Reviewed, UniProtKB/Swiss-Prot P06702 (S10A9_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein S100-A9
Alternative name(s):
    S100 calcium-binding protein A9
    Calgranulin-B
    Migration inhibitory factor-related protein 14
      Short name=MRP-14
      Short name=p14
    Leukocyte L1 complex heavy chain
    Calprotectin L1H subunit

Gene names

Name:	S100A9
Synonyms:	CAGB, CFAG, MRP14

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	114 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	Calcium-binding protein. Has antimicrobial activity towards bacteria and fungi. Important for resistance to invasion by pathogenic bacteria. Up-regulates transcription of genes that are under the control of NF-kappa-B. Plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS) By similarity. Promotes tubulin polymerization when unphosphorylated. Promotes phagocyte migration and infiltration of granulocytes at sites of wounding. Plays a role as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1. Extracellular calprotectin binds to target cells and promotes apoptosis. Antimicrobial and proapoptotic activity is inhibited by zinc ions. Ref.11 Ref.14 Ref.15 Ref.16 Ref.20 Ref.21 Ref.23
Subunit structure	Homodimer. Heterotetramer with S100A8. Component of the heterotetrameric calprotectin complex containing two copies each of S100A8 and S100A9. Interacts with CEACAM3 and tubulin filaments in a calcium-dependent manner. Heterotetrameric calprotectin interacts with ANXA6 and associates with tubulin filaments in activated monocytes. May interact with components of the intermediate filaments in monocytes and epithelial cells. The homodimer interacts with AGER and with the heterodimeric complex formed by TLR4 and LY96 in the presence of calcium and/or zinc ions. The homodimer binds quinoline-3-carboxamides in the presence of calcium and/or zinc ions. Ref.14 Ref.16 Ref.20 Ref.21 Ref.23 Ref.12 Ref.13 Ref.17 Ref.24 Ref.25
Subcellular location	Secreted. Cytoplasm. Cytoplasm › cytoskeleton. Cell membrane; Peripheral membrane protein. Note: Associates with tubulin filaments in activated monocytes. Targeted to the cell surface upon calcium influx. Released from blood leukocytes upon exposure to CSF2/GM-CSF, bacterial lipopolysaccharide (LPS) and during inflammatory processes. Serum levels are high in patients suffering from chronic inflammation. Ref.11 Ref.15 Ref.23 Ref.12 Ref.17
Tissue specificity	Expressed by macrophages in acutely inflammed tissues and in chronic inflammation. Detected in peripheral blood leukocytes, in neutrophils and granulocytes. Detected at sites of vascular inflammation (at protein level). Also expressed in epithelial cells constitutively or induced during dermatoses. Ref.11 Ref.15 Ref.12 Ref.1 Ref.2
Post-translational modification	Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization. Ref.14 Ref.8 Ref.18 Ref.19
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.
Mass spectrometry	Molecular mass is 13115 Da from positions 2 - 114. Determined by MALDI. Ref.24

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium
Molecular function	Antimicrobial
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-cell signaling Ref.1 Traceable author statement. Source: ProtInc chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct signal transducer activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-1055001,EBI-743313
ARRB2	P32121	1	EBI-1055001,EBI-714559
ILK	Q13418	1	EBI-1055001,EBI-747644
NUAK1	O60285	1	EBI-1055001,EBI-1046789
PAK7	Q9P286	1	EBI-1055001,EBI-1051061
TAGLN	Q01995	1	EBI-1055001,EBI-1054248
USF2	Q15853	1	EBI-1055001,EBI-1055994

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 114

113

Protein S100-A9

PRO_0000143997

Regions

Domain

12 – 47

36

EF-hand 1

Domain

54 – 89

36

EF-hand 2

Calcium binding

23 – 36

14

1; low affinity

Calcium binding

67 – 78

12

2; high affinity Probable

Amino acid modifications

Modified residue

2

1

Blocked amino end (Thr)

Modified residue

113

1

Phosphothreonine Ref.8 Ref.18 Ref.19

Natural variations

Natural variant

20

1

H → R

VAR_013008

Experimental info

Mutagenesis

36

1

E → Q: Loss of resistance to bacterial invasion; when associated with Q-78. Ref.21

Mutagenesis

63

1

M → A: Loss of antifungal activity. Ref.20

Mutagenesis

78

1

E → Q: Loss of resistance to bacterial invasion; when associated with Q-36. Ref.21

Mutagenesis

81

1

M → A: No effect on antifungal activity. Ref.20

Mutagenesis

83

1

M → A: Loss of antifungal activity. Ref.20

Sequence conflict

6

1

S → H AA sequence Ref.11

Sequence conflict

25

1

K → F AA sequence Ref.11

Sequence conflict

28

1

H → L AA sequence Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

114

Helix Strand Turn

Details...

Helix

7 – 23

17

Beta strand

25 – 28

4

Helix

34 – 44

11

Turn

46 – 51

6

Helix

52 – 54

3

Helix

56 – 66

11

Helix

76 – 79

4

Helix

81 – 85

5

Helix

87 – 91

5

Sequences

	Sequence		Length	Mass (Da)
	P06702-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: C3BE19729E14C078	FASTA	114	13,242
	10 20 30 40 50 60 MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE 70 80 90 100 110 HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis." Odink K., Cerletti N., Bruggen J., Clerc R.G., Tarcsay L., Zwaldo G., Gerhards G., Schlegel R., Sorg C. Nature 330:80-82(1987) [PubMed: 3313057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation." Lagasse E., Clerc R.G. Mol. Cell. Biol. 8:2402-2410(1988) [PubMed: 3405210] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[3]	"A protein containing the cystic fibrosis antigen is an inhibitor of protein kinases." Murao S., Collart F.R., Huberman E. J. Biol. Chem. 264:8356-8360(1989) [PubMed: 2656677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BLOCKAGE OF N-TERMINUS.
[4]	"Human gene for migration inhibitory factor-related protein 14 (MRP14), variant allele." Wang M., Xu X., Cai Y., Xu H., Han Y., Xu Z., Wu M. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-20.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) 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: Lung.
[8]	"Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14." Edgeworth J., Freemont P., Hogg N. Nature 342:189-192(1989) [PubMed: 2478889] [Abstract] Cited for: PROTEIN SEQUENCE OF 84-114, PHOSPHORYLATION AT THR-113.
[9]	"Amino acid sequences of 60B8 antigens induced in HL-60 cells by 1,25-dihydroxyvitamin D3. The antigens are identical with macrophage-related protein-14 and -8." Tobe T., Murakami K., Tomita M., Nozawa R. Chem. Pharm. Bull. 37:1576-1580(1989) [PubMed: 2776242] [Abstract] Cited for: PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS.
[10]	"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 11-19; 26-37 AND 94-107. Tissue: Keratinocyte.
[11]	"In vitro antimicrobial activity of the human neutrophil cytosolic S-100 protein complex, calprotectin, against Capnocytophaga sputigena." Miyasaki K.T., Bodeau A.L., Murthy A.R., Lehrer R.I. J. Dent. Res. 72:517-523(1993) [PubMed: 8423249] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-34, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CALPROTECTIN COMPLEX, FUNCTION, TISSUE SPECIFICITY.
[12]	"Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway." Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., Sorg C. J. Biol. Chem. 272:9496-9502(1997) [PubMed: 9083090] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
[13]	"The microbial receptor CEACAM3 is linked to the calprotectin complex in granulocytes." Streichert T., Ebrahimnejad A., Ganzer S., Flayeh R., Wagener C., Bruemmer J. Biochem. Biophys. Res. Commun. 289:191-197(2001) [PubMed: 11708798] [Abstract] Cited for: INTERACTION WITH CEACAM3.
[14]	"MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes." Vogl T., Ludwig S., Goebeler M., Strey A., Thorey I.S., Reichelt R., Foell D., Gerke V., Manitz M.P., Nacken W., Werner S., Sorg C., Roth J. Blood 104:4260-4268(2004) [PubMed: 15331440] [Abstract] Cited for: FUNCTION, INTERACTION WITH TUBULIN, PHOSPHORYLATION.
[15]	"Myeloid-related proteins 8 and 14 induce a specific inflammatory response in human microvascular endothelial cells." Viemann D., Strey A., Janning A., Jurk K., Klimmek K., Vogl T., Hirono K., Ichida F., Foell D., Kehrel B., Gerke V., Sorg C., Roth J. Blood 105:2955-2962(2005) [PubMed: 15598812] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]	"Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity." Nakatani Y., Yamazaki M., Chazin W.J., Yui S. Mediators Inflamm. 2005:280-292(2005) [PubMed: 16258195] [Abstract] Cited for: FUNCTION, INHIBITION BY ZINC IONS, SUBUNIT.
[17]	"Interaction between S100A8/A9 and annexin A6 is involved in the calcium-induced cell surface exposition of S100A8/A9." Bode G., Lueken A., Kerkhoff C., Roth J., Ludwig S., Nacken W. J. Biol. Chem. 283:31776-31784(2008) [PubMed: 18786929] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ANXA6.
[18]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, MASS SPECTROMETRY. Tissue: Liver.
[19]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"Substitution of methionine 63 or 83 in S100A9 and cysteine 42 in S100A8 abrogate the antifungal activities of S100A8/A9: potential role for oxidative regulation." Sroussi H.Y., Koehler G.A., Agabian N., Villines D., Palefsky J.M. FEMS Immunol. Med. Microbiol. 55:55-61(2009) [PubMed: 19087201] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF MET-63; MET-81 AND MET-83, INHIBITION BY ZINC IONS.
[21]	"Calprotectin S100A9 calcium-binding loops I and II are essential for keratinocyte resistance to bacterial invasion." Champaiboon C., Sappington K.J., Guenther B.D., Ross K.F., Herzberg M.C. J. Biol. Chem. 284:7078-7090(2009) [PubMed: 19122197] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-36 AND GLU-78.
[22]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, MASS SPECTROMETRY.
[23]	"Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides." Bjoerk P., Bjoerk A., Vogl T., Stenstroem M., Liberg D., Olsson A., Roth J., Ivars F., Leanderson T. PLoS Biol. 7:E97-E97(2009) [PubMed: 19402754] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4; LY96 AND AGER, QUINOLINE-3-CARBOXAMIDE BINDING.
[24]	"The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process." Itou H., Yao M., Fujita I., Watanabe N., Suzuki M., Nishihira J., Tanaka I. J. Mol. Biol. 316:265-276(2002) [PubMed: 11851337] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, MASS SPECTROMETRY, SUBUNIT.
[25]	"The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins." Korndoerfer I.P., Brueckner F., Skerra A. J. Mol. Biol. 370:887-898(2007) [PubMed: 17553524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-114 IN COMPLEX WITH S100A8, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06233 mRNA. Translation: CAA29579.1.
M21064 Genomic DNA. Translation: AAA36326.1.
M26311 mRNA. Translation: AAA68480.1.
AF237581 Genomic DNA. Translation: AAF62536.1.
AF237582 Genomic DNA. Translation: AAF62537.1.
CR542207 mRNA. Translation: CAG47003.1.
CR542224 mRNA. Translation: CAG47020.1.
AL591704 Genomic DNA. Translation: CAI19494.1.
BC047681 mRNA. Translation: AAH47681.1.

IPI

IPI00027462.

PIR

B31848.

RefSeq

NP_002956.1.

UniGene

Hs.112405

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IRJ	X-ray	2.10	A/B/C/D/E/F/G/H	2-114	[»]
1XK4	X-ray	1.80	C/D/G/H/K/L	4-114	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1166N.

IntAct

P06702. 15 interactions.

STRING

P06702.

PTM databases

PhosphoSite

P06702.

2-D gel databases

SWISS-2DPAGE

P06702.

Aarhus/Ghent-2DPAGE

5007. IEF.
6010. IEF.
6017. IEF.
7013. IEF.

OGP

P06702.

PMMA-2DPAGE

P06702.

Proteomic databases

PeptideAtlas

P06702.

PRIDE

P06702.

Genome annotation databases

Ensembl

ENST00000368738; ENSP00000357727; ENSG00000163220; Homo sapiens. [Genome view]

GeneID

6280.

KEGG

hsa:6280.

UCSC

uc001fbq.1. human.

Organism-specific databases

CTD

6280.

GeneCards

GC01P151596.

H-InvDB

HIX0023536.

HGNC

HGNC:10499. S100A9.

HPA

CAB009441.
HPA004193.

MIM

123886. gene.

PharmGKB

PA34911.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20489.

HOGENOM

HBG716817.

HOVERGEN

P06702.

InParanoid

P06702.

OMA

VASHEEM.

OrthoDB

EOG9TB6WH.

PhylomeDB

P06702.

Gene expression databases

ArrayExpress

P06702.

Bgee

P06702.

CleanEx

HS_S100A9.

Genevestigator

P06702.

GermOnline

ENSG00000163220. Homo sapiens.

Family and domain databases

InterPro

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

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 Resources

NextBio

24377.

SOURCE

Search...

Entry information

Entry name

S10A9_HUMAN

Accession

Primary (citable) accession number: P06702
Secondary accession number(s): Q6FGA1, Q9NYM0, Q9UCJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	February 9, 2010
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.