P21399 (ACOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic aconitate hydratase
Short name=Aconitase
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase
Ferritin repressor protein
Iron regulatory protein 1
Short name=IRP1
Iron-responsive element-binding protein 1
Short name=IRE-BP 1

Gene names

Name:	ACO1
Synonyms:	IREB1

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	889 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding. Ref.8 Ref.9 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity. Ref.8 Ref.9
Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit. Ref.14
Subunit structure	Interacts (when associated with the 4Fe-4S) with FBXL5. Interacts with frataxin(81-210). Ref.10 Ref.11 Ref.12
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding RNA-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: Compara citrate metabolic process Inferred from direct assay Ref.9. Source: UniProtKB intestinal absorption Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of translation Inferred from electronic annotation. Source: Compara response to iron(II) ion Inferred from direct assay Ref.9. Source: UniProtKB tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 16144863. Source: MGI cytosol Inferred from direct assay PubMed 16527810. Source: HGNC endoplasmic reticulum Inferred from direct assay PubMed 16144863. Source: MGI mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay Ref.14. Source: UniProtKB aconitate hydratase activity Inferred from direct assay Ref.8Ref.9. Source: UniProtKB citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC iron-responsive element binding Inferred from direct assay Ref.9. Source: UniProtKB isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NEB	P20929	2	EBI-2847111,EBI-1049657
SGCG	Q13326	2	EBI-2847111,EBI-5357343

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 889

889

Cytoplasmic aconitate hydratase

PRO_0000076680

Regions

Region

205 – 207

3

Substrate binding By similarity

Region

779 – 780

2

Substrate binding By similarity

Sites

Metal binding

437

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

503

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

506

1

Iron-sulfur (4Fe-4S) By similarity

Binding site

86

1

Substrate By similarity

Binding site

536

1

Substrate By similarity

Binding site

541

1

Substrate By similarity

Binding site

699

1

Substrate By similarity

Natural variations

Natural variant

395

1

A → D.
Corresponds to variant rs3814519 [ dbSNP | Ensembl ].

VAR_048180

Natural variant

486

1

G → R.
Corresponds to variant rs34630459 [ dbSNP | Ensembl ].

VAR_048181

Experimental info

Mutagenesis

300

1

C → S: No effect on aconitase activity or on RNA binding. Ref.9

Mutagenesis

437

1

C → S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels. Ref.9

Mutagenesis

503

1

C → S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels. Ref.9

Mutagenesis

506

1

C → S: Loss of aconitase activity. Leads of iron levels. Ref.9

Mutagenesis

536

1

R → Q: Strongly reduced RNA binding. Ref.9

Mutagenesis

541

1

R → Q: Strongly reduced RNA binding. Ref.9

Mutagenesis

699

1

R → K: No effect on RNA binding. Ref.9

Mutagenesis

778

1

S → A: No effect on iron-regulated RNA binding. Loss of aconitase activity. Ref.9

Mutagenesis

780

1

R → Q: Nearly abolishes RNA binding. Ref.9

Secondary structure

1

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889

Helix Strand Turn

Details...

Helix

6 – 8

3

Beta strand

9 – 12

4

Beta strand

20 – 22

3

Helix

24 – 27

4

Helix

32 – 34

3

Helix

37 – 48

12

Beta strand

52 – 55

4

Helix

57 – 64

8

Helix

66 – 69

4

Turn

70 – 73

4

Beta strand

75 – 78

4

Beta strand

81 – 86

6

Helix

87 – 106

20

Helix

111 – 113

3

Beta strand

120 – 123

4

Helix

138 – 163

26

Beta strand

167 – 170

4

Helix

177 – 183

7

Beta strand

188 – 192

5

Beta strand

195 – 198

4

Beta strand

200 – 205

6

Helix

206 – 214

9

Beta strand

217 – 220

4

Helix

223 – 230

8

Beta strand

235 – 238

4

Beta strand

242 – 249

8

Helix

257 – 271

15

Beta strand

277 – 282

6

Helix

283 – 285

3

Helix

290 – 298

9

Helix

300 – 303

4

Beta strand

306 – 309

4

Helix

314 – 322

9

Helix

327 – 340

14

Helix

349 – 351

3

Beta strand

356 – 362

7

Helix

363 – 365

3

Beta strand

368 – 371

4

Beta strand

379 – 381

3

Helix

382 – 384

3

Helix

385 – 394

10

Helix

406 – 408

3

Beta strand

412 – 417

6

Beta strand

420 – 425

6

Beta strand

428 – 434

7

Helix

437 – 440

4

Helix

443 – 458

16

Beta strand

467 – 471

5

Helix

476 – 484

9

Helix

488 – 493

6

Beta strand

501 – 503

3

Helix

504 – 507

4

Helix

515 – 524

10

Beta strand

529 – 535

7

Turn

539 – 541

3

Beta strand

547 – 551

5

Helix

554 – 563

10

Beta strand

564 – 566

3

Turn

570 – 572

3

Beta strand

575 – 578

4

Turn

579 – 581

3

Beta strand

582 – 584

3

Helix

586 – 589

4

Helix

593 – 603

11

Helix

606 – 613

8

Turn

614 – 618

5

Helix

621 – 625

5

Helix

647 – 649

3

Beta strand

662 – 671

10

Helix

677 – 680

4

Beta strand

688 – 690

3

Helix

691 – 698

8

Helix

703 – 705

3

Helix

710 – 712

3

Helix

716 – 721

6

Turn

722 – 724

3

Turn

732 – 734

3

Beta strand

735 – 737

3

Beta strand

739 – 742

4

Turn

744 – 746

3

Beta strand

749 – 751

3

Helix

752 – 761

10

Beta strand

766 – 769

4

Beta strand

772 – 774

3

Helix

782 – 789

8

Beta strand

792 – 798

7

Helix

802 – 810

9

Beta strand

814 – 818

5

Helix

824 – 827

4

Beta strand

835 – 837

3

Beta strand

848 – 853

6

Beta strand

858 – 863

6

Helix

868 – 876

9

Helix

879 – 888

10

Sequences

	Sequence		Length	Mass (Da)
	P21399 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: E1A05AF701D46DCB	FASTA	889	98,399
	10 20 30 40 50 60 MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC DEFLVKKQDI 70 80 90 100 110 120 ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPVCPA 130 140 150 160 170 180 DLVIDHSIQV DFNRRADSLQ KNQDLEFERN RERFEFLKWG SQAFHNMRII PPGSGIIHQV 190 200 210 220 230 240 NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP 250 260 270 280 290 300 QVIGYRLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 310 320 330 340 350 360 PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS QDPDFTQVVE 370 380 390 400 410 420 LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPEHHN DHKTFIYDNT 430 440 450 460 470 480 EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY 490 500 510 520 530 540 YLQESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG 550 560 570 580 590 600 RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE 610 620 630 640 650 660 RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE NLTLDLQPPK 670 680 690 700 710 720 SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAVMA 730 740 750 760 770 780 RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR 790 800 810 820 830 840 DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP 850 860 870 880 ENLKPQMKVQ VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation." Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C., Kuehn L. Nucleic Acids Res. 20:33-39(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NHLBI resequencing and genotyping service (RS&G) Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[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]. Tissue: Uterus.
[6]	"Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein." Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J., Samaniego F., McBride O.W., Harford J.B., Klausner R.D. Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, RNA-BINDING, PARTIAL PROTEIN SEQUENCE.
[7]	"Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase." Hentze M.W., Argos P. Nucleic Acids Res. 19:1739-1740(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SIMILARITY TO ACONITASES AND IPM ISOMERASES.
[8]	"A regulated RNA binding protein also possesses aconitase activity." Kaptain S., Downey W.E., Tang C.K., Philpott C., Haile D.J., Orloff D.G., Harford J.B., Rouault T.A., Klausner R.D. Proc. Natl. Acad. Sci. U.S.A. 88:10109-10113(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ACONITASE.
[9]	"The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation." Philpott C.C., Klausner R.D., Rouault T.A. Proc. Natl. Acad. Sci. U.S.A. 91:7321-7325(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-300; CYS-437; CYS-503; CYS-506; ARG-536; ARG-541; ARG-699; SER-778 AND ARG-780.
[10]	"Control of iron homeostasis by an iron-regulated ubiquitin ligase." Vashisht A.A., Zumbrennen K.B., Huang X., Powers D.N., Durazo A., Sun D., Bhaskaran N., Persson A., Uhlen M., Sangfelt O., Spruck C., Leibold E.A., Wohlschlegel J.A. Science 326:718-721(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
[11]	"An E3 ligase possessing an iron responsive hemerythrin domain is a regulator of iron homeostasis." Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q., Grishin N.V., Bruick R.K. Science 326:722-726(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
[12]	"Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin." Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R. Hum. Mol. Genet. 19:1221-1229(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FRATAXIN(81-210).
[13]	"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].
[14]	"Crystal structure of human iron regulatory protein 1 as cytosolic aconitase." Dupuy J., Volbeda A., Carpentier P., Darnault C., Moulis J.-M., Fontecilla-Camps J.C. Structure 14:129-139(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
+	Additional computationally mapped references.

Web resources

Wikipedia

Aconitase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z11559 mRNA. Translation: CAA77651.1.
DQ496106 Genomic DNA. Translation: ABF47095.1.
AL161783 Genomic DNA. Translation: CAH72598.1.
CH471071 Genomic DNA. Translation: EAW58549.1.
CH471071 Genomic DNA. Translation: EAW58550.1.
CH471071 Genomic DNA. Translation: EAW58552.1.
BC018103 mRNA. Translation: AAH18103.1.
M58510 mRNA. Translation: AAA69900.1.

IPI

IPI00008485.

PIR

S26403.

RefSeq

NP_002188.1. NM_002197.2.

UniGene

Hs.567229.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B3X	X-ray	2.54	A	2-889	[»]
2B3Y	X-ray	1.85	A/B	2-889	[»]

ProteinModelPortal

P21399.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21399. 8 interactions.

STRING

9606.ENSP00000309477.

PTM databases

PhosphoSite

P21399.

Polymorphism databases

DMDM

3123225.

2D gel databases

REPRODUCTION-2DPAGE

IPI00008485.

UCD-2DPAGE

P21399.

Proteomic databases

PaxDb

P21399.

PeptideAtlas

P21399.

PRIDE

P21399.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309951; ENSP00000309477; ENSG00000122729.
ENST00000379923; ENSP00000369255; ENSG00000122729.

GeneID

48.

KEGG

hsa:48.

UCSC

uc003zqw.4. human.

Organism-specific databases

CTD

48.

GeneCards

GC09P032374.

HGNC

HGNC:117. ACO1.

HPA

HPA019371.
HPA024157.

MIM

100880. gene.

neXtProt

NX_P21399.

PharmGKB

PA24442.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1048.

HOGENOM

HOG000025704.

HOVERGEN

HBG052147.

InParanoid

P21399.

KO

K01681.

OMA

RNCDGKK.

OrthoDB

EOG4C2H8W.

PhylomeDB

P21399.

Enzyme and pathway databases

BioCyc

MetaCyc:HS04597-MONOMER.

Gene expression databases

ArrayExpress

P21399.

Bgee

P21399.

CleanEx

HS_ACO1.

Genevestigator

P21399.

GermOnline

ENSG00000122729. Homo sapiens.

Family and domain databases

Gene3D

3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.

InterPro

IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_prot_2.
IPR015934. Aconitase/Fe_reg_prot_2/AcnD.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]

PANTHER

PTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 1 hit.

Pfam

PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]

PRINTS

PR00415. ACONITASE.

SUPFAM

SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.

TIGRFAMs

TIGR01341. aconitase_1. 1 hit.

PROSITE

PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

P21399.

GenomeRNAi

48.

NextBio

187.

SOURCE

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Entry information

Entry name

ACOC_HUMAN

Accession

Primary (citable) accession number: P21399
Secondary accession number(s): D3DRK7, Q14652, Q5VZA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 143 of the entry and version 3 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.