsa:6281.

UCSC

uc001ezl.3. human.

Organism-specific databases

CTD

6281.

GeneCards

GC01M151955.

HGNC

HGNC:10487. S100A10.

HPA

CAB025484.
HPA003340.

MIM

114085. gene.

neXtProt

NX_P60903.

PharmGKB

PA34899.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG26977.

HOVERGEN

HBG001479.

InParanoid

P60903.

OMA

AMETLMF.

OrthoDB

EOG4DNF5Z.

PhylomeDB

P60903.

Gene expression databases

ArrayExpress

P60903.

Bgee

P60903.

CleanEx

HS_S100A10.

Genevestigator

P60903.

GermOnline

ENSG00000197747. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00303. S100_CABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P60903.

ChEMBL

CHEMBL1764939.

ChiTaRS

S100A10. human.

EvolutionaryTrace

P60903.

GenomeRNAi

6281.

NextBio

24381.

SOURCE

Search...

Entry information

Entry name

S10AA_HUMAN

Accession

Primary (citable) accession number: P60903
Secondary accession number(s): A8K4V8, P08206, Q5T1C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 98 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.