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Reviewed, UniProtKB/Swiss-Prot P29349 (CSW_DROME)

Last modified June 16, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosine-protein phosphatase corkscrew
    EC=3.1.3.48
Gene names
Name: csw
ORF Names: CG3954
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw effects its role by mediating heteromeric protein interactions. Maternally required for normal determination of cell fates at the termini of the embryo. Required for cell fate specification of the ventral ectoderm, in the developing embryonic CNS and for embryonic tracheal cell migration. Functions during imaginal development for proper formation of adult structures such as eyes, aristae, L5 wing vein and the tarsal claw. Ref.1 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed uniformly throughout all tissues during embryogenesis. Ref.1

Developmental stage

Expressed throughout development. Ref.1

Miscellaneous

The PTPase domain is interrupted by a PTPase insert which shares no homologies with other PTPase proteins. This PTPase insert is reminiscent of the kinase insert within the kinase catalytic domains of several receptor tyrosine kinases.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 2 SH2 domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH2 domain
   Molecular functionDevelopmental protein
Hydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdorsal/ventral axis specification, ovarian follicular epithelium Ref.8

Inferred from mutant phenotype. Source: FlyBase

epidermal growth factor receptor signaling pathway Ref.8

Inferred from genetic interaction. Source: FlyBase

epithelial cell migration, open tracheal system Ref.8

Inferred from mutant phenotype. Source: FlyBase

fibroblast growth factor receptor signaling pathway Ref.8

Inferred from mutant phenotype. Source: FlyBase

imaginal disc development Ref.8

Inferred from mutant phenotype. Source: FlyBase

mesoderm development

Inferred from mutant phenotype. Source: FlyBase

mitotic cell cycle

Inferred from mutant phenotype. Source: FlyBase

primary branching, open tracheal system

Traceable author statement. Source: FlyBase

protein amino acid dephosphorylation

Inferred from direct assay. Source: FlyBase

regulation of compound eye photoreceptor development

Inferred from mutant phenotype. Source: FlyBase

sevenless signaling pathway

Traceable author statement. Source: FlyBase

terminal region determination Ref.1

Inferred from mutant phenotype. Source: UniProtKB

torso signaling pathway Ref.1

Inferred from genetic interaction. Source: UniProtKB

ventral midline development Ref.8

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentcytoplasm Ref.1

Non-traceable author statement. Source: UniProtKB

   Molecular functionnon-membrane spanning protein tyrosine phosphatase activity Ref.1

Non-traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

receptor signaling protein tyrosine phosphatase activity

Non-traceable author statement. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 2 (identifier: P29349-1)

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 1 (identifier: P29349-2)

Also known as: Y1229; A;

The sequence of this isoform differs from the canonical sequence as follows:
     810-845: GKMQQPAPPLRPRPGILKLLTSPVIFQQNSKTFPKT → AKFKNIPKDMIGLRPPSHAPALPPPPTPPRKT
Isoform 3 (identifier: P29349-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     810-845: GKMQQPAPPLRPRPGILKLLTSPVIFQQNSKTFPKT → AKFKNIPKDMIGLRPPSHAPALPPPPTPPRKT
Isoform 4 (identifier: P29349-4)

Also known as: 4A; B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: MSSRRWFHPT...LICAEPTTER → MLFNKCLEKL...TMRVQLHGYT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Tyrosine-protein phosphatase corkscrew
PRO_0000094850

Regions

Domain6 – 10196SH2 1
Domain111 – 20595SH2 2
Domain227 – 645419Tyrosine-protein phosphatase
Region289 – 444156PTPase insert (Cys/Ser-rich)

Sites

Active site5831Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue4191Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 159159Missing in isoform 3.
VSP_005139
Alternative sequence1 – 110110MSSRR…PTTER → MLFNKCLEKLSSSLGNVVNH KLQEKQVYNNNNINNNNNNT LNNNNAYNNQRNFEYERAIQ AHYGSKGRRSEERERSGKFK ASKGRKAKVTPPTETPEAQE PACKNCMTHDELAQIIKGVA KGADAQRNRDNRLQRRRRPL SAQPSAAASASTSTESLHRL TPSPQASYPATPTSWTATPP QFPAAFGGASCSNSTLSLLA TMRVQLHGYT in isoform 4.
VSP_005140
Alternative sequence810 – 84536GKMQQ…TFPKT → AKFKNIPKDMIGLRPPSHAP ALPPPPTPPRKT in isoform 1 and isoform 3.
VSP_005141
Natural variant1191K → T in strain: Kenya-HLa3, Kenya-HLa6, Kakamega-b1 and Makindu-b1. Ref.3
Natural variant7491G → S in strain: Ann Arbor1, DP CN BW, Kakamega-b1, Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6, Makindu-b5 and Reids2. Ref.3

Experimental info

Sequence conflict8151P → S in AAB02544. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 2147F0F2576202CC

FASTA84592,975
        10         20         30         40         50         60 
MSSRRWFHPT ISGIEAEKLL QEQGFDGSFL ARLSSSNPGA FTLSVRRGNE VTHIKIQNNG 

        70         80         90        100        110        120 
DFFDLYGGEK FATLPELVQY YMENGELKEK NGQAIELKQP LICAEPTTER WFHGNLSGKE 

       130        140        150        160        170        180 
AEKLILERGK NGSFLVRESQ SKPGDFVLSV RTDDKVTHVM IRWQDKKYDV GGGESFGTLS 

       190        200        210        220        230        240 
ELIDHYKRNP MVETCGTVVH LRQPFNATRI TAAGINARVE QLVKGGFWEE FESLQQDSRD 

       250        260        270        280        290        300 
TFSRNEGYKQ ENRLKNRYRN ILPYDHTRVK LLDVEHSVAG AEYINANYIR LPTDGDLYNM 

       310        320        330        340        350        360 
SSSSESLNSS VPSCPACTAA QTQRNCSNCQ LQNKTCVQCA VKSAILPYSN CATCSRKSDS 

       370        380        390        400        410        420 
LSKHKRSESS ASSSPSSGSG SGPGSSGTSG VSSVNGPGTP TNLTSGTAGC LVGLLKRHSN 

       430        440        450        460        470        480 
DSSGAVSISM AERERERERE MFKTYIATQG CLLTQQVNTV TDFWNMVWQE NTRVIVMTTK 

       490        500        510        520        530        540 
EYERGKEKCA RYWPDEGRSE QFGHARIQCV SENSTSDYTL REFLVSWRDQ PARRIFHYHF 

       550        560        570        580        590        600 
QVWPDHGVPA DPGCVLNFLQ DVNTRQSHLA QAGEKPGPIC VHCSAGIGRT GTFIVIDMIL 

       610        620        630        640        650        660 
DQIVRNGLDT EIDIQRTIQM VRSQRSGLVQ TEAQYKFVYY AVQHYIQTLI ARKRAEEQSL 

       670        680        690        700        710        720 
QVGREYTNIK YTGEIGNDSQ RSPLPPAISS ISLVPSKTPL TPTSADLGTG MGLSMGVGMG 

       730        740        750        760        770        780 
VGNKHASKQQ PPLPVVNCNN NNNGIGNSGC SNGGGSSTTS SSNGSSNGNI NALLGGIGLG 

       790        800        810        820        830        840 
LGGNMRKSNF YSDSLKQQQQ REEQAPAGAG KMQQPAPPLR PRPGILKLLT SPVIFQQNSK 


TFPKT 

« Hide

Isoform 1 (Y1229) (A).

Checksum: 03295DA37A8DA824
Show »

FASTA84192,431
Isoform 3 (C).

Checksum: CA4F23438AC61598
Show »

FASTA68274,528
Isoform 4 (4A) (B).

Checksum: CB95C38AB3038342
Show »

FASTA945103,768

References

« Hide 'large scale' references
[1]"Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso."
Perkins L.A., Larsen I., Perrimon N.
Cell 70:225-236(1992) [PubMed: 1638629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryo.
[2]"The role of the Drosophila corkscrew protein as a transducer downstream of receptor tyrosine kinases is functionally conserved."
Melnick M.B., Melnick C.B., Larsen I., Perrimon N., Perkins L.A.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 4).
Strain: DP CN BW.
[3]"Contrasting selection pressures on components of the Ras-mediated signal transduction pathway in Drosophila."
Riley R.M., Jin W., Gibson G.
Mol. Ecol. 12:1315-1323(2003) [PubMed: 12694293] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 4), VARIANTS THR-119 AND SER-749.
Strain: 10A, Ann Arbor1, Ann Arbor20, Ann Arbor3, Ann Arbor6, Kakamega-b1, Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6, Kenya-HLb1, M2, Makindu-b1, Makindu-b5, Nairobi-a, PYR2, Reids2 and Sapporo.
[4]"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. expand/collapse author list , 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] (ISOFORMS 1; 2 AND 4).
Strain: Berkeley.
[5]"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. expand/collapse author list , 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, ALTERNATIVE SPLICING.
[6]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 4).
Strain: Oregon-R.
[7]"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] (ISOFORM 1).
Strain: Berkeley.
Tissue: Ovary.
[8]"The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila."
Perkins L.A., Johnson M.R., Melnick M.B., Perrimon N.
Dev. Biol. 180:63-81(1996) [PubMed: 8948575] [Abstract]
Cited for: FUNCTION.
[9]"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-419, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

M94730 mRNA. Translation: AAA28433.1.
U19909 Genomic DNA. Translation: AAB02543.1.
U19909 Genomic DNA. Translation: AAB02544.1.
AY135117 Genomic DNA. Translation: AAN17607.1.
AY135117 Genomic DNA. Translation: AAN17608.1.
AY135118 Genomic DNA. Translation: AAN17609.1.
AY135118 Genomic DNA. Translation: AAN17610.1.
AY135119 Genomic DNA. Translation: AAN17611.1.
AY135119 Genomic DNA. Translation: AAN17612.1.
AY135120 Genomic DNA. Translation: AAN17613.1.
AY135120 Genomic DNA. Translation: AAN17614.1.
AY135121 Genomic DNA. Translation: AAN17615.1.
AY135121 Genomic DNA. Translation: AAN17616.1.
AY135122 Genomic DNA. Translation: AAN17617.1.
AY135122 Genomic DNA. Translation: AAN17618.1.
AY135123 Genomic DNA. Translation: AAN17619.1.
AY135123 Genomic DNA. Translation: AAN17620.1.
AY135124 Genomic DNA. Translation: AAN17621.1.
AY135124 Genomic DNA. Translation: AAN17622.1.
AY135125 Genomic DNA. Translation: AAN17623.1.
AY135125 Genomic DNA. Translation: AAN17624.1.
AY135126 Genomic DNA. Translation: AAN17625.1.
AY135126 Genomic DNA. Translation: AAN17626.1.
AY135127 Genomic DNA. Translation: AAN17627.1.
AY135127 Genomic DNA. Translation: AAN17628.1.
AY135128 Genomic DNA. Translation: AAN17629.1.
AY135128 Genomic DNA. Translation: AAN17630.1.
AY135129 Genomic DNA. Translation: AAN17631.1.
AY135129 Genomic DNA. Translation: AAN17632.1.
AY135130 Genomic DNA. Translation: AAN17633.1.
AY135130 Genomic DNA. Translation: AAN17634.1.
AY135131 Genomic DNA. Translation: AAN17635.1.
AY135131 Genomic DNA. Translation: AAN17636.1.
AY135132 Genomic DNA. Translation: AAN17637.1.
AY135132 Genomic DNA. Translation: AAN17638.1.
AY135133 Genomic DNA. Translation: AAN17639.1.
AY135133 Genomic DNA. Translation: AAN17640.1.
AY135134 Genomic DNA. Translation: AAN17641.1.
AY135134 Genomic DNA. Translation: AAN17642.1.
AE014298 Genomic DNA. Translation: AAF45724.2.
AE014298 Genomic DNA. Translation: AAG22389.2.
AE014298 Genomic DNA. Translation: AAF45725.1.
AL132797 Genomic DNA. Translation: CAB65870.1.
AL132797 Genomic DNA. Translation: CAB65871.1.
BT001484 mRNA. Translation: AAN71239.1.
PIRA43254.
RefSeqNP_477130.1.
NP_477131.1.
NP_726793.1.
UniGeneDm.5129

3D structure databases

HSSPHSSP built from PDB template 2SHP based on UniProtKB Q06124.
SMRP29349. Positions 3-289.
ModBaseSearch...

Protein-protein interaction databases

IntActP29349. 9 interactions.

Genome annotation databases

EnsemblFBgn0000382. Drosophila melanogaster. [Contig view]
GeneID45278.
KEGGdme:Dmel_CG3954.

Organism-specific databases

FlyBaseFBgn0000382. csw.

Phylogenomic databases

OMAP29349. ERWFHGN.

Enzyme and pathway databases

BRENDA3.1.3.48. 48.

Gene expression databases

ArrayExpressP29349.
GermOnlineCG3954. Drosophila melanogaster.

Family and domain databases

InterProIPR000980. SH2.
IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 2 hits.
PfamPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
ProDomPD000093. SH2. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
PROSITEPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio837970.

Entry information

Entry nameCSW_DROME
AccessionPrimary (citable) accession number: P29349
Secondary accession number(s): Q24032 expand/collapse secondary AC list , Q24033, Q8I074, Q8I0H8, Q8I0S4, Q8ISD5, Q8ISD6, Q9V3H1, Q9W524
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents