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O75145

- LIPA3_HUMAN

UniProt

O75145 - LIPA3_HUMAN

Protein

Liprin-alpha-3

Gene

PPFIA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (16 Feb 2004)
      Previous versions | rss
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    Functioni

    May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Liprin-alpha-3
    Alternative name(s):
    Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3
    Short name:
    PTPRF-interacting protein alpha-3
    Gene namesi
    Name:PPFIA3
    Synonyms:KIAA0654
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9247. PPFIA3.

    Subcellular locationi

    Cytoplasm By similarity. Cell surface By similarity
    Note: Colocalizes with PTPRF at the cell surface.By similarity

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11941194Liprin-alpha-3PRO_0000191029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine1 Publication
    Modified residuei207 – 2071Phosphoserine1 Publication
    Modified residuei645 – 6451PhosphoserineBy similarity
    Modified residuei714 – 7141Phosphothreonine1 Publication
    Modified residuei718 – 7181Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75145.
    PaxDbiO75145.
    PRIDEiO75145.

    PTM databases

    PhosphoSiteiO75145.

    Expressioni

    Tissue specificityi

    Expressed only in brain.1 Publication

    Gene expression databases

    BgeeiO75145.
    CleanExiHS_PPFIA3.
    GenevestigatoriO75145.

    Organism-specific databases

    HPAiHPA043567.
    HPA050340.

    Interactioni

    Subunit structurei

    Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS. Binds RIMS1, RIMS2, RIMS3 and RIMS4 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114111. 8 interactions.
    IntActiO75145. 2 interactions.
    MINTiMINT-3001008.
    STRINGi9606.ENSP00000335614.

    Structurei

    3D structure databases

    ProteinModelPortaliO75145.
    SMRiO75145. Positions 812-1115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini838 – 90467SAM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini953 – 101765SAM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1041 – 111070SAM 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili26 – 133108Sequence AnalysisAdd
    BLAST
    Coiled coili161 – 501341Sequence AnalysisAdd
    BLAST
    Coiled coili596 – 64449Sequence AnalysisAdd
    BLAST
    Coiled coili1014 – 104027Sequence AnalysisAdd
    BLAST

    Domaini

    The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type alpha/alpha. The C-terminal, non-coiled coil regions mediate heterodimerization type alpha/beta and interaction with PTPRD, PTPRF and PTPRS.

    Sequence similaritiesi

    Belongs to the liprin family. Liprin-alpha subfamily.Curated
    Contains 3 SAM (sterile alpha motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG322697.
    HOGENOMiHOG000017513.
    HOVERGENiHBG052330.
    InParanoidiO75145.
    OMAiDEPSKDW.
    OrthoDBiEOG7T7GS7.
    PhylomeDBiO75145.
    TreeFamiTF314207.

    Family and domain databases

    Gene3Di1.10.150.50. 2 hits.
    InterProiIPR029515. Liprin.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR021129. SAM_type1.
    [Graphical view]
    PANTHERiPTHR12587. PTHR12587. 1 hit.
    PfamiPF00536. SAM_1. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    SMARTiSM00454. SAM. 3 hits.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 3 hits.
    PROSITEiPS50105. SAM_DOMAIN. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75145-1) [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

    MMCEVMPTIS EDGRRGSALG PDEAGGELER LMVTMLTERE RLLETLREAQ     50
    DGLATAQLRL RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE 100
    EEIAELKAER NNTRLLLEHL ECLVSRHERS LRMTVVKRQA QSPGGVSSEV 150
    EVLKALKSLF EHHKALDEKV RERLRMALER VAVLEEELEL SNQETLNLRE 200
    QLSRRRSGLE EPGKDGDGQT LANGLGPGGD SNRRTAELEE ALERQRAEVC 250
    QLRERLAVLC RQMSQLEEEL GTAHRELGKA EEANSKLQRD LKEALAQRED 300
    MEERITTLEK RYLSAQREAT SLHDANDKLE NELASKESLY RQSEEKSRQL 350
    AEWLDDAKQK LQQTLQKAET LPEIEAQLAQ RVAALNKAEE RHGNFEERLR 400
    QLEAQLEEKN QELQRARQRE KMNDDHNKRL SETVDKLLSE SNERLQLHLK 450
    ERMGALEEKN SLSEEIANMK KLQDELLLNK EQLLAEMERM QMEIDQLRGR 500
    PPSSYSRSLP GSALELRYSQ APTLPSGAHL DPYVAGSGRA GKRGRWSGVK 550
    EEPSKDWERS APAGSIPPPF PGELDGSDEE EAEGMFGAEL LSPSGQADVQ 600
    TLAIMLQEQL EAINKEIKLI QEEKETTEQR AEELESRVSS SGLDSLGRYR 650
    SSCSLPPSLT TSTLASPSPP SSGHSTPRLA PPSPAREGTD KANHVPKEEA 700
    GAPRGEGPAI PGDTPPPTPR SARLERMTQA LALQAGSLED GGPPRGSEGT 750
    PDSLHKAPKK KSIKSSIGRL FGKKEKGRMG PPGRDSSSLA GTPSDETLAT 800
    DPLGLAKLTG PGDKDRRNKR KHELLEEACR QGLPFAAWDG PTVVSWLELW 850
    VGMPAWYVAA CRANVKSGAI MANLSDTEIQ REIGISNPLH RLKLRLAIQE 900
    MVSLTSPSAP ASSRTSTGNV WMTHEEMESL TATTKPETKE ISWEQILAYG 950
    DMNHEWVGND WLPSLGLPQY RSYFMESLVD ARMLDHLNKK ELRGQLKMVD 1000
    SFHRVSLHYG IMCLKRLNYD RKDLERRREE SQTQIRDVMV WSNERVMGWV 1050
    SGLGLKEFAT NLTESGVHGA LLALDETFDY SDLALLLQIP TQNAQARQLL 1100
    EKEFSNLISL GTDRRLDEDS AKSFSRSPSW RKMFREKDLR GVTPDSAEML 1150
    PPNFRSAAAG ALGSPGLPLR KLQPEGQTSG SSRADGVSVR TYSC 1194
    Length:1,194
    Mass (Da):133,496
    Last modified:February 16, 2004 - v3
    Checksum:i4DD92531AD8AE12D
    GO
    Isoform 2 (identifier: O75145-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         937-945: Missing.

    Note: May be due to exon skipping.

    Show »
    Length:1,185
    Mass (Da):132,365
    Checksum:i2D4AAB5416E93397
    GO

    Sequence cautioni

    The sequence BAA31629.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti878 – 8781E → K in AAC26101. (PubMed:9624153)Curated
    Sequence conflicti1011 – 10111I → V in AAC26101. (PubMed:9624153)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti563 – 5631A → S.3 Publications
    Corresponds to variant rs2303053 [ dbSNP | Ensembl ].
    VAR_017757

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei937 – 9459Missing in isoform 2. 2 PublicationsVSP_009392

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014554 mRNA. Translation: BAA31629.2. Different initiation.
    AK023850 mRNA. Translation: BAB14702.1.
    AK025972 mRNA. No translation available.
    AK289757 mRNA. Translation: BAF82446.1.
    CH471177 Genomic DNA. Translation: EAW52457.1.
    BC021255 mRNA. Translation: AAH21255.2.
    BC101518 mRNA. Translation: AAI01519.1.
    BC101520 mRNA. Translation: AAI01521.1.
    AF034800 mRNA. Translation: AAC26101.1.
    CCDSiCCDS12758.1. [O75145-1]
    RefSeqiNP_003651.1. NM_003660.3. [O75145-1]
    XP_006723513.1. XM_006723450.1. [O75145-2]
    UniGeneiHs.413748.
    Hs.604638.

    Genome annotation databases

    EnsembliENST00000334186; ENSP00000335614; ENSG00000177380. [O75145-1]
    ENST00000602351; ENSP00000473622; ENSG00000177380. [O75145-2]
    ENST00000602848; ENSP00000473418; ENSG00000177380.
    ENST00000602897; ENSP00000473423; ENSG00000177380.
    GeneIDi8541.
    KEGGihsa:8541.
    UCSCiuc002pmr.3. human. [O75145-1]
    uc002pms.3. human. [O75145-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014554 mRNA. Translation: BAA31629.2 . Different initiation.
    AK023850 mRNA. Translation: BAB14702.1 .
    AK025972 mRNA. No translation available.
    AK289757 mRNA. Translation: BAF82446.1 .
    CH471177 Genomic DNA. Translation: EAW52457.1 .
    BC021255 mRNA. Translation: AAH21255.2 .
    BC101518 mRNA. Translation: AAI01519.1 .
    BC101520 mRNA. Translation: AAI01521.1 .
    AF034800 mRNA. Translation: AAC26101.1 .
    CCDSi CCDS12758.1. [O75145-1 ]
    RefSeqi NP_003651.1. NM_003660.3. [O75145-1 ]
    XP_006723513.1. XM_006723450.1. [O75145-2 ]
    UniGenei Hs.413748.
    Hs.604638.

    3D structure databases

    ProteinModelPortali O75145.
    SMRi O75145. Positions 812-1115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114111. 8 interactions.
    IntActi O75145. 2 interactions.
    MINTi MINT-3001008.
    STRINGi 9606.ENSP00000335614.

    PTM databases

    PhosphoSitei O75145.

    Proteomic databases

    MaxQBi O75145.
    PaxDbi O75145.
    PRIDEi O75145.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334186 ; ENSP00000335614 ; ENSG00000177380 . [O75145-1 ]
    ENST00000602351 ; ENSP00000473622 ; ENSG00000177380 . [O75145-2 ]
    ENST00000602848 ; ENSP00000473418 ; ENSG00000177380 .
    ENST00000602897 ; ENSP00000473423 ; ENSG00000177380 .
    GeneIDi 8541.
    KEGGi hsa:8541.
    UCSCi uc002pmr.3. human. [O75145-1 ]
    uc002pms.3. human. [O75145-2 ]

    Organism-specific databases

    CTDi 8541.
    GeneCardsi GC19P049622.
    HGNCi HGNC:9247. PPFIA3.
    HPAi HPA043567.
    HPA050340.
    MIMi 603144. gene.
    neXtProti NX_O75145.
    PharmGKBi PA33568.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322697.
    HOGENOMi HOG000017513.
    HOVERGENi HBG052330.
    InParanoidi O75145.
    OMAi DEPSKDW.
    OrthoDBi EOG7T7GS7.
    PhylomeDBi O75145.
    TreeFami TF314207.

    Miscellaneous databases

    ChiTaRSi PPFIA3. human.
    GenomeRNAii 8541.
    NextBioi 31992.
    PROi O75145.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75145.
    CleanExi HS_PPFIA3.
    Genevestigatori O75145.

    Family and domain databases

    Gene3Di 1.10.150.50. 2 hits.
    InterProi IPR029515. Liprin.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR021129. SAM_type1.
    [Graphical view ]
    PANTHERi PTHR12587. PTHR12587. 1 hit.
    Pfami PF00536. SAM_1. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    SMARTi SM00454. SAM. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 3 hits.
    PROSITEi PS50105. SAM_DOMAIN. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-1194 (ISOFORM 2), VARIANT SER-563.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-563.
    5. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 909-1194 (ISOFORM 2), VARIANT SER-563.
      Tissue: Brain and Muscle.
    6. "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins."
      Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.
      J. Biol. Chem. 273:15611-15620(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-1194 (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH PTPRD; PTPRF AND PTPRS.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-207; THR-714 AND THR-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLIPA3_HUMAN
    AccessioniPrimary (citable) accession number: O75145
    Secondary accession number(s): A8K142
    , Q3MJA0, Q9H8B5, Q9UEW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3