P05109 (S10A8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A8

Alternative name(s):
Calgranulin-A
Calprotectin L1L subunit
Cystic fibrosis antigen
Short name=CFAG
Leukocyte L1 complex light chain
Migration inhibitory factor-related protein 8
Short name=MRP-8
Short name=p8
S100 calcium-binding protein A8
Urinary stone protein band A

Gene names

Name:	S100A8
Synonyms:	CAGA, CFAG, MRP8

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	93 AA.
Sequence status	Complete.
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. Promotes phagocyte migration and infiltration of granulocytes at sites of wounding. Plays a role as 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.18 Ref.19 Ref.20 Ref.22 Ref.23
Subunit structure	Homodimer. Heterotetramer with S100A9. Component of the heterotetrameric calprotectin complex containing two copies each of S100A8 and S100A9. Interacts with AGER and with the heterodimeric complex formed by TLR4 and LY96. 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. Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.26
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.17 Ref.19 Ref.21
Tissue specificity	Expressed by macrophages in chronic inflammations. Also expressed in epithelial cells constitutively or induced during dermatoses. Ref.17 Ref.19
Miscellaneous	Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins.
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Secreted
Domain	Repeat
Ligand	Calcium
Molecular function	Antimicrobial
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
S100A9	P06702	3	EBI-355281,EBI-1055001

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 93

93

Protein S100-A8

PRO_0000143993

Regions

Domain

12 – 47

36

EF-hand 1

Domain

46 – 81

36

EF-hand 2

Calcium binding

20 – 33

14

1; low affinity

Calcium binding

59 – 70

12

2; high affinity

Experimental info

Mutagenesis

42

1

C → A: Loss of antifungal activity. Ref.22

Sequence conflict

80 – 93

14

VAAHK…ESHKE → WQPTKKAMKKATKSS in CAA68390. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

93

Helix Strand Turn

Details...

Helix

4 – 20

17

Beta strand

22 – 25

4

Helix

31 – 41

11

Helix

44 – 47

4

Helix

51 – 58

8

Beta strand

63 – 66

4

Helix

68 – 86

19

Sequences

	Sequence		Length	Mass (Da)
	P05109 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 78F589140B9CE166	FASTA	93	10,835
	10 20 30 40 50 60 MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI 70 80 90 NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene." Dorin J.R., Novak M., Hill R.E., Brock D.J.H., Secher D.S., van Heyningen V. Nature 326:614-617(1987) [PubMed: 3561500] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[3]	"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].
[4]	"The calcium-binding protein MRP-8 is produced by human pulmonary tumor cells." Schaefer T., Sachse G.E., Gassen H.G. Biol. Chem. Hoppe-Seyler 372:1-4(1991) [PubMed: 2039599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"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].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: Skeletal muscle.
[11]	"Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin." Marti T., Erttmann K.D., Gallin M.Y. Biochem. Biophys. Res. Commun. 221:454-458(1996) [PubMed: 8619876] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19; 24-35 AND 63-89.
[12]	"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 1-27.
[13]	"Translocation of a small cytosolic calcium-binding protein (MRP-8) to plasma membrane correlates with human neutrophil activation." Lemarchand P., Vaglio M., Mauel J., Markert M. J. Biol. Chem. 267:19379-19382(1992) [PubMed: 1326551] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25. Tissue: Neutrophil.
[14]	"Calprotectin-like protein is related to soluble organic matrix in calcium oxalate urinary stone." Umekawa T., Kurita T. Biochem. Mol. Biol. Int. 34:309-313(1994) [PubMed: 7849642] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20.
[15]	"Isolation of an ascitic oncodevelopmental protein exhibiting high sequence homology with calcium-binding protein MRP8." Nakai M., Ishikawa M., Hamada Y., Sugano S. Biol. Chem. Hoppe-Seyler 375:789-792(1994) [PubMed: 7695842] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Tissue: Ascites.
[16]	"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 38-47 AND 50-56. Tissue: Keratinocyte.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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, MUTAGENESIS OF CYS-42.
[23]	"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.
[24]	"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].
[25]	"The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution." Ishikawa K., Nakagawa A., Tanaka I., Suzuki M., Nishihira J. Acta Crystallogr. D 56:559-566(2000) [PubMed: 10771424] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[26]	"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) IN COMPLEX WITH S100A9, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00278 mRNA. Translation: CAA68390.1.
X06234 mRNA. Translation: CAA29580.1.
M21005 Genomic DNA. Translation: AAA36327.1.
AK291328 mRNA. Translation: BAF84017.1.
CR407674 mRNA. Translation: CAG28602.1.
BT007378 mRNA. Translation: AAP36042.1.
AL591704 Genomic DNA. Translation: CAI19497.1.
CH471121 Genomic DNA. Translation: EAW53330.1.
CH471121 Genomic DNA. Translation: EAW53331.1.
BC005928 mRNA. Translation: AAH05928.1.

IPI

IPI00007047.

PIR

BCHUCF. A31848.

RefSeq

NP_002955.2. NM_002964.4.

UniGene

Hs.416073.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MR8	X-ray	1.90	A/B	1-93	[»]
1XK4	X-ray	1.80	A/B/E/F/I/J	1-93	[»]

ProteinModelPortal

P05109.

SMR

P05109. Positions 1-90.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1165N.

IntAct

P05109. 24 interactions.

MINT

MINT-1151603.

STRING

P05109.

Polymorphism databases

DMDM

115442.

2D gel databases

SWISS-2DPAGE

P05109.

Aarhus/Ghent-2DPAGE

1003. IEF.

PMMA-2DPAGE

P05109.

Proteomic databases

PeptideAtlas

P05109.

PRIDE

P05109.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368732; ENSP00000357721; ENSG00000143546.
ENST00000368733; ENSP00000357722; ENSG00000143546.

GeneID

6279.

KEGG

hsa:6279.

UCSC

uc001fbs.1. human.

Organism-specific databases

CTD

6279.

GeneCards

GC01M153362.

H-InvDB

HIX0001079.

HGNC

HGNC:10498. S100A8.

HPA

CAB002791.
HPA024372.

MIM

123885. gene.

neXtProt

NX_P05109.

PharmGKB

PA34910.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21380.

GeneTree

ENSGT00590000083207.

HOVERGEN

HBG001479.

InParanoid

P05109.

OMA

KDADTWF.

OrthoDB

EOG4V9TS7.

PhylomeDB

P05109.

Gene expression databases

ArrayExpress

P05109.

Bgee

P05109.

CleanEx

HS_S100A8.

Genevestigator

P05109.

GermOnline

ENSG00000143546. 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

NextBio

24373.

SOURCE

Search...

Entry information

Entry name

S10A8_HUMAN

Accession

Primary (citable) accession number: P05109
Secondary accession number(s): A8K5L3 , D3DV37, Q5SY70, Q9UC84, Q9UC92, Q9UCJ0, Q9UCM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 1, 1988
Last modified:	January 25, 2012
This is version 132 of the entry and version 1 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.