O35973 (PER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Period circadian protein homolog 1
Short name=mPER1

Alternative name(s):
Circadian clock protein PERIOD 1
Circadian pacemaker protein Rigui

Gene names

Name:	Per1
Synonyms:	Per, Rigui

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences CLOCK function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation. Can bind heme. Ref.6 Ref.19
Subunit structure	Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, BMAL1 or BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS, PER2, PER3 and, through a C-terminal domain, with CRY1 and CRY2. Interaction with CSNK1D or CSNK1E promotes nuclear location of PER proteins. Interacts with GPRASP1. Binding to CSNK1G2 triggers proteasomal degradation By similarity. Ref.6 Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Nucleus. Cytoplasm. Note: Mainly nuclear. Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation or by interaction with CSNK1E and/or phosphorylation which appears to mask the PER1 nuclear localization signal. Also translocated to the nucleus by CRY1 or CRY2. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18
Tissue specificity	In brain, highest expression is observed in the SCN. Highly expressed in the pyramidal cell layer of the piriform cortex, the periventricular part of the caudate-putamen, many thalamic nuclei, and the granular layer of the cerebellar cortex. Weaker expression is detected in most area of the brain, including cortical and non cortical structures. Expression but no oscillations occurs in the glomerular and mitral cell layers of the olfactory bulb, the internal granular layer of the cerebellum, the cornu ammonis and dentate gyrus of the hyppocampus, the cerebral and piriform cortices. Also found in heart, brain, spleen, lung, liver, skeletal muscle, testis. Highest level in testis. Low level in kidney. Ref.2 Ref.5 Ref.7
Developmental stage	Expressed in the suprachiasmatic nucleus (SCN) during late fetal and early neonatal life.
Induction	In the suprachiasmatic nucleus (SCN), behaves like a day-type oscillator, with maximum expression during the light period. Oscillations are maintained under constant darkness and are responsive to changes of the light/dark cycles. There is a 4 hour time delay between PER1 and PER2 oscillations. The expression rhythms appear to originate from retina. In liver, peak levels at CT9. In the SCN, levels increase by light exposure during subjective night. Circadian oscillations also observed in skeletal muscle and liver but not in testis. Ref.1 Ref.2 Ref.5 Ref.7 Ref.12
Post-translational modification	Phosphorylated on serine residues by CSNK1E. Also can be phosphorylated by the delta isoform. Phosphorylation by CSNK1 retains PER1 in the cytoplasm and leads to its ubiquitination and subsequent degradation. Ref.12 Ref.14 Ref.15 Ref.18 Ubiquitinated. Ref.14
Sequence similarities	Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
Biological process	Biological rhythms Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	circadian regulation of gene expression Inferred from electronic annotation. Source: Compara circadian rhythm Inferred from expression pattern PubMed 15038852. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12397359PubMed 15147242. Source: BHF-UCL response to light stimulus Inferred from expression pattern PubMed 15038852. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	E-box binding Inferred from electronic annotation. Source: Compara RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from electronic annotation. Source: Compara protein binding transcription factor activity Inferred from direct assay PubMed 15147242. Source: BHF-UCL signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Timeless	Q9R1X4	3	EBI-1266764,EBI-1793117

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1291

1291

Period circadian protein homolog 1

PRO_0000162628

Regions

Domain

208 – 275

68

PAS 1

Domain

348 – 414

67

PAS 2

Domain

422 – 465

44

PAC

Region

596 – 815

220

CSNK1E binding domain

Region

1148 – 1291

144

CRY binding domain

Motif

486 – 498

13

Nuclear export signal

Motif

824 – 840

17

Nuclear localization signal Ref.11

Compositional bias

49 – 129

81

Ser-rich

Compositional bias

653 – 656

4

Poly-Ser

Compositional bias

841 – 844

4

Poly-His

Compositional bias

847 – 971

125

Pro-rich

Compositional bias

1029 – 1103

75

Ser-rich

Compositional bias

1224 – 1277

54

Gly-rich

Compositional bias

1270 – 1273

4

Poly-Glu

Amino acid modifications

Modified residue

704

1

Phosphoserine By similarity

Modified residue

815

1

Phosphoserine By similarity

Modified residue

978

1

Phosphoserine By similarity

Modified residue

979

1

Phosphoserine By similarity

Experimental info

Mutagenesis

267

1

Y → E: No effect on homodimerization. Abolishes homodimerization; when associated with E-444. Ref.19

Mutagenesis

444

1

F → E: Reduces homodimerization. Abolishes homodimerization; when associated with E-267. Ref.19

Mutagenesis

448

1

W → E: Abolishes homodimerization. Ref.19

Mutagenesis

661

1

S → A: Reduced phosphorylation. No nuclear entry of PER1, CRY1 nor CKSN1E; when associated with A-663.

Mutagenesis

663

1

S → A: Reduced phosphorylation. No nuclear entry PER1, CRY1 nor CKSN1E; when associated with A-661.

Mutagenesis

831 – 833

3

HCR → ACA: No effect on nuclear import. Ref.11

Mutagenesis

835 – 838

4

KAKR → AAKA: Abolishes nuclear accumulation. Ref.11

Sequence conflict

1199

1

T → M in AAC53355. Ref.1

Sequence conflict

1199

1

T → M in BAA22634. Ref.2

Sequence conflict

1199

1

T → M in BAA94086. Ref.3

Secondary structure

1

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1291

Helix Strand Turn

Details...

Beta strand

198 – 200

3

Helix

202 – 212

11

Beta strand

217 – 225

9

Turn

226 – 228

3

Beta strand

230 – 234

5

Helix

237 – 242

6

Turn

247 – 251

5

Helix

254 – 257

4

Helix

260 – 269

10

Turn

272 – 274

3

Beta strand

297 – 301

5

Beta strand

314 – 325

12

Beta strand

334 – 343

10

Beta strand

347 – 351

5

Helix

355 – 357

3

Beta strand

359 – 364

6

Beta strand

369 – 373

5

Helix

377 – 381

5

Helix

385 – 388

4

Helix

393 – 396

4

Helix

399 – 401

3

Helix

402 – 412

11

Beta strand

415 – 417

3

Beta strand

425 – 428

4

Beta strand

430 – 432

3

Beta strand

434 – 438

5

Beta strand

440 – 445

6

Turn

447 – 449

3

Beta strand

451 – 463

13

Helix

485 – 498

14

Sequences

	Sequence		Length	Mass (Da)
	O35973 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 77FB9BC71EDF31A6	FASTA	1,291	136,373
	10 20 30 40 50 60 MSGPLEGADG GGDPRPGEPF CPGGVPSPGA PQHRPCPGPS LADDTDANSN GSSGNESNGP 70 80 90 100 110 120 ESRGASQRSS HSSSSGNGKD SALLETTESS KSTNSQSPSP PSSSIAYSLL SASSEQDNPS 130 140 150 160 170 180 TSGCSSEQSA RARTQKELMT ALRELKLRLP PERRGKGRSG TLATLQYALA CVKQVQANQE 190 200 210 220 230 240 YYQQWSLEEG EPCAMDMSTY TLEELEHITS EYTLRNQDTF SVAVSFLTGR IVYISEQAGV 250 260 270 280 290 300 LLRCKRDVFR GARFSELLAP QDVGVFYGST TPSRLPTWGT GTSAGSGLKD FTQEKSVFCR 310 320 330 340 350 360 IRGGPDRDPG PRYQPFRLTP YVTKIRVSDG APAQPCCLLI AERIHSGYEA PRIPPDKRIF 370 380 390 400 410 420 TTRHTPSCLF QDVDERAAPL LGYLPQDLLG APVLLFLHPE DRPLMLAIHK KILQLAGQPF 430 440 450 460 470 480 DHSPIRFCAR NGEYVTMDTS WAGFVHPWSR KVAFVLGRHK VRTAPLNEDV FTPPAPSPAP 490 500 510 520 530 540 SLDSDIQELS EQIHRLLLQP VHSSSPTGLC GVGPLMSPGP LHSPGSSSDS NGGDAEGPGP 550 560 570 580 590 600 PAPVTFQQIC KDVHLVKHQG QQLFIESRAK PPPRPRLLAT GTFKAKVLPC QSPNPELEVA 610 620 630 640 650 660 PVPDQASLAL APEEPERKET SGCSYQQINC LDSILRYLES CNIPSTTKRK CASSSSYTAS 670 680 690 700 710 720 SASDDDKQRA GPVPVGAKKD PSSAMLSGEG ATPRKEPVVG GTLSPLALAN KAESVVSVTS 730 740 750 760 770 780 QCSFSSTIVH VGDKKPPESD IIMMEDLPGL APGPAPSPAP SPTVAPDPTP DAYRPVGLTK 790 800 810 820 830 840 AVLSLHTQKE EQAFLNRFRD LGRLRGLDTS SVAPSAPGCH HGPIPPGRRH HCRSKAKRSR 850 860 870 880 890 900 HHHHQTPRPE TPCYVSHPSP VPSSGPWPPP PATTPFPAMV QPYPLPVFSP RGGPQPLPPA 910 920 930 940 950 960 PTSVSPATFP SPLVTPMVAL VLPNYLFPTP PSYPYGVSQA PVEGPPTPAS HSPSPSLPPP 970 980 990 1000 1010 1020 PLSPPHRPDS PLFNSRCSSP LQLNLLQLEE SPRTEGGAAA GGPGSSAGPL PPSEETAEPE 1030 1040 1050 1060 1070 1080 ARLVEVTESS NQDALSGSSD LLELLLQEDS RSGTGSAASG SLGSGLGSGS GSGSHEGGST 1090 1100 1110 1120 1130 1140 SASITRSSQS SHTSKYFGSI DSSEAEAGAA RARTEPGDQV IKCVLQDPIW LLMANADQRV 1150 1160 1170 1180 1190 1200 MMTYQVPSRD AASVLKQDRE RLRAMQKQQP RFSEDQRREL GAVHSWVRKG QLPRALDVTA 1210 1220 1230 1240 1250 1260 CVDCGSSVQD PGHSDDPLFS ELDGLGLEPM EEGGGEGGGC GVGGGGGDGG EEAQTQIGAK 1270 1280 1290 GSSSQDSAME EEEQGGGSSS PALPAEENST S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rigui, a putative mammalian ortholog of the Drosophila period gene." Sun Z.S., Albrecht U., Zhuchenko O., Bailey J., Eichele G., Lee C.C. Cell 90:1003-1011(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Tissue: Brain.
[2]	"Circadian oscillation of a mammalian homologue of the Drosophila period gene." Tei H., Okamura H., Shigeyoshi Y., Fukuhara C., Ozawa R., Hirose M., Sakaki Y. Nature 389:512-516(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: BALB/c. Tissue: Brain.
[3]	"The human and mouse Period1 genes: five well-conserved E-boxes additively contribute to the enhancement of mPer1 transcription." Hida A., Koike N., Hirose M., Hattori M., Sakaki Y., Tei H. Genomics 65:224-233(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei." Shearman L.P., Zylka M.J., Weaver D.R., Kolakowski L.F. Jr., Reppert S.M. Neuron 19:1261-1269(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]	"Mammalian circadian autoregulatory loop: a timeless ortholog and mPer1 interact and negatively regulate CLOCK-BMAL1-induced transcription." Sangoram A.M., Saez L., Antoch M.P., Gekakis N., Staknis D., Whiteley A., Fruechte E.M., Vitaterna M.H., Shimomura K., King D.P., Young M.W., Weitz C.J., Takahashi J.S. Neuron 21:1101-1113(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TIMELESS.
[7]	"Circadian regulation of cryptochrome genes in the mouse." Miyamoto Y., Sancar A. Brain Res. Mol. Brain Res. 71:238-243(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]	"mCRY1 and mCRY2 are essential components of the negative limb of the circadian clock feedback loop." Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X., Maywood E.S., Hastings M.H., Reppert S.M. Cell 98:193-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PER3; CRY1 AND CRY2, SUBCELLULAR LOCATION.
[9]	"A mammalian ortholog of Drosophila timeless, highly expressed in SCN and retina, forms a complex with mPER1." Takumi T., Nagamine Y., Miyake S., Matsubara C., Taguchi K., Takekida S., Sakakida Y., Nishikawa K., Kishimoto T., Niwa S., Okumura K., Okamura H. Genes Cells 4:67-75(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIMELESS, SUBCELLULAR LOCATION.
[10]	"Nuclear export of mammalian PERIOD proteins." Vielhaber E.L., Duricka D., Ullman K.S., Virshup D.M. J. Biol. Chem. 276:45921-45927(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
[11]	"Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon." Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M. Mol. Cell. Biol. 20:4888-4899(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PER2; CKSN1D AND CKSN1E, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 831-HIS--ARG-833 AND 835-LYS--ARG-838.
[12]	"Posttranslational mechanisms regulate the mammalian circadian clock." Lee C., Etchegaray J.-P., Cagampang F.R.A., Loudon A.S.I., Reppert S.M. Cell 107:855-867(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, INDUCTION.
[13]	"The circadian regulatory proteins BMAL1 and cryptochromes are substrates of casein kinase Iepsilon." Eide E.J., Vielhaber E.L., Hinz W.A., Virshup D.M. J. Biol. Chem. 277:17248-17254(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRY1 AND CRY2, CRY BINDING DOMAIN, SUBCELLULAR LOCATION.
[14]	"Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells." Akashi M., Tsuchiya Y., Yoshino T., Nishida E. Mol. Cell. Biol. 22:1693-1703(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSNK1D AND CKSN1E, PHOSPHORYLATION, UBIQUITINATION.
[15]	"Identification of mPer1 phosphorylation sites responsible for the nuclear entry." Takano A., Isojima Y., Nagai K. J. Biol. Chem. 279:32578-32585(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-661 AND SER-663, SUBCELLULAR LOCATION, MUTAGENESIS OF 661-SER--SER-663.
[16]	"Direct association between mouse PERIOD and CKIepsilon is critical for a functioning circadian clock." Lee C., Weaver D.R., Reppert S.M. Mol. Cell. Biol. 24:584-594(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CKSN1E; PER2; PER3; CRY1 AND CRY2.
[17]	"Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance." Chaves I., Yagita K., Barnhoorn S., Okamura H., van der Horst G.T.J., Tamanini F. Mol. Cell. Biol. 26:1743-1753(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRY1 AND CRY2, SUBCELLULAR LOCATION.
[18]	"Casein kinase 1 delta regulates the pace of the mammalian circadian clock." Etchegaray J.P., Machida K.K., Noton E., Constance C.M., Dallmann R., Di Napoli M.N., DeBruyne J.P., Lambert C.M., Yu E.A., Reppert S.M., Weaver D.R. Mol. Cell. Biol. 29:3853-3866(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSNK1D AND CSNK1E, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[19]	"Unwinding the differences of the mammalian PERIOD clock proteins from crystal structure to cellular function." Kucera N., Schmalen I., Hennig S., Ollinger R., Strauss H.M., Grudziecki A., Wieczorek C., Kramer A., Wolf E. Proc. Natl. Acad. Sci. U.S.A. 109:3311-3316(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 191-502, MUTAGENESIS OF TYR-267; PHE-444 AND TRP-448, FUNCTION IN HEME BINDING, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF022992 mRNA. Translation: AAC53355.1.
AB002108 mRNA. Translation: BAA22634.1.
AB030818 Genomic DNA. Translation: BAA94086.1.
AL645527 Genomic DNA. Translation: CAI35245.1.

IPI

IPI00554857.

PIR

T00019.

RefSeq

NP_001152839.1. NM_001159367.1.
NP_035195.2. NM_011065.4.

UniGene

Mm.7373.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DJ2	X-ray	2.75	A/B/C/D	191-502	[»]

ProteinModelPortal

O35973.

SMR

O35973. Positions 196-502.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38519N.

IntAct

O35973. 7 interactions.

PTM databases

PhosphoSite

O35973.

Proteomic databases

PaxDb

O35973.

PRIDE

O35973.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021271; ENSMUSP00000021271; ENSMUSG00000020893.
ENSMUST00000166748; ENSMUSP00000132635; ENSMUSG00000020893.

GeneID

18626.

KEGG

mmu:18626.

Organism-specific databases

CTD

5187.

MGI

MGI:1098283. Per1.

Phylogenomic databases

eggNOG

NOG253593.

GeneTree

ENSGT00510000046467.

HOVERGEN

HBG008167.

InParanoid

B1ASX0.

KO

K02633.

OMA

ELGAVHS.

OrthoDB

EOG4HMJ8R.

Enzyme and pathway databases

Reactome

REACT_109335. Circadian Clock.
REACT_24972. Circadian Clock (mouse).

Gene expression databases

ArrayExpress

O35973.

Bgee

O35973.

CleanEx

MM_PER1.

Genevestigator

O35973.

GermOnline

ENSMUSG00000020893. Mus musculus.

Family and domain databases

InterPro

IPR001610. PAC.
IPR000014. PAS.
IPR013655. PAS_fold_3.
IPR022728. Period_circadian-like_C.
[Graphical view]

Pfam

PF08447. PAS_3. 1 hit.
PF12114. Period_C. 1 hit.
[Graphical view]

SMART

SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]

PROSITE

PS50113. PAC. False negative.
PS50112. PAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

294576.

SOURCE

Search...

Entry information

Entry name

PER1_MOUSE

Accession

Primary (citable) accession number: O35973
Secondary accession number(s): B1ASX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program