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P00522

- ABL_DROME

UniProt

P00522 - ABL_DROME

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Protein
Tyrosine-protein kinase Abl
Gene
Abl, ABL-1, Dash, CG4032
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways.3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei400 – 4001ATP By similarity
Active sitei492 – 4921Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi377 – 3859ATP By similarity
Nucleotide bindingi445 – 4517ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: FlyBase
  3. protein binding Source: UniProtKB
  4. protein tyrosine kinase activity Source: FlyBase

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. axon midline choice point recognition Source: FlyBase
  3. axonogenesis Source: FlyBase
  4. central nervous system development Source: FlyBase
  5. compound eye development Source: FlyBase
  6. cytoplasmic transport, nurse cell to oocyte Source: FlyBase
  7. dorsal closure Source: FlyBase
  8. epithelial cell morphogenesis Source: FlyBase
  9. morphogenesis of an epithelium Source: FlyBase
  10. motor neuron axon guidance Source: FlyBase
  11. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  12. neuron migration Source: FlyBase
  13. peptidyl-tyrosine phosphorylation Source: FlyBase
  14. photoreceptor cell axon guidance Source: FlyBase
  15. planar cell polarity pathway involved in axis elongation Source: FlyBase
  16. positive regulation of protein export from nucleus Source: FlyBase
  17. protein phosphorylation Source: FlyBase
  18. regulation of actin polymerization or depolymerization Source: FlyBase
  19. regulation of cell shape Source: FlyBase
  20. regulation of protein localization Source: FlyBase
  21. regulation of protein stability Source: FlyBase
  22. ventral cord development Source: FlyBase
  23. ventral furrow formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.
REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
SignaLinkiP00522.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Abl (EC:2.7.10.2)
Alternative name(s):
D-ash
Protein abelson
Gene namesi
Name:Abl
Synonyms:ABL-1, Dash
ORF Names:CG4032
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000017. Abl.

Subcellular locationi

GO - Cellular componenti

  1. adherens junction Source: FlyBase
  2. apical cortex Source: FlyBase
  3. axon Source: FlyBase
  4. cell cortex Source: FlyBase
  5. cell-cell junction Source: FlyBase
  6. cytoplasm Source: FlyBase
  7. cytosol Source: FlyBase
  8. extrinsic component of plasma membrane Source: FlyBase
  9. muscle tendon junction Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Both loss- and gain-of-function mutants exhibit neurons within the pCC/MP2 pathway that incorrectly project across the midline. Loss of Abl disrupts cell migration and cell shape changes during dorsal closure.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16201620Tyrosine-protein kinase Abl
PRO_0000088054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei522 – 5221Phosphotyrosine; by autocatalysis By similarity
Modified residuei1497 – 14971Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00522.

Expressioni

Tissue specificityi

Arm and ena colocalize with Abl at adherens junctions throughout development.2 Publications

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP00522.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
enaQ8T4F72EBI-534090,EBI-466810
LarP166214EBI-534090,EBI-668630

Protein-protein interaction databases

BioGridi69904. 15 interactions.
IntActiP00522. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP00522.
SMRiP00522. Positions 172-639.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 24862SH3
Add
BLAST
Domaini254 – 34693SH2
Add
BLAST
Domaini371 – 627257Protein kinase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi510 – 53425Kinase activation loop By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 9291Gly/Ser-rich
Add
BLAST
Compositional biasi1056 – 108025Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091347.
InParanoidiP00522.
KOiK06619.
OrthoDBiEOG7GTT2V.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00522-1 [UniParc]FASTAAdd to Basket

« Hide

MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP     50
LGGGSTLRGS RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP 100
TVGLNIFTEH NEALLQSRPL PHIPAGSTAA SLLADAAELQ QHQQDSGGLG 150
LQGSSLGGGH SSTTSVFESA HRWTSKENLL APGPEEDDPQ LFVALYDFQA 200
GGENQLSLKK GEQVRILSYN KSGEWCEAHS DSGNVGWVPS NYVTPLNSLE 250
KHSWYHGPIS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH 300
YRISEDPDGK VFVTQEAKFN TLAELVHHHS VPHEGHGLIT PLLYPAPKQN 350
KPTVFPLSPE PDEWEICRTD IMMKHKLGGG QYGEVYEAVW KRYGNTVAVK 400
TLKEDTMALK DFLEEAAIMK EMKHPNLVQL IGVCTREPPF YIITEFMSHG 450
NLLDFLRSAG RETLDAVALL YMATQIASGM SYLESRNYIH RDLAARNCLV 500
GDNKLVKVAD FGLARLMRDD TYTAHAGAKF PIKWTAPEGL AYNKFSTKSD 550
VWAFGVLLWE IATYGMSPYP AIDLTDVYHK LDKGYRMERP PGCPPEVYDL 600
MRQCWQWDAT DRPTFKSIHH ALEHMFQESS ITEAVEKQLN ANATSASSSA 650
PSTSGVATGG GATTTTAASG CASSSSATAS LSLTPQMVKK GLPGGQALTP 700
NAHHNDPHQQ QASTPMSETG STSTKLSTFS SQGKGNVQMR RTTNKQGKQA 750
PAPPKRTSLL SSSRDSTYRE EDPANARCNF IDDLSTNGLA RDINSLTQRY 800
DSETDPAADP DTDATGDSLE QSLSQVIAAP VTNKMQHSLH SGGGGGGIGP 850
RSSQQHSSFK RPTGTPVMGN RGLETRQSKR SQLHSQAPGP GPPSTQPHHG 900
NNGVVTSAHP ITVGALDVMN VKQVVNRYGT LPKGARIGAY LDSLEDSSEA 950
APALPATAPS LPPANGHATP PAARLNPKAS PIPPQQMIRS NSSGGVTMQN 1000
NAAASLNKLQ RHRTTTEGTM MTFSSFRAGG SSSSPKRSAS GVASGVQPAL 1050
ANLEFPPPPL DLPPPPEEFE GGPPPPPPAP ESAVQAIQQH LHAQLPNNGN 1100
ISNGNGTNNN DSSHNDVSNI APSVEEASSR FGVSLRKREP STDSCSSLGS 1150
PPEDLKEKLI TEIKAAGKDT APASHLANGS GIAVVDPVSL LVTELAESMN 1200
LPKPPPQQQQ KLTNGNSTGS GFKAQLKKVE PKKMSAPMPK AEPANTIIDF 1250
KAHLRRVDKE KEPATPAPAP ATVAVANNAN CNTTGTLNRK EDGSKKFSQA 1300
MQKTEIKIDV TNSNVEADAG AAGEGDLGKR RSTGSINSLK KLWEQQPPAP 1350
DYATSTILQQ QPSVVNGGGT PNAQLSPKYG MKSGAINTVG TLPAKLGNKQ 1400
PPAAPPPPPP NCTTSNSSTT SISTSSRDCT SRQQASSTIK TSHSTQLFTD 1450
DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP 1500
IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK 1550
LNILHNSCVI FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN 1600
ERLVAEVGQS LRQISNALNR 1620
Length:1,620
Mass (Da):171,588
Last modified:April 12, 2005 - v3
Checksum:i14287B02CC8FE86B
GO

Sequence cautioni

The sequence AAL13726.1 differs from that shown. Reason: Frameshift at position 323.
The sequence AAA28934.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1368AASLLADA → RPLFWRI in AAA28934. 1 Publication
Sequence conflicti357 – 3604LSPE → ASAQ1 Publication
Sequence conflicti628 – 6314ESSI → VGDV1 Publication
Sequence conflicti1241 – 12433AEP → RT in AAA28934. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19692, M19690, M19691 Genomic DNA. Translation: AAA28934.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF49431.2.
AY058497 mRNA. Translation: AAL13726.1. Frameshift.
K01042 Genomic DNA. Translation: AAA28443.1.
PIRiA28128. TVFFA.
RefSeqiNP_524843.2. NM_080104.3.
UniGeneiDm.5397.

Genome annotation databases

EnsemblMetazoaiFBtr0075357; FBpp0075116; FBgn0000017.
GeneIDi45821.
KEGGidme:Dmel_CG4032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19692 , M19690 , M19691 Genomic DNA. Translation: AAA28934.1 . Sequence problems.
AE014296 Genomic DNA. Translation: AAF49431.2 .
AY058497 mRNA. Translation: AAL13726.1 . Frameshift.
K01042 Genomic DNA. Translation: AAA28443.1 .
PIRi A28128. TVFFA.
RefSeqi NP_524843.2. NM_080104.3.
UniGenei Dm.5397.

3D structure databases

ProteinModelPortali P00522.
SMRi P00522. Positions 172-639.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 69904. 15 interactions.
IntActi P00522. 4 interactions.

Proteomic databases

PaxDbi P00522.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075357 ; FBpp0075116 ; FBgn0000017 .
GeneIDi 45821.
KEGGi dme:Dmel_CG4032.

Organism-specific databases

CTDi 45821.
FlyBasei FBgn0000017. Abl.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091347.
InParanoidi P00522.
KOi K06619.
OrthoDBi EOG7GTT2V.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1994.
Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.
REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
SignaLinki P00522.

Miscellaneous databases

GenomeRNAii 45821.
NextBioi 838372.
PROi P00522.

Gene expression databases

Bgeei P00522.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence, structure, and tyrosine kinase activity of the Drosophila melanogaster Abelson proto-oncogene homolog."
    Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M.
    Mol. Cell. Biol. 8:843-853(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1620.
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Nucleotide sequences of the Drosophila src and abl homologs: conservation and variability in the src family oncogenes."
    Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.
    Cell 35:393-401(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-631.
  6. "Roles of Armadillo, a Drosophila catenin, during central nervous system development."
    Loureiro J., Peifer M.
    Curr. Biol. 8:622-632(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  7. "Abelson kinase regulates epithelial morphogenesis in Drosophila."
    Grevengoed E.E., Loureiro J.J., Jesse T.L., Peifer M.
    J. Cell Biol. 155:1185-1198(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  8. "Abelson tyrosine kinase is required to transduce midline repulsive cues."
    Hsouna A., Kim Y.-S., VanBerkum M.F.A.
    J. Neurobiol. 57:15-30(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiABL_DROME
AccessioniPrimary (citable) accession number: P00522
Secondary accession number(s): Q95TV1, Q9VV86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 12, 2005
Last modified: September 3, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi