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Q61136

- PRP4B_MOUSE

UniProt

Q61136 - PRP4B_MOUSE

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Protein

Serine/threonine-protein kinase PRP4 homolog

Gene

Prpf4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei717 – 7171ATPPROSITE-ProRule annotation
Active sitei815 – 8151Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi693 – 7019ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: Ensembl
  3. protein kinase activity Source: MGI
  4. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PRP4 homolog (EC:2.7.11.1)
Alternative name(s):
PRP4 pre-mRNA-processing factor 4 homolog
Pre-mRNA protein kinase
Gene namesi
Name:Prpf4b
Synonyms:Cbp143, Prp4h, Prp4k, Prp4m, Prpk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:109584. Prpf4b.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: Ensembl
  2. chromosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10071006Serine/threonine-protein kinase PRP4 homologPRO_0000086587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei88 – 881Phosphoserine1 Publication
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei141 – 1411PhosphotyrosineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei242 – 2421PhosphoserineBy similarity
Modified residuei258 – 2581PhosphoserineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei294 – 2941PhosphoserineBy similarity
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei354 – 3541PhosphoserineBy similarity
Modified residuei356 – 3561PhosphoserineBy similarity
Modified residuei366 – 3661PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei385 – 3851PhosphothreonineBy similarity
Modified residuei387 – 3871PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity
Modified residuei431 – 4311Phosphoserine1 Publication
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei519 – 5191PhosphoserineBy similarity
Modified residuei520 – 5201PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei569 – 5691PhosphoserineBy similarity
Modified residuei576 – 5761Phosphoserine1 Publication
Modified residuei578 – 5781Phosphoserine1 Publication
Modified residuei580 – 5801Phosphoserine1 Publication
Modified residuei717 – 7171N6-acetyllysineBy similarity
Modified residuei849 – 8491Phosphotyrosine2 Publications
Modified residuei852 – 8521PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by Clk1.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61136.
PaxDbiQ61136.
PRIDEiQ61136.

PTM databases

PhosphoSiteiQ61136.

Expressioni

Gene expression databases

BgeeiQ61136.
ExpressionAtlasiQ61136. baseline and differential.
GenevestigatoriQ61136.

Interactioni

Subunit structurei

Identified in the spliceosome C complex (By similarity). Interacts with Clk1 C-terminus.By similarity

Protein-protein interaction databases

BioGridi202400. 2 interactions.
IntActiQ61136. 3 interactions.
MINTiMINT-1751441.

Structurei

3D structure databases

ProteinModelPortaliQ61136.
SMRiQ61136. Positions 603-1005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini687 – 1006320Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 497458Arg/Lys-rich (basic)Add
BLAST
Compositional biasi41 – 7939His-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOVERGENiHBG055182.
InParanoidiQ61136.
KOiK08827.
OMAiRSEIDKE.
OrthoDBiEOG76HQ1K.
TreeFamiTF315246.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61136-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAATEPPSLR EQAEMDDADN SEKSVNEENG EVSEDQSQNK HSRHKKKKHK
60 70 80 90 100
HRSKHKKHKH SSEEDRDKKH KHKHKHKKHK RKEVIEASDK EGLSPAKRTK
110 120 130 140 150
LDDLALLEDL EKQRALIKAE LDNELMEGKV QSGMGLILQG YESGSEEEGE
160 170 180 190 200
IHEKARNGNR SSTRSSSTRG KLEITDNKNS AKKRSKSRSK ERTRHRSDKR
210 220 230 240 250
KSKGAGEMLR EKANRSKSKE RRKSKSPSKR SKSQDQARKS KSPPLRRRSQ
260 270 280 290 300
EKVGKARSPA EEKMKSEEKG KIKDRKKSPI VNERSRDRSK KSKSPVDLRD
310 320 330 340 350
KSKDRRSRSK ERKSKRSEID KEKKPIKSPS KDASSGKENR SPSRRPGRSP
360 370 380 390 400
KRRSLSPKLR DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK
410 420 430 440 450
RREPERRRLS SPRTRPRDDI LGRCERSKDA SPINRWSPTR RRSRSPIRRR
460 470 480 490 500
SRSPLRRSRS PRRRSRSPRR RDRSRRSRSR LRRRSRSRGG HRRRSRSKVK
510 520 530 540 550
EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ RRIQRQAIVQ
560 570 580 590 600
KYKYLAEDSN ISVPSEPSSP QSSTRSRSPS PDDILERVAA DVKEYERENV
610 620 630 640 650
DTFEASVKAK HNLMTVEQNN GSSQKKILAP DMFTESDDMF AAYFDSARLR
660 670 680 690 700
AAGIGKDFKE NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN
710 720 730 740 750
VVRARDNARA NQEVAVKIIR NNELMQKTGL KELEFLKKLN DADPDDKFHC
760 770 780 790 800
LRLFRHFYHK QHLCLVFEPL SMNLREVLKK YGKDVGLHIK AVRSYSQQLF
810 820 830 840 850
LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH VADNDITPYL
860 870 880 890 900
VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL
910 920 930 940 950
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN
960 970 980 990 1000
PTKDLLADLI GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH

AFIQEKI
Length:1,007
Mass (Da):116,976
Last modified:July 27, 2011 - v3
Checksum:i18E1B7371E17AB4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1873SKS → IPG in AAC32042. (PubMed:9701556)Curated
Sequence conflicti223 – 2231K → I in AAC32042. (PubMed:9701556)Curated
Sequence conflicti478 – 4781R → K in AAM19102. (PubMed:12077342)Curated
Sequence conflicti478 – 4781R → K in AAC32042. (PubMed:9701556)Curated
Sequence conflicti633 – 6331F → L in AAB03269. (PubMed:9102632)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF283466 mRNA. Translation: AAM19102.1.
AK020579 mRNA. Translation: BAB32137.3.
AK021274 mRNA. Translation: BAB32358.3.
AK083926 mRNA. Translation: BAC39069.1.
CH466546 Genomic DNA. Translation: EDL40895.1.
BC141272 mRNA. Translation: AAI41273.1.
BC141273 mRNA. Translation: AAI41274.1.
AF033663 mRNA. Translation: AAC32042.1.
U48737 mRNA. Translation: AAB03269.1.
CCDSiCCDS26448.1.
RefSeqiNP_038858.2. NM_013830.2.
UniGeneiMm.10027.
Mm.482253.

Genome annotation databases

EnsembliENSMUST00000077853; ENSMUSP00000077019; ENSMUSG00000021413.
GeneIDi19134.
KEGGimmu:19134.
UCSCiuc007qbp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF283466 mRNA. Translation: AAM19102.1 .
AK020579 mRNA. Translation: BAB32137.3 .
AK021274 mRNA. Translation: BAB32358.3 .
AK083926 mRNA. Translation: BAC39069.1 .
CH466546 Genomic DNA. Translation: EDL40895.1 .
BC141272 mRNA. Translation: AAI41273.1 .
BC141273 mRNA. Translation: AAI41274.1 .
AF033663 mRNA. Translation: AAC32042.1 .
U48737 mRNA. Translation: AAB03269.1 .
CCDSi CCDS26448.1.
RefSeqi NP_038858.2. NM_013830.2.
UniGenei Mm.10027.
Mm.482253.

3D structure databases

ProteinModelPortali Q61136.
SMRi Q61136. Positions 603-1005.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202400. 2 interactions.
IntActi Q61136. 3 interactions.
MINTi MINT-1751441.

PTM databases

PhosphoSitei Q61136.

Proteomic databases

MaxQBi Q61136.
PaxDbi Q61136.
PRIDEi Q61136.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077853 ; ENSMUSP00000077019 ; ENSMUSG00000021413 .
GeneIDi 19134.
KEGGi mmu:19134.
UCSCi uc007qbp.2. mouse.

Organism-specific databases

CTDi 8899.
MGIi MGI:109584. Prpf4b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119032.
HOVERGENi HBG055182.
InParanoidi Q61136.
KOi K08827.
OMAi RSEIDKE.
OrthoDBi EOG76HQ1K.
TreeFami TF315246.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.

Miscellaneous databases

NextBioi 295762.
PROi Q61136.
SOURCEi Search...

Gene expression databases

Bgeei Q61136.
ExpressionAtlasi Q61136. baseline and differential.
Genevestigatori Q61136.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian PRP4 kinase copurifies and interacts with components of both the U5 snRNP and the N-CoR deacetylase complexes."
    Dellaire G., Makarov E.M., Cowger J.J.M., Longman D., Sutherland H.G.E., Luehrmann R., Torchia J., Bickmore W.A.
    Mol. Cell. Biol. 22:5141-5156(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus, Spinal ganglion and Urinary bladder.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Capturing novel mouse genes encoding chromosomal and other nuclear proteins."
    Tate P., Lee M., Tweedie S., Skarnes W.C., Bickmore W.A.
    J. Cell Sci. 111:2575-2585(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-1007.
  6. "Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue."
    Gross T., Lutzelberger M., Wiegmann H., Klingenhoff A., Shenoy S., Kaeufer N.F.
    Nucleic Acids Res. 25:1028-1035(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-94; SER-431; SER-437 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPRP4B_MOUSE
AccessioniPrimary (citable) accession number: Q61136
Secondary accession number(s): B2RUN6
, O88378, Q8BND8, Q8R4Y5, Q9CTL9, Q9CTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3