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Protein

Liprin-alpha-2

Gene

Ppfia2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Alters PTPRF cellular localization and induces PTPRF clustering. 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 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Liprin-alpha-2
Alternative name(s):
Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2
Short name:
PTPRF-interacting protein alpha-2
Gene namesi
Name:Ppfia2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2443834. Ppfia2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell surface By similarity

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

GO - Cellular componenti

  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12571257Liprin-alpha-2PRO_0000191028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei237 – 2371PhosphothreonineCombined sources
Modified residuei239 – 2391PhosphoserineCombined sources
Modified residuei687 – 6871PhosphoserineCombined sources
Modified residuei689 – 6891PhosphoserineCombined sources
Modified residuei817 – 8171PhosphoserineCombined sources
Modified residuei820 – 8201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BSS9.
MaxQBiQ8BSS9.
PaxDbiQ8BSS9.
PRIDEiQ8BSS9.

PTM databases

iPTMnetiQ8BSS9.
PhosphoSiteiQ8BSS9.

Expressioni

Gene expression databases

BgeeiQ8BSS9.

Interactioni

Subunit structurei

Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi236493. 5 interactions.
IntActiQ8BSS9. 2 interactions.
STRINGi10090.ENSMUSP00000029404.

Structurei

3D structure databases

ProteinModelPortaliQ8BSS9.
SMRiQ8BSS9. Positions 871-1182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini898 – 96467SAM 1PROSITE-ProRule annotationAdd
BLAST
Domaini1020 – 108465SAM 2PROSITE-ProRule annotationAdd
BLAST
Domaini1108 – 117770SAM 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili29 – 154126Sequence analysisAdd
BLAST
Coiled coili185 – 23551Sequence analysisAdd
BLAST
Coiled coili264 – 541278Sequence analysisAdd
BLAST
Coiled coili643 – 69553Sequence analysisAdd
BLAST
Coiled coili1081 – 110727Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi115 – 528414Glu-richAdd
BLAST
Compositional biasi622 – 6276Poly-Asp

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 (By similarity).By similarity

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

eggNOGiKOG0249. Eukaryota.
ENOG410XP8Z. LUCA.
HOVERGENiHBG052330.
InParanoidiQ8BSS9.
PhylomeDBiQ8BSS9.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR029515. Liprin.
IPR030441. PPFIA2.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PANTHERiPTHR12587. PTHR12587. 3 hits.
PTHR12587:SF6. PTHR12587:SF6. 3 hits.
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]

Sequencei

Sequence statusi: Complete.

Q8BSS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMCEVMPTIN EDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR
60 70 80 90 100
ETQESLSLAQ QRLQDVIYDR DSLQRQLNSA LPQDIESLTG GLTGSKGADP
110 120 130 140 150
PEFAALTKEL NACREQLLEK EEEISELKAE RNNTRLLLEH LECLVSRHER
160 170 180 190 200
SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL FEHHKALDEK VRERLRVSLE
210 220 230 240 250
RVSALEEELA AANQEIVALR EQNVHIQRKM VSSEGSTESE HLEGMEAGQK
260 270 280 290 300
VHEKRLSNGS IDSTDDTSQI VELQELLEKQ NYEMAQMKER LTALSSRVGE
310 320 330 340 350
VEQEAETARK DLIKTEEMNT KYQRDIREAM AQKEDMEERI TTLEKRYLSA
360 370 380 390 400
QRESTSIHDM NDKLENELAN KEAILRQMEE KNRQLQERLE LAEQKLQQTM
410 420 430 440 450
RKAETLPEVE AELAQRIAAL TKAEERHGNI EERMRHLEGQ LEEKNQELQR
460 470 480 490 500
ARQREKMNEE HNKRLSDTVD RLLTESNERL QLHLKERMAA LEEKNVLIQE
510 520 530 540 550
SENFRKNLEE SLHDKVSLAE EIEKLRSELD QMKMRTGSLI EPTISRTHID
560 570 580 590 600
TSTELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW
610 620 630 640 650
NRTQQIGVLG SHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA
660 670 680 690 700
MMLQEQLDAI NKEIRLIQEE KESTELRAEE IENRVASVSL EGLNLARVHP
710 720 730 740 750
GTSITASVTA SSLASSSPPS GHSTPKLTPR SPAREMDRMG VMTLPSDLRK
760 770 780 790 800
HRRKIAVVEE DGREDKATIK CETSPPPTPR AVRMTHTLPS SYHNDARSSL
810 820 830 840 850
SASLEPDSLG LGSANSSQDS LHKAPKKKGI KSSIGRLFGK KEKARLGQLR
860 870 880 890 900
GFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG
910 920 930 940 950
PTVVAWLELW LGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH
960 970 980 990 1000
RLKLRLAIQE MVSLTSPSAP PTSRTPSGNV WVTHEEMENL TAPAKTKESE
1010 1020 1030 1040 1050
EGSWAQCPVF LQTLAYGDMN HEWIGNEWLP SLGLPQYRSY FMECLVDARM
1060 1070 1080 1090 1100
LDHLTKKDLR VHLKMVDSFH RTSLQYGIMC LKRLNYDRKE LERRREASQH
1110 1120 1130 1140 1150
EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA LDENFDYSSL
1160 1170 1180 1190 1200
ALLLQIPTQN TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ
1210 1220 1230 1240 1250
FPPREVHGIS MMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS

TVRTYSC
Length:1,257
Mass (Da):143,234
Last modified:February 16, 2004 - v2
Checksum:i2EC6B680B46EA4B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti516 – 5172VS → ER in AAH65133 (PubMed:15489334).Curated
Sequence conflicti798 – 7981Missing in AAH65133 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC111014 Genomic DNA. No translation available.
BC065133 mRNA. Translation: AAH65133.1.
AK030621 mRNA. Translation: BAC27051.1.
AK087448 mRNA. Translation: BAC39878.1.
CCDSiCCDS56746.1.
RefSeqiNP_796347.2. NM_177373.4.
UniGeneiMm.391424.

Genome annotation databases

GeneIDi327814.
KEGGimmu:327814.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC111014 Genomic DNA. No translation available.
BC065133 mRNA. Translation: AAH65133.1.
AK030621 mRNA. Translation: BAC27051.1.
AK087448 mRNA. Translation: BAC39878.1.
CCDSiCCDS56746.1.
RefSeqiNP_796347.2. NM_177373.4.
UniGeneiMm.391424.

3D structure databases

ProteinModelPortaliQ8BSS9.
SMRiQ8BSS9. Positions 871-1182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi236493. 5 interactions.
IntActiQ8BSS9. 2 interactions.
STRINGi10090.ENSMUSP00000029404.

PTM databases

iPTMnetiQ8BSS9.
PhosphoSiteiQ8BSS9.

Proteomic databases

EPDiQ8BSS9.
MaxQBiQ8BSS9.
PaxDbiQ8BSS9.
PRIDEiQ8BSS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi327814.
KEGGimmu:327814.

Organism-specific databases

CTDi8499.
MGIiMGI:2443834. Ppfia2.

Phylogenomic databases

eggNOGiKOG0249. Eukaryota.
ENOG410XP8Z. LUCA.
HOVERGENiHBG052330.
InParanoidiQ8BSS9.
PhylomeDBiQ8BSS9.

Miscellaneous databases

ChiTaRSiPpfia2. mouse.
PROiQ8BSS9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BSS9.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR029515. Liprin.
IPR030441. PPFIA2.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PANTHERiPTHR12587. PTHR12587. 3 hits.
PTHR12587:SF6. PTHR12587:SF6. 3 hits.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "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] OF 1-215 AND 1019-1257.
    Strain: C57BL/6J.
    Tissue: Eye and Pituitary.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; THR-237; SER-239; SER-687; SER-689; SER-817 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiLIPA2_MOUSE
AccessioniPrimary (citable) accession number: Q8BSS9
Secondary accession number(s): Q6P1D2, Q8BN73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: June 8, 2016
This is version 116 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

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 one 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.