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O35973 (PER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Protein existenceEvidence 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.20

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.19 Ref.20

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.19

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 Ref.18

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 Ref.18

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.19

Ubiquitinated. Ref.14

Sequence similarities

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcircadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

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

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of hair cycle

Inferred from sequence or structural similarity. Source: UniProtKB

response to light stimulus

Inferred from expression pattern PubMed 15038852. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: MGI

   Molecular_functionE-box binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding transcription factor activity

Inferred from direct assay PubMed 15147242. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TimelessQ9R1X43EBI-1266764,EBI-1793117

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12911291Period circadian protein homolog 1
PRO_0000162628

Regions

Domain208 – 27568PAS 1
Domain348 – 41467PAS 2
Domain422 – 46544PAC
Region596 – 815220CSNK1E binding domain
Region1148 – 1291144CRY binding domain
Motif486 – 49813Nuclear export signal
Motif824 – 84017Nuclear localization signal Ref.11
Compositional bias49 – 12981Ser-rich
Compositional bias653 – 6564Poly-Ser
Compositional bias841 – 8444Poly-His
Compositional bias847 – 971125Pro-rich
Compositional bias1029 – 110375Ser-rich
Compositional bias1224 – 127754Gly-rich
Compositional bias1270 – 12734Poly-Glu

Amino acid modifications

Modified residue6611Phosphoserine Ref.15
Modified residue6631Phosphoserine Ref.15
Modified residue7041Phosphoserine By similarity
Modified residue8151Phosphoserine By similarity
Modified residue9781Phosphoserine By similarity
Modified residue9791Phosphoserine By similarity

Experimental info

Mutagenesis2671Y → E: No effect on homodimerization. Abolishes homodimerization; when associated with E-444. Ref.20
Mutagenesis4441F → E: Reduces homodimerization. Abolishes homodimerization; when associated with E-267. Ref.20
Mutagenesis4481W → E: Abolishes homodimerization. Ref.20
Mutagenesis6611S → A: Reduced phosphorylation. No nuclear entry of PER1, CRY1 nor CKSN1E; when associated with A-663.
Mutagenesis6631S → A: Reduced phosphorylation. No nuclear entry PER1, CRY1 nor CKSN1E; when associated with A-661.
Mutagenesis831 – 8333HCR → ACA: No effect on nuclear import. Ref.11
Mutagenesis835 – 8384KAKR → AAKA: Abolishes nuclear accumulation. Ref.11
Sequence conflict11991T → M in AAC53355. Ref.1
Sequence conflict11991T → M in BAA22634. Ref.2
Sequence conflict11991T → M in BAA94086. Ref.3

Secondary structure

........................................................... 1291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35973 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 77FB9BC71EDF31A6

FASTA1,291136,373
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[19]"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.
[20]"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.
PIRT00019.
RefSeqNP_001152839.1. NM_001159367.1.
NP_035195.2. NM_011065.4.
XP_006532543.1. XM_006532480.1.
UniGeneMm.7373.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJ2X-ray2.75A/B/C/D191-502[»]
ProteinModelPortalO35973.
SMRO35973. Positions 196-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202111. 24 interactions.
DIPDIP-38519N.
IntActO35973. 8 interactions.

PTM databases

PhosphoSiteO35973.

Proteomic databases

PaxDbO35973.
PRIDEO35973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021271; ENSMUSP00000021271; ENSMUSG00000020893.
ENSMUST00000166748; ENSMUSP00000132635; ENSMUSG00000020893.
GeneID18626.
KEGGmmu:18626.
UCSCuc007jpg.2. mouse.

Organism-specific databases

CTD5187.
MGIMGI:1098283. Per1.

Phylogenomic databases

eggNOGNOG253593.
GeneTreeENSGT00510000046467.
HOVERGENHBG008167.
InParanoidB1ASX0.
KOK02633.
OMAELGAVHS.
TreeFamTF318445.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_24972. Circadian Clock.

Gene expression databases

ArrayExpressO35973.
BgeeO35973.
CleanExMM_PER1.
GenevestigatorO35973.

Family and domain databases

InterProIPR001610. PAC.
IPR000014. PAS.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamPF12114. Period_C. 1 hit.
[Graphical view]
SMARTSM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
PROSITEPS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294576.
PROO35973.
SOURCESearch...

Entry information

Entry namePER1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot