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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene

Pip5k1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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-phosphatidylinositol-4-phosphate 5-kinase activity Source: MGI
    • ATP binding Source: UniProtKB-KW
    • kinase binding Source: MGI

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.68. 3474.
    ReactomeiREACT_272541. 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 Componenti: Chromosome 3

    Organism-specific databases

    MGIiMGI:107929. Pip5k1a.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: MGI
    • focal adhesion Source: MGI
    • lamellipodium Source: MGI
    • mRNA cleavage and polyadenylation specificity factor complex Source: Ensembl
    • nuclear speck Source: UniProtKB
    • nucleoplasm Source: MGI
    • nucleus Source: MGI
    • plasma membrane Source: UniProtKB
    • 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.
    GenevisibleiP70182. MM.

    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

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000102855.

    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. AlignAdd to basket

    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.
    CCDSiCCDS38542.1. [P70182-1]
    RefSeqiNP_001280636.1. NM_001293707.1. [P70182-3]
    NP_032873.2. NM_008847.3. [P70182-1]
    UniGeneiMm.296409.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000102855.

    PTM databases

    PhosphoSiteiP70182.

    Proteomic databases

    MaxQBiP70182.
    PaxDbiP70182.
    PRIDEiP70182.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi8394.
    MGIiMGI:107929. Pip5k1a.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi2.7.1.68. 3474.
    ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    ChiTaRSiPip5k1a. mouse.
    NextBioi294821.
    PROiP70182.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP70182.
    ExpressionAtlasiP70182. baseline and differential.
    GenevisibleiP70182. MM.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    There is confusion in the literature with phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due to the fact that frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-kinase type I alpha.Curated

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.