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P70182

- PI51A_MOUSE

UniProt

P70182 - PI51A_MOUSE

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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene

Pip5k1a

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

Functioni

Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs.5 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Enzyme regulationi

Activated by phosphatidic acid.2 Publications

Kineticsi

  1. KM=26 µM for PtdIns4P1 Publication
  2. KM=33 µM for ATP1 Publication

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. activation of Rac GTPase activity Source: UniProtKB
  3. cell chemotaxis Source: UniProtKB
  4. fibroblast migration Source: MGI
  5. focal adhesion assembly Source: UniProtKB
  6. phosphatidylinositol metabolic process Source: MGI
  7. phosphatidylinositol phosphorylation Source: GOC
  8. phospholipid biosynthetic process Source: Ensembl
  9. protein targeting to plasma membrane Source: UniProtKB
  10. ruffle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198973. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (EC:2.7.1.68)
Short name:
PIP5K1-alpha
Short name:
PtdIns(4)P-5-kinase 1 alpha
Alternative name(s):
68 kDa type I phosphatidylinositol 4-phosphate 5-kinase
Phosphatidylinositol 4-phosphate 5-kinase type I alpha
Short name:
PIP5KIalpha
Phosphatidylinositol 4-phosphate 5-kinase type I beta
Short name:
PI4P5KIbeta
Gene namesi
Name:Pip5k1a
Synonyms:Pip5k1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:107929. Pip5k1a.

Subcellular locationi

Cell membrane 1 Publication. Nucleus speckle By similarity. Cytoplasm 1 Publication. Cell projectionruffle By similarity
Note: Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. lamellipodium Source: Ensembl
  3. mRNA cleavage and polyadenylation specificity factor complex Source: Ensembl
  4. nuclear speck Source: UniProtKB
  5. nucleus Source: MGI
  6. plasma membrane Source: UniProtKB
  7. ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Survive to adulthood, but bred poorly and display reduced fertility. Failed to form any vessel occlusion after chemical-induced carotid injury. Platelets have defective aggregation. Bone marrow-derived macrophages are defective in actin polymerization during phagocytosis. PIP5K1A and PIP5K1C double mutant mice are embryonic lethal.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Phosphatidylinositol 4-phosphate 5-kinase type-1 alphaPRO_0000185457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki88 – 88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP70182.
PaxDbiP70182.
PRIDEiP70182.

PTM databases

PhosphoSiteiP70182.

Expressioni

Tissue specificityi

Highest expression in brain. Also detected in skeletal muscle, testis, brain and lung.2 Publications

Developmental stagei

Expression is highest during early embryogenesis and slightly decreases over time.1 Publication

Gene expression databases

BgeeiP70182.
ExpressionAtlasiP70182. baseline and differential.
GenevestigatoriP70182.

Interactioni

Subunit structurei

Interacts with RAC1. Interacts with TUT1 (By similarity). Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP70182.
SMRiP70182. Positions 67-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 434369PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiP70182.
KOiK00889.
OMAiETEDHMG.
OrthoDBiEOG70W3DM.
PhylomeDBiP70182.
TreeFamiTF319618.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P70182-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MASASSGPAA AGFSSLDAGA PAGTAAASGI KRATVSEGPS ASVMPVKKIG
60 70 80 90 100
HRSVDSSGET TYKKTTSSAL KGAIQLGITH TVGSLSTKPE RDVLMQDFYV
110 120 130 140 150
VESIFFPSEG SNLTPAHHYN DFRFKTYAPV AFRYFRELFG IRPDDYLYSL
160 170 180 190 200
CSEPLIELSN SGASGSLFYV SSDDEFIIKT VQHKEAEFLQ KLLPGYYMNL
210 220 230 240 250
NQNPRTLLPK FYGLYCVQAG GKNIRIVVMN NLLPRSVKMH MKYDLKGSTY
260 270 280 290 300
KRRASQKERE KTLPTFKDLD FLQDIPDGLF LDADMYSALC KTLQRDCLVL
310 320 330 340 350
QSFKIMDYSL LMSIHNMDHA QREPTSNDTQ YSADTRRPAP QKALYSTAME
360 370 380 390 400
SIQGEARRGG TVETEDHMGG IPARNNKGER LLLYIGIIDI LQSYRFVKKL
410 420 430 440 450
EHSWKALVHD GDTVSVHRPG FYAERFQRFM CNTVFKKIPL KPSPTKKFRS
460 470 480 490 500
GPSFSRRSGP SGNSCTSQLM ASGEHRAQVT TKAEVEPDVH LGRPDVLPQT
510 520 530 540
PPLEEISEGS PVPGPSFSPV VGQPLQILNL SSTLEKLDVA ESEFTH
Length:546
Mass (Da):60,485
Last modified:October 25, 2005 - v2
Checksum:i6E895F22A75B7140
GO
Isoform 2 (identifier: P70182-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-27: A → AA
     238-431: Missing.

Note: No experimental confirmation available.

Show »
Length:353
Mass (Da):38,098
Checksum:i99BDCE9D767BE901
GO
Isoform 3 (identifier: P70182-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-27: A → AA

Note: No experimental confirmation available.

Show »
Length:547
Mass (Da):60,556
Checksum:i65889A83CE3F2B32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071P → R in BAE29943. (PubMed:16141072)Curated
Sequence conflicti107 – 1071P → R in BAE30850. (PubMed:16141072)Curated
Sequence conflicti120 – 1201N → S in AAH03763. (PubMed:15489334)Curated
Sequence conflicti258 – 2581E → D in BAA13031. (PubMed:8798574)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 271A → AA in isoform 2 and isoform 3. 2 PublicationsVSP_053437
Alternative sequencei238 – 431194Missing in isoform 2. 1 PublicationVSP_016009Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86177 mRNA. Translation: BAA13031.1.
AK150898 mRNA. Translation: BAE29943.1.
AK151984 mRNA. Translation: BAE30850.1.
AK158062 mRNA. Translation: BAE34344.1.
AC087062 Genomic DNA. No translation available.
AC131769 Genomic DNA. No translation available.
BC003763 mRNA. Translation: AAH03763.1.
BC031774 mRNA. Translation: AAH31774.1.
CCDSiCCDS38542.1. [P70182-1]
RefSeqiNP_001280636.1. NM_001293707.1. [P70182-3]
NP_032873.2. NM_008847.3. [P70182-1]
UniGeneiMm.296409.

Genome annotation databases

EnsembliENSMUST00000107233; ENSMUSP00000102852; ENSMUSG00000028126. [P70182-3]
ENSMUST00000107236; ENSMUSP00000102855; ENSMUSG00000028126. [P70182-1]
GeneIDi18720.
KEGGimmu:18720.
UCSCiuc008qhx.2. mouse. [P70182-1]
uc008qhy.2. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86177 mRNA. Translation: BAA13031.1 .
AK150898 mRNA. Translation: BAE29943.1 .
AK151984 mRNA. Translation: BAE30850.1 .
AK158062 mRNA. Translation: BAE34344.1 .
AC087062 Genomic DNA. No translation available.
AC131769 Genomic DNA. No translation available.
BC003763 mRNA. Translation: AAH03763.1 .
BC031774 mRNA. Translation: AAH31774.1 .
CCDSi CCDS38542.1. [P70182-1 ]
RefSeqi NP_001280636.1. NM_001293707.1. [P70182-3 ]
NP_032873.2. NM_008847.3. [P70182-1 ]
UniGenei Mm.296409.

3D structure databases

ProteinModelPortali P70182.
SMRi P70182. Positions 67-352.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P70182.

Proteomic databases

MaxQBi P70182.
PaxDbi P70182.
PRIDEi P70182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000107233 ; ENSMUSP00000102852 ; ENSMUSG00000028126 . [P70182-3 ]
ENSMUST00000107236 ; ENSMUSP00000102855 ; ENSMUSG00000028126 . [P70182-1 ]
GeneIDi 18720.
KEGGi mmu:18720.
UCSCi uc008qhx.2. mouse. [P70182-1 ]
uc008qhy.2. mouse.

Organism-specific databases

CTDi 8394.
MGIi MGI:107929. Pip5k1a.

Phylogenomic databases

eggNOGi COG5253.
GeneTreei ENSGT00760000119184.
HOGENOMi HOG000193876.
HOVERGENi HBG052818.
InParanoidi P70182.
KOi K00889.
OMAi ETEDHMG.
OrthoDBi EOG70W3DM.
PhylomeDBi P70182.
TreeFami TF319618.

Enzyme and pathway databases

Reactomei REACT_198973. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSi Pip5k1a. mouse.
NextBioi 294821.
PROi P70182.
SOURCEi Search...

Gene expression databases

Bgeei P70182.
ExpressionAtlasi P70182. baseline and differential.
Genevestigatori P70182.

Family and domain databases

Gene3Di 3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProi IPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view ]
PANTHERi PTHR23086. PTHR23086. 1 hit.
Pfami PF01504. PIP5K. 1 hit.
[Graphical view ]
SMARTi SM00330. PIPKc. 1 hit.
[Graphical view ]
PROSITEi PS51455. PIPK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs encoding two isoforms of 68-kDa type I phosphatidylinositol 4-phosphate 5-kinase."
    Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T., Oka Y.
    J. Biol. Chem. 271:23611-23614(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Insulinoma.
  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] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Inner ear and Macrophage.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORMS 1 AND 2).
    Tissue: Eye and Mammary tumor.
  5. "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family."
    Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y.
    J. Biol. Chem. 273:8741-8748(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly."
    Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.
    Curr. Biol. 10:153-156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1.
  7. "Loss of PIP5KIbeta demonstrates that PIP5KI isoform-specific PIP2 synthesis is required for IP3 formation."
    Wang Y., Chen X., Lian L., Tang T., Stalker T.J., Sasaki T., Kanaho Y., Brass L.F., Choi J.K., Hartwig J.H., Abrams C.S.
    Proc. Natl. Acad. Sci. U.S.A. 105:14064-14069(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELETS, DISRUPTION PHENOTYPE.
  8. "Essential and unique roles of PIP5K-gamma and -alpha in Fcgamma receptor-mediated phagocytosis."
    Mao Y.S., Yamaga M., Zhu X., Wei Y., Sun H.-Q., Wang J., Yun M., Wang Y., Di Paolo G., Bennett M., Mellman I., Abrams C.S., De Camilli P., Lu C.Y., Yin H.L.
    J. Cell Biol. 184:281-296(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHAGOCYTOSIS, DISRUPTION PHENOTYPE.
  9. "Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5-bisphosphate synthesis in the brain."
    Volpicelli-Daley L.A., Lucast L., Gong L.-W., Liu L., Sasaki J., Sasaki T., Abrams C.S., Kanaho Y., De Camilli P.
    J. Biol. Chem. 285:28708-28714(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EMBRYOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPI51A_MOUSE
AccessioniPrimary (citable) accession number: P70182
Secondary accession number(s): F8WIX5
, Q3U917, Q8K0D3, Q99L80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 26, 2014
This is version 111 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3