P24468 (COT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
COUP transcription factor 2
Short name=COUP-TF2

Alternative name(s):
Apolipoprotein A-I regulatory protein 1
Short name=ARP-1
COUP transcription factor II
Short name=COUP-TF II
Nuclear receptor subfamily 2 group F member 2

Gene names

Name:	NR2F2
Synonyms:	ARP1, TFCOUP2

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

General annotation (Comments)

Function	Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. Ref.1 Ref.11 Ref.14
Subunit structure	Interacts with SQSTM1 By similarity. Binds DNA as a dimer; homodimer or heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3 and PPARGC1A. Interacts with ZFPM2 By similarity. Ref.1 Ref.12 Ref.14
Subcellular location	Nucleus.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR2 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara blood vessel morphogenesis Inferred from electronic annotation. Source: Compara fertilization Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara limb development Inferred from electronic annotation. Source: Compara lipid metabolic process Traceable author statement Ref.1. Source: ProtInc maternal placenta development Inferred from electronic annotation. Source: Compara negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from direct assay PubMed 19210544. Source: BHF-UCL negative regulation of endothelial cell migration Inferred from mutant phenotype PubMed 19210544. Source: BHF-UCL negative regulation of endothelial cell proliferation Inferred from mutant phenotype PubMed 19210544. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.11. Source: UniProtKB neuron migration Inferred from electronic annotation. Source: Compara placenta blood vessel development Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.14. Source: UniProtKB radial pattern formation Inferred from electronic annotation. Source: Compara regulation of transcription involved in lymphatic endothelial cell fate commitment Inferred from mutant phenotype PubMed 18815287. Source: BHF-UCL response to estradiol stimulus Inferred from electronic annotation. Source: Compara skeletal muscle tissue development Inferred from electronic annotation. Source: Compara trophoblast giant cell differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Inferred from direct assay PubMed 19210544. Source: BHF-UCL
Molecular_function	ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from direct assay Ref.14. Source: UniProtKB retinoic acid binding Inferred from direct assay Ref.14. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay Ref.11. Source: UniProtKB steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription corepressor activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P24468-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P24468-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-147: MAMVVSTWRD...KCLKVGMRRE → MQAVWDLEQGKYGF

Isoform 3 (identifier: P24468-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 414

414

COUP transcription factor 2

PRO_0000053606

Regions

DNA binding

76 – 151

76

Nuclear receptor Ref.3

Zinc finger

79 – 99

21

NR C4-type

Zinc finger

115 – 139

25

NR C4-type

Region

117 – 414

298

Interaction with ZFPM2 By similarity

Region

183 – 414

232

Ligand-binding By similarity

Region

337 – 414

78

Important for dimerization

Compositional bias

71 – 75

5

Poly-Gln

Natural variations

Alternative sequence

1 – 153

153

Missing in isoform 3.

VSP_043897

Alternative sequence

1 – 147

147

MAMVV…GMRRE → MQAVWDLEQGKYGF in isoform 2.

VSP_042630

Experimental info

Mutagenesis

228

1

R → E: Reduces transcription activation by 40%; when associated with R-398. Ref.14

Mutagenesis

249

1

W → A: Reduces transcription activation by 50%; when associated with A-250. Ref.14

Mutagenesis

250

1

S → A: Reduces transcription activation by 50%; when associated with A-249. Ref.14

Mutagenesis

250

1

S → W: Reduces transcription activation by 50%. Ref.14

Mutagenesis

253 – 254

2

FV → AA: Reduces transcription activation by 50%.

Mutagenesis

269 – 270

2

LL → AA: Reduces transcription activation by 50%.

Mutagenesis

364 – 365

2

LL → AA: Reduces transcription activation by 80%.

Mutagenesis

398

1

D → R: Reduces transcription activation by 40%; when associated with E-228. Ref.14

Secondary structure

1

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414

Helix Strand Turn

Details...

Helix

175 – 187

13

Helix

212 – 229

18

Beta strand

230 – 232

3

Helix

233 – 235

3

Helix

238 – 260

23

Helix

290 – 304

15

Helix

309 – 320

12

Helix

331 – 352

22

Helix

359 – 364

6

Helix

367 – 372

6

Helix

375 – 382

8

Helix

384 – 387

4

Helix

392 – 394

3

Helix

396 – 400

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: C24CB2E8C8A27E8C	FASTA	414	45,571
	10 20 30 40 50 60 MAMVVSTWRD PQDEVPGSQG SQASQAPPVP GPPPGAPHTP QTPGQGGPAS TPAQTAAGGQ 70 80 90 100 110 120 GGPGGPGSDK QQQQQHIECV VCGDKSSGKH YGQFTCEGCK SFFKRSVRRN LSYTCRANRN 130 140 150 160 170 180 CPIDQHHRNQ CQYCRLKKCL KVGMRREAVQ RGRMPPTQPT HGQFALTNGD PLNCHSYLSG 190 200 210 220 230 240 YISLLLRAEP YPTSRFGSQC MQPNNIMGIE NICELAARML FSAVEWARNI PFFPDLQITD 250 260 270 280 290 300 QVALLRLTWS ELFVLNAAQC SMPLHVAPLL AAAGLHASPM SADRVVAFMD HIRIFQEQVE 310 320 330 340 350 360 KLKALHVDSA EYSCLKAIVL FTSDACGLSD VAHVESLQEK SQCALEEYVR SQYPNQPTRF 370 380 390 400 410 GKLLLRLPSL RTVSSSVIEQ LFFVRLVGKT PIETLIRDML LSGSSFNWPY MAIQ
	Isoform 2 [UniParc]. Checksum: 038DD27B80868BB5	FASTA	281	31,484
	10 20 30 40 50 60 MQAVWDLEQG KYGFAVQRGR MPPTQPTHGQ FALTNGDPLN CHSYLSGYIS LLLRAEPYPT 70 80 90 100 110 120 SRFGSQCMQP NNIMGIENIC ELAARMLFSA VEWARNIPFF PDLQITDQVA LLRLTWSELF 130 140 150 160 170 180 VLNAAQCSMP LHVAPLLAAA GLHASPMSAD RVVAFMDHIR IFQEQVEKLK ALHVDSAEYS 190 200 210 220 230 240 CLKAIVLFTS DACGLSDVAH VESLQEKSQC ALEEYVRSQY PNQPTRFGKL LLRLPSLRTV 250 260 270 280 SSSVIEQLFF VRLVGKTPIE TLIRDMLLSG SSFNWPYMAI Q
	Isoform 3 [UniParc]. Checksum: 5526AD057E2A639E	FASTA	261	29,163
	10 20 30 40 50 60 MPPTQPTHGQ FALTNGDPLN CHSYLSGYIS LLLRAEPYPT SRFGSQCMQP NNIMGIENIC 70 80 90 100 110 120 ELAARMLFSA VEWARNIPFF PDLQITDQVA LLRLTWSELF VLNAAQCSMP LHVAPLLAAA 130 140 150 160 170 180 GLHASPMSAD RVVAFMDHIR IFQEQVEKLK ALHVDSAEYS CLKAIVLFTS DACGLSDVAH 190 200 210 220 230 240 VESLQEKSQC ALEEYVRSQY PNQPTRFGKL LLRLPSLRTV SSSVIEQLFF VRLVGKTPIE 250 260 TLIRDMLLSG SSFNWPYMAI Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily." Ladias J.A.A., Karathanasis S.K. Science 251:561-565(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT.
[2]	Speckmayer R.W.M., Paulweber B., Sandhofer F. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system." Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T. FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING.
[4]	"Characterisation of a new, DNA binding domain deficient chicken ovalbumin upstream promoter- transcription factor IIdelta isoform in the human brain." Schote A.B., Bechet T., Pirrotte P., Turner J.D., Muller C.P. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Liver.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Mammary gland.
[6]	"Isolation of cDNA coding for multiple human nuclear receptor clones." Kaighin V.A., Martin A.L., Aronstam R.S. Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Kidney.
[7]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORMS 1 AND 2). Tissue: Brain, Kidney and Spleen.
[10]	"The COUP-TFs compose a family of functionally related transcription factors." Wang L.H., Ing N.H., Tsai S.Y., O'Malley B.W., Tsai M.J. Gene Expr. 1:207-216(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-351 (ISOFORM 1).
[11]	"The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers of the human oxytocin gene promoter." Chu K., Zingg H.H. J. Mol. Endocrinol. 19:163-172(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Heterodimeric interactions between chicken ovalbumin upstream promoter-transcription factor family members ARP1 and ear2." Avram D., Ishmael J.E., Nevrivy D.J., Peterson V.J., Lee S.H., Dowell P., Leid M. J. Biol. Chem. 274:14331-14336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH NR2F6.
[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]	"Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor." Kruse S.W., Suino-Powell K., Zhou X.E., Kretschman J.E., Reynolds R., Vonrhein C., Xu Y., Wang L., Tsai S.Y., Tsai M.J., Xu H.E. PLoS Biol. 6:E227-E227(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 175-414, FUNCTION, SUBUNIT, INTERACTION WITH NCOA1; NCOA2; NCOA3 AND PPARGC1A, MUTAGENESIS OF ARG-228; TRP-249; SER-250; 253-PHE-VAL-254; 260-LEU-LEU-270; 364-LEU-LEU-365 AND ASP-398.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64497 mRNA. Translation: AAA86429.1.
U60477 Genomic DNA. Translation: AAB09475.1.
AB307711 mRNA. Translation: BAH02302.1.
FM208183 mRNA. Translation: CAR63888.1.
AK298824 mRNA. Translation: BAG60954.1.
AK301595 mRNA. Translation: BAG63083.1.
AK316086 mRNA. Translation: BAH14457.1.
HQ692849 mRNA. Translation: ADZ17360.1.
HQ692850 mRNA. Translation: ADZ17361.1.
AC016251 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02195.1.
CH471101 Genomic DNA. Translation: EAX02196.1.
CH471101 Genomic DNA. Translation: EAX02197.1.
BC014664 mRNA. Translation: AAH14664.1.
BC042897 mRNA. Translation: AAH42897.1.
BC106083 mRNA. Translation: AAI06084.1.
M62760 mRNA. Translation: AAA21479.1.

IPI

IPI00028611.
IPI00789037.

PIR

A37133.

RefSeq

NP_001138627.1. NM_001145155.1.
NP_001138628.1. NM_001145156.1.
NP_001138629.1. NM_001145157.1.
NP_066285.1. NM_021005.3.

UniGene

Hs.347991.
Hs.519445.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CJW	X-ray	1.48	A	175-414	[»]

ProteinModelPortal

P24468.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29713N.

IntAct

P24468. 5 interactions.

MINT

MINT-1183332.

STRING

9606.ENSP00000329908.

PTM databases

PhosphoSite

P24468.

Polymorphism databases

DMDM

114203.

Proteomic databases

PaxDb

P24468.

PRIDE

P24468.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000394166; ENSP00000377721; ENSG00000185551.
ENST00000394171; ENSP00000377726; ENSG00000185551.
ENST00000421109; ENSP00000401674; ENSG00000185551.
ENST00000453270; ENSP00000389853; ENSG00000185551.

GeneID

7026.

KEGG

hsa:7026.

UCSC

uc002btp.3. human.
uc010uri.2. human.

Organism-specific databases

CTD

7026.

GeneCards

GC15P096869.

HGNC

HGNC:7976. NR2F2.

MIM

107773. gene.

neXtProt

NX_P24468.

PharmGKB

PA31759.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327099.

HOGENOM

HOG000260820.

HOVERGEN

HBG005606.

InParanoid

P24468.

KO

K08548.

OMA

GPPNNTQ.

OrthoDB

EOG4MGS7H.

PhylomeDB

P24468.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.
telomerasepathway. Regulation of Telomerase.

SignaLink

P24468.

Gene expression databases

ArrayExpress

P24468.

Bgee

P24468.

CleanEx

HS_NR2F2.

Genevestigator

P24468.

GermOnline

ENSG00000185551. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.
3.30.50.10. 1 hit.

InterPro

IPR003068. COUP_TF.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR01282. COUPTNFACTOR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1961790.

EvolutionaryTrace

P24468.

GenomeRNAi

7026.

NextBio

27451.

SOURCE

Search...

Entry information

Entry name

COT2_HUMAN

Accession

Primary (citable) accession number: P24468
Secondary accession number(s): B4DQJ2 , B6ZGU1, Q03754, Q3KQR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 29, 2013
This is version 138 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.