Q24572 (CAF1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable histone-binding protein Caf1

Alternative name(s):
Chromatin assembly factor 1 p55 subunit
Short name=CAF-1 p55 subunit
Nucleosome-remodeling factor 55 kDa subunit
Short name=NURF-55
dCAF-1

Gene names

Name:	Caf1
ORF Names:	CG4236

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2. Ref.1 Ref.6 Ref.9 Ref.14 Ref.20
Subunit structure	Probably binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Self associates. Associates with chromatin. Component of the CAF-1 complex, composed of Caf1, Caf1-105 and Caf1-180. Within the CAF-1 complex, Caf1-180 interacts directly with both Caf1 and Caf1-105. Component of the NuRD complex, composed of at least Caf1, Mi-2, MTA1-like and Rpd3. Within the NuRD complex, Caf1 may interact directly with Mi-2, MTA1-like and Rpd3. The NuRD complex may also associate with the methyl-DNA binding protein MBD-like via Caf1 and Mi-2. Component of the NURF complex, composed of Caf1, E(bx), Nurf-38 and Iswi. Component of the Esc/E(z) complex, composed of Caf1, esc, E(z), Su(z)1, and possibly Pho1. The Esc/E(z) complex may also associate with Pcl and Rpd3 during early embryogenesis. Interacts with Rbf and Rbf2. Component of the DREAM complex at least composed of Myb, Caf1, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and l3mbt. Ref.9 Ref.11 Ref.20
Subcellular location	Nucleus Ref.1 Ref.6.
Developmental stage	Highest level during early embryogenesis and then decreases in larvae, pupae and adults. Ref.1
Sequence similarities	Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. Contains 6 WD repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
E(z)	P42124	6	EBI-75924,EBI-112315
esc	Q24338	11	EBI-75924,EBI-88911
Rpd3	Q94517	4	EBI-75924,EBI-302197

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 430

430

Probable histone-binding protein Caf1

PRO_0000050895

Regions

Repeat

126 – 159

34

WD 1

Repeat

179 – 210

32

WD 2

Repeat

229 – 260

32

WD 3

Repeat

275 – 306

32

WD 4

Repeat

319 – 350

32

WD 5

Repeat

376 – 407

32

WD 6

Amino acid modifications

Modified residue

11

1

Phosphoserine Ref.21

Modified residue

100

1

Phosphoserine Ref.22

Secondary structure

1

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430

Helix Strand Turn

Details...

Helix

12 – 35

24

Beta strand

36 – 43

8

Beta strand

51 – 59

9

Beta strand

64 – 73

10

Beta strand

77 – 79

3

Beta strand

81 – 91

11

Beta strand

118 – 129

12

Beta strand

132 – 137

6

Beta strand

140 – 147

8

Beta strand

149 – 151

3

Beta strand

153 – 157

5

Turn

158 – 160

3

Beta strand

174 – 177

4

Beta strand

187 – 189

3

Beta strand

191 – 193

3

Beta strand

196 – 200

5

Beta strand

206 – 210

5

Turn

217 – 219

3

Beta strand

224 – 227

4

Beta strand

234 – 239

6

Beta strand

246 – 251

6

Beta strand

254 – 260

7

Beta strand

270 – 274

5

Beta strand

280 – 285

6

Beta strand

290 – 297

8

Beta strand

300 – 306

7

Helix

307 – 309

3

Beta strand

315 – 318

4

Beta strand

324 – 329

6

Beta strand

336 – 341

6

Beta strand

346 – 350

5

Helix

351 – 353

3

Turn

360 – 362

3

Beta strand

363 – 366

4

Beta strand

370 – 374

5

Beta strand

381 – 386

6

Beta strand

388 – 390

3

Beta strand

393 – 398

6

Beta strand

401 – 408

8

Helix

410 – 412

3

Sequences

	Sequence		Length	Mass (Da)
	Q24572 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 90C5FB959F1660D5	FASTA	430	48,635
	10 20 30 40 50 60 MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ 70 80 90 100 110 120 DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE 130 140 150 160 170 180 IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH 190 200 210 220 230 240 QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH 250 260 270 280 290 300 LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK 310 320 330 340 350 360 TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST 370 380 390 400 410 420 EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI 430 PASELETNTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein." Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T. Mol. Cell. Biol. 16:6149-6159(1996) [PubMed: 8887645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 256-268; 301-313; 322-334 AND 354-376, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: Canton-S.
[2]	"Widespread adaptive evolution of Drosophila genes with sex-biased expression." Proeschel M., Zhang Z., Parsch J. Genetics 174:893-900(2006) [PubMed: 16951084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84 and ZBMEL95.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[6]	"Drosophila NURF-55, a WD repeat protein involved in histone metabolism." Martinez-Balbas M.A., Tsukiyama T., Gdula D., Wu C. Proc. Natl. Acad. Sci. U.S.A. 95:132-137(1998) [PubMed: 9419341] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-80; 256-269; 301-310; 314-339 AND 354-368, FUNCTION, IDENTIFICATION IN THE NURF COMPLEX, ASSOCIATION WITH CHROMATIN, SUBCELLULAR LOCATION.
[7]	"Assembly of regularly spaced nucleosome arrays by Drosophila chromatin assembly factor 1 and a 56-kDa histone-binding protein." Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T. Proc. Natl. Acad. Sci. U.S.A. 92:11726-11730(1995) [PubMed: 8524837] [Abstract] Cited for: CHARACTERIZATION OF THE CAF-1 COMPLEX.
[8]	"Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor 1." Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T. Mol. Cell. Biol. 16:810-817(1996) [PubMed: 8622682] [Abstract] Cited for: CHARACTERIZATION OF THE CAF-1 COMPLEX.
[9]	"Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex." Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C. Genes Dev. 12:3206-3216(1998) [PubMed: 9784495] [Abstract] Cited for: FUNCTION, INTERACTION WITH ISWI AND NURF-38.
[10]	"The Drosophila polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3." Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J. Development 128:275-286(2001) [PubMed: 11124122] [Abstract] Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
[11]	"Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly factors." Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M., Harte P.J., Kobayashi R., Kadonaga J.T. Mol. Cell. Biol. 21:6574-6584(2001) [PubMed: 11533245] [Abstract] Cited for: INTERACTION WITH CAF1-105 AND CAF1-180.
[12]	"Drosophila Enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites." Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Cell 111:185-196(2002) [PubMed: 12408863] [Abstract] Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); RPD3 AND SU(Z)12.
[13]	"Histone methyltransferase activity of a Drosophila Polycomb group repressor complex." Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A. Cell 111:197-208(2002) [PubMed: 12408864] [Abstract] Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND SU(Z)12.
[14]	"Role for a Drosophila Myb-containing protein complex in site-specific DNA replication." Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R. Nature 420:833-837(2002) [PubMed: 12490953] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS PSECTROMETRY, IDENTIFICATION IN THE DREAM COMPLEX.
[15]	"Polycomb group proteins ESC and E(Z) are present in multiple distinct complexes that undergo dynamic changes during development." Furuyama T., Tie F., Harte P.J. Genesis 35:114-124(2003) [PubMed: 12533794] [Abstract] Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
[16]	"A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike and RPD3." Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J. Mol. Cell. Biol. 23:3352-3362(2003) [PubMed: 12697833] [Abstract] Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); PCL; RPD3 AND SU(Z)12.
[17]	"The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2." Marhold J., Brehm A., Kramer K. BMC Mol. Biol. 5:20-20(2004) [PubMed: 15516265] [Abstract] Cited for: IDENTIFICATION IN THE NURD COMPLEX, SELF-ASSOCIATION.
[18]	"Native E2F/RBF complexes contain Myb-interacting proteins and repress transcription of developmentally controlled E2F target genes." Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O., Aasland R., White-Cooper H., Dyson N., Brehm A. Cell 119:181-193(2004) [PubMed: 15479636] [Abstract] Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[19]	"Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor complex." Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J., Botchan M.R. Genes Dev. 18:2929-2940(2004) [PubMed: 15545624] [Abstract] Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[20]	"p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the repression of dE2F2/RBF-regulated genes." Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J. Mol. Cell. Biol. 24:9124-9136(2004) [PubMed: 15456884] [Abstract] Cited for: FUNCTION, INTERACTION WITH RBF AND RBF2.
[21]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY.
[22]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U62388 mRNA. Translation: AAB37257.1.
AM294392 Genomic DNA. Translation: CAL26322.1.
AM294393 Genomic DNA. Translation: CAL26323.1.
AM294394 Genomic DNA. Translation: CAL26324.1.
AM294395 Genomic DNA. Translation: CAL26325.1.
AM294396 Genomic DNA. Translation: CAL26330.1.
AM294397 Genomic DNA. Translation: CAL26335.1.
AM294398 Genomic DNA. Translation: CAL26337.1.
AM294399 Genomic DNA. Translation: CAL26338.1.
AM294400 Genomic DNA. Translation: CAL26339.1.
AM294401 Genomic DNA. Translation: CAL26340.1.
AM294402 Genomic DNA. Translation: CAL26341.1.
AM294403 Genomic DNA. Translation: CAL26342.1.
AE014297 Genomic DNA. Translation: AAF55146.1.
AY061408 mRNA. Translation: AAL28956.1.

RefSeq

NP_524354.1. NM_079630.3.

UniGene

Dm.1657.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XYI	X-ray	1.75	A	1-430	[»]
2YB8	X-ray	2.30	B	1-418	[»]
2YBA	X-ray	2.55	A/B	1-418	[»]
3C99	X-ray	2.90	A	1-430	[»]
3C9C	X-ray	3.20	A	1-430	[»]

ProteinModelPortal

Q24572.

SMR

Q24572. Positions 9-415.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-23697N.

IntAct

Q24572. 19 interactions.

MINT

MINT-252601.

STRING

Q24572.

Proteomic databases

PRIDE

Q24572.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0083052; FBpp0082511; FBgn0015610.

GeneID

41836.

KEGG

dme:Dmel_CG4236.

NMPDR

fig|7227.3.peg.12911.

Organism-specific databases

CTD

41836.

FlyBase

FBgn0263347. Caf1.

Phylogenomic databases

eggNOG

inNOG08914.

GeneTree

EMGT00050000002914.

InParanoid

Q24572.

OMA

ATPKEHR.

OrthoDB

EOG4ZCRKP.

PhylomeDB

Q24572.

Gene expression databases

ArrayExpress

Q24572.

Bgee

Q24572.

GermOnline

CG4236. Drosophila melanogaster.

Family and domain databases

InterPro

IPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Gene3D

G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

KO

K10752.

Pfam

PF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 6 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

825799.

Entry information

Entry name

CAF1_DROME

Accession

Primary (citable) accession number: Q24572
Secondary accession number(s): A0AP04, Q9VFB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project