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O75334 (LIPA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPFIA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS. Ref.1

Subcellular location

Cytoplasm. Cell surface. Note: Colocalizes with PTPRF at the cell surface. Ref.1

Tissue specificity

Expressed only in brain. Ref.1

Domain

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 similarities

Belongs to the liprin family. Liprin-alpha subfamily.

Contains 3 SAM (sterile alpha motif) domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-matrix adhesion

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Traceable author statement Ref.1. Source: ProtInc

synapse

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75334-1)

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.
Isoform 2 (identifier: O75334-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-101: Missing.
     881-881: K → NTSG
     1238-1257: DVASSRLQRLDNSTVRTYSC → DDGVFSVYST
Isoform 3 (identifier: O75334-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1006-1011: Missing.
Isoform 4 (identifier: O75334-4)

The sequence of this isoform differs from the canonical sequence as follows:
     975-995: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12571257Liprin-alpha-2
PRO_0000191027

Regions

Domain898 – 96467SAM 1
Domain1020 – 108465SAM 2
Domain1108 – 117770SAM 3
Coiled coil29 – 154126 Potential
Coiled coil185 – 541357 Potential
Coiled coil643 – 69553 Potential
Coiled coil1081 – 110727 Potential
Compositional bias115 – 528414Glu-rich
Compositional bias622 – 6276Poly-Asp

Amino acid modifications

Modified residue5381Phosphoserine By similarity
Modified residue6891Phosphoserine By similarity
Modified residue7741Phosphoserine By similarity

Natural variations

Alternative sequence84 – 10118Missing in isoform 2.
VSP_043819
Alternative sequence8811K → NTSG in isoform 2.
VSP_043820
Alternative sequence975 – 99521Missing in isoform 4.
VSP_043821
Alternative sequence1006 – 10116Missing in isoform 3.
VSP_043822
Alternative sequence1238 – 125720DVASS…RTYSC → DDGVFSVYST in isoform 2.
VSP_043823

Experimental info

Sequence conflict3941Q → E in AAC26100. Ref.1
Sequence conflict4261R → T in AAC26100. Ref.1
Sequence conflict5171R → S in AAC26100. Ref.1
Sequence conflict6971R → M in AAC26100. Ref.1

Secondary structure

................................................... 1257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 13, 2012. Version 2.
Checksum: BD77601F444EEE10

FASTA1,257143,291
        10         20         30         40         50         60 
MMCEVMPTIN EDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR ETQESLSLAQ 

        70         80         90        100        110        120 
QRLQDVIYDR DSLQRQLNSA LPQDIESLTG GLAGSKGADP PEFAALTKEL NACREQLLEK 

       130        140        150        160        170        180 
EEEISELKAE RNNTRLLLEH LECLVSRHER SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL 

       190        200        210        220        230        240 
FEHHKALDEK VRERLRVSLE RVSALEEELA AANQEIVALR EQNVHIQRKM ASSEGSTESE 

       250        260        270        280        290        300 
HLEGMEPGQK VHEKRLSNGS IDSTDETSQI VELQELLEKQ NYEMAQMKER LAALSSRVGE 

       310        320        330        340        350        360 
VEQEAETARK DLIKTEEMNT KYQRDIREAM AQKEDMEERI TTLEKRYLSA QRESTSIHDM 

       370        380        390        400        410        420 
NDKLENELAN KEAILRQMEE KNRQLQERLE LAEQKLQQTM RKAETLPEVE AELAQRIAAL 

       430        440        450        460        470        480 
TKAEERHGNI EERMRHLEGQ LEEKNQELQR ARQREKMNEE HNKRLSDTVD RLLTESNERL 

       490        500        510        520        530        540 
QLHLKERMAA LEEKNVLIQE SETFRKNLEE SLHDKERLAE EIEKLRSELD QLKMRTGSLI 

       550        560        570        580        590        600 
EPTIPRTHLD TSAELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW 

       610        620        630        640        650        660 
NRTQQIGVLS SHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA MMLQEQLDAI 

       670        680        690        700        710        720 
NKEIRLIQEE KESTELRAEE IENRVASVSL EGLNLARVHP GTSITASVTA SSLASSSPPS 

       730        740        750        760        770        780 
GHSTPKLTPR SPAREMDRMG VMTLPSDLRK HRRKIAVVEE DGREDKATIK CETSPPPTPR 

       790        800        810        820        830        840 
ALRMTHTLPS SYHNDARSSL SVSLEPESLG LGSANSSQDS LHKAPKKKGI KSSIGRLFGK 

       850        860        870        880        890        900 
KEKARLGQLR GFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG 

       910        920        930        940        950        960 
PTVVAWLELW LGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE 

       970        980        990       1000       1010       1020 
MVSLTSPSAP PTSRTPSGNV WVTHEEMENL AAPAKTKESE EGSWAQCPVF LQTLAYGDMN 

      1030       1040       1050       1060       1070       1080 
HEWIGNEWLP SLGLPQYRSY FMECLVDARM LDHLTKKDLR VHLKMVDSFH RTSLQYGIMC 

      1090       1100       1110       1120       1130       1140 
LKRLNYDRKE LERRREASQH EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA 

      1150       1160       1170       1180       1190       1200 
LDENFDYSSL ALLLQIPTQN TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ 

      1210       1220       1230       1240       1250 
FPPREVHGIS MMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS TVRTYSC 

« Hide

Isoform 2 [UniParc].

Checksum: 8A789850F4E1E605
Show »

FASTA1,232140,673
Isoform 3 [UniParc].

Checksum: 18169E6210D89CE5
Show »

FASTA1,251142,603
Isoform 4 [UniParc].

Checksum: 27D95B02136893F6
Show »

FASTA1,236141,027

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPRD; PTPRF AND PTPRS.
Tissue: Brain, Fetal brain, Heart and Kidney.
[2]"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. expand/collapse author list , 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 2).
Tissue: Brain.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 3 AND 4).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF034799 mRNA. Translation: AAC26100.1.
AK126971 mRNA. Translation: BAG54412.1.
AC011316 Genomic DNA. No translation available.
AC069228 Genomic DNA. No translation available.
AC078920 Genomic DNA. No translation available.
AC079363 Genomic DNA. No translation available.
AC079408 Genomic DNA. No translation available.
BC104912 mRNA. Translation: AAI04913.1.
BC143485 mRNA. Translation: AAI43486.1.
IPIIPI00289271.
RefSeqNP_001207403.1. NM_001220474.1.
NP_001207404.1. NM_001220475.1.
NP_001207405.1. NM_001220476.1.
NP_003616.2. NM_003625.3.
UniGeneHs.506216.
Hs.737103.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TACX-ray2.20B866-1193[»]
3TADX-ray2.90A/B866-1193[»]
ProteinModelPortalO75334.
SMRO75334. Positions 871-1182.
ModBaseSearch...

Protein-protein interaction databases

IntActO75334. 3 interactions.
STRING9606.ENSP00000388373.

PTM databases

PhosphoSiteO75334.

Proteomic databases

PaxDbO75334.
PRIDEO75334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000548586; ENSP00000449338; ENSG00000139220.
ENST00000549325; ENSP00000450298; ENSG00000139220.
ENST00000549396; ENSP00000450337; ENSG00000139220.
ENST00000552948; ENSP00000447868; ENSG00000139220.
GeneID8499.
KEGGhsa:8499.

Organism-specific databases

CTD8499.
GeneCardsGC12M081584.
H-InvDBHIX0010857.
HGNCHGNC:9246. PPFIA2.
HPAHPA040724.
MIM603143. gene.
neXtProtNX_O75334.
PharmGKBPA33567.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322697.
HOVERGENHBG052330.
InParanoidO75334.

Gene expression databases

ArrayExpressO75334.
BgeeO75334.
CleanExHS_PPFIA2.
GenevestigatorO75334.
GermOnlineENSG00000139220. Homo sapiens.

Family and domain databases

Gene3D1.10.150.50. 2 hits.
InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR021129. SAM_type1.
[Graphical view]
PfamPF00536. SAM_1. 2 hits.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 3 hits.
[Graphical view]
SUPFAMSSF47769. SAM_homology. 3 hits.
PROSITEPS50105. SAM_DOMAIN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPFIA2. human.
GenomeRNAi8499.
NextBio31801.
SOURCESearch...

Entry information

Entry nameLIPA2_HUMAN
AccessionPrimary (citable) accession number: O75334
Secondary accession number(s): B3KXA0 expand/collapse secondary AC list , B7ZKZ5, F8VP68, Q2M3G8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: June 13, 2012
Last modified: April 3, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families