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Q13136 (LIPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Liprin-alpha-1
Alternative name(s):
LAR-interacting protein 1
Short name=LIP-1
Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1
Short name=PTPRF-interacting protein alpha-1
Gene names
Name:PPFIA1
Synonyms:LIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Interacts with GIT1, KIF1A and GRIP1 By similarity. Ref.1 Ref.5 Ref.6

Subcellular location

Cytoplasm. Note: Colocalizes with PTPRF at the ends of focal adhesions most proximal to the cell nucleus. Ref.1

Tissue specificity

Ubiquitous. Ref.1 Ref.6

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.

Sequence caution

The sequence BAA08353.1 differs from that shown. Reason: Frameshift at positions 1033, 1041, 1045, 1067 and 1113.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gria2P194912EBI-745426,EBI-77718From a different organism.
Grip1P978794EBI-745426,EBI-936113From a different organism.
MBIPQ9NS733EBI-745426,EBI-741953
PPP2R5DQ147382EBI-745426,EBI-396563

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13136-1)

Also known as: LAR-interacting protein 1b; LIP.1b; b;

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: Q13136-2)

Also known as: LAR-interacting protein 1a; LIP.1a; a;

The sequence of this isoform differs from the canonical sequence as follows:
     1185-1202: NVSGTQRLDSATVRTYSC → M
Note: Due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12021202Liprin-alpha-1
PRO_0000191026

Regions

Domain878 – 94467SAM 1
Domain963 – 102765SAM 2
Domain1051 – 112070SAM 3
Coiled coil34 – 141108 Potential
Coiled coil176 – 21439 Potential
Coiled coil249 – 521273 Potential
Coiled coil623 – 66947 Potential
Coiled coil847 – 87125 Potential
Coiled coil1021 – 105030 Potential
Compositional bias17 – 259Poly-Gly

Amino acid modifications

Modified residue2301Phosphothreonine Ref.10
Modified residue2391Phosphoserine Ref.12 Ref.14
Modified residue2421Phosphoserine Ref.10 Ref.12 Ref.14
Modified residue2441Phosphoserine Ref.10 Ref.14
Modified residue4481Phosphoserine Ref.14
Modified residue6931Phosphoserine Ref.12
Modified residue11591Phosphothreonine Ref.12

Natural variations

Alternative sequence1185 – 120218NVSGT…RTYSC → M in isoform 2.
VSP_009391
Natural variant711V → I.
Corresponds to variant rs546502 [ dbSNP | Ensembl ].
VAR_017756
Natural variant10721L → F.
Corresponds to variant rs11236045 [ dbSNP | Ensembl ].
VAR_049998

Experimental info

Sequence conflict4921E → G in AAH34046. Ref.3
Sequence conflict5551P → T in AAH34046. Ref.3
Sequence conflict672 – 6743LGR → EFG in BAA08353. Ref.4
Sequence conflict800 – 8012KK → EE in BAA08353. Ref.4
Sequence conflict8661E → G in AAH34046. Ref.3
Sequence conflict9941L → Q in BAA08353. Ref.4
Sequence conflict10231C → S in BAA08353. Ref.4
Sequence conflict10441E → EVRV in BAA08353. Ref.4
Sequence conflict1121 – 11233GTD → PEF in BAA08353. Ref.4

Secondary structure

... 1202
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LAR-interacting protein 1b) (LIP.1b) (b) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C8CF7C20B298BFB1

FASTA1,202135,779
        10         20         30         40         50         60 
MMCEVMPTIS EAEGPPGGGG GHGSGSPSQP DADSHFEQLM VSMLEERDRL LDTLRETQET 

        70         80         90        100        110        120 
LALTQGKLHE VGHERDSLQR QLNTALPQEF AALTKELNVC REQLLEREEE IAELKAERNN 

       130        140        150        160        170        180 
TRLLLEHLEC LVSRHERSLR MTVVKRQAQS PAGVSSEVEV LKALKSLFEH HKALDEKVRE 

       190        200        210        220        230        240 
RLRVALERCS LLEEELGATH KELMILKEQN NQKKTLTDGV LDINHEQENT PSTSGKRSSD 

       250        260        270        280        290        300 
GSLSHEEDLA KVIELQEIIS KQSREQSQMK ERLASLSSHV TELEEDLDTA RKDLIKSEEM 

       310        320        330        340        350        360 
NTKLQRDVRE AMAQKEDMEE RITTLEKRYL AAQREATSVH DLNDKLENEI ANKDSMHRQT 

       370        380        390        400        410        420 
EDKNRQLQER LELAEQKLQQ TLRKAETLPE VEAELAQRVA ALSKAEERHG NIEERLRQME 

       430        440        450        460        470        480 
AQLEEKNQEL QRARQREKMN EEHNKRLSDT VDKLLSESNE RLQLHLKERM AALEDKNSLL 

       490        500        510        520        530        540 
REVESAKKQL EETQHDKDQL VLNIEALRAE LDHMRLRGAS LHHGRPHLGS VPDFRFPMAD 

       550        560        570        580        590        600 
GHTDSYSTSA VLRRPQKGRL AALRDEPSKV QTLNEQDWER AQQASVLANV AQAFESDADV 

       610        620        630        640        650        660 
SDGEDDRDTL LSSVDLLSPS GQADAHTLAM MLQEQLDAIN KEIRLIQEEK ENTEQRAEEI 

       670        680        690        700        710        720 
ESRVGSGSLD NLGRFRSMSS IPPYPASSLA SSSPPGSGRS TPRRIPHSPA REVDRLGVMT 

       730        740        750        760        770        780 
LLPPSREEVR DDKTTIKCET SPPSSPRALR LDRLHKGALH TVSHEDIRDI RNSTGSQDGP 

       790        800        810        820        830        840 
VSNPSSSNSS QDSLHKAPKK KGIKSSIGRL FGKKEKGRPG QTGKEALGQA GVSETDNSSQ 

       850        860        870        880        890        900 
DALGLSKLGG QAEKNRKLQK KHELLEEARR QGLPFAQWDG PTVVVWLELW VGMPAWYVAA 

       910        920        930        940        950        960 
CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE IMSLTSPSAP PTSRTTLAYG 

       970        980        990       1000       1010       1020 
DMNHEWIGNE WLPSLGLPQY RSYFMECLVD ARMLDHLTKK DLRGQLKMVD SFHRNSFQCG 

      1030       1040       1050       1060       1070       1080 
IMCLRRLNYD RKELERKREE SQSEIKDVLV WSNDRVIRWI LSIGLKEYAN NLIESGVHGA 

      1090       1100       1110       1120       1130       1140 
LLALDETFDF SALALLLQIP TQNTQARAVL EREFNNLLVM GTDRRFDEDD DKSFRRAPSW 

      1150       1160       1170       1180       1190       1200 
RKKFRPKDIR GLAAGSAETL PANFRVTSSM SSPSMQPKKM QMDGNVSGTQ RLDSATVRTY 


SC 

« Hide

Isoform 2 (LAR-interacting protein 1a) (LIP.1a) (a) [UniParc].

Checksum: 00E9FA5C94C8217C
Show »

FASTA1,185133,970

References

« Hide 'large scale' references
[1]"The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions."
Serra-Pages C., Kedersha N.L., Fazikas L., Medley Q.G., Debant A., Streuli M.
EMBO J. 14:2827-2838(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPRF.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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).
Tissue: Brain.
[4]"Molecular cloning of a cDNA encoding enhancer protein in hsp70 gene."
Taira T., Iguchi-Ariga S.M., Ariga H.
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 672-1123.
[5]"The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1."
Pulido R., Serra-Pages C., Tang M., Streuli M.
Proc. Natl. Acad. Sci. U.S.A. 92:11686-11690(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRD; PTPRF AND PTPRS.
[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: TISSUE SPECIFICITY, INTERACTION WITH PTPRD; PTPRF AND PTPRS.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230; SER-242 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-239; SER-242; SER-693 AND THR-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-244 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22815 mRNA. Translation: AAC50172.1.
U22816 mRNA. Translation: AAC50173.1.
AP002336 Genomic DNA. No translation available.
BC034046 mRNA. Translation: AAH34046.1.
D49354 mRNA. Translation: BAA08353.1. Frameshift.
CCDSCCDS31627.1. [Q13136-1]
CCDS31628.1. [Q13136-2]
PIRS55553.
RefSeqNP_003617.1. NM_003626.3. [Q13136-1]
NP_803172.1. NM_177423.2. [Q13136-2]
UniGeneHs.530749.
Hs.708791.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7FX-ray1.80C/D1195-1202[»]
ProteinModelPortalQ13136.
SMRQ13136. Positions 851-1120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114072. 31 interactions.
IntActQ13136. 16 interactions.
MINTMINT-1460222.
STRING9606.ENSP00000253925.

PTM databases

PhosphoSiteQ13136.

Polymorphism databases

DMDM42558969.

Proteomic databases

MaxQBQ13136.
PaxDbQ13136.
PRIDEQ13136.

Protocols and materials databases

DNASU8500.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253925; ENSP00000253925; ENSG00000131626. [Q13136-1]
ENST00000389547; ENSP00000374198; ENSG00000131626. [Q13136-2]
GeneID8500.
KEGGhsa:8500.
UCSCuc001opn.2. human. [Q13136-2]
uc001opo.3. human. [Q13136-1]

Organism-specific databases

CTD8500.
GeneCardsGC11P070116.
HGNCHGNC:9245. PPFIA1.
HPACAB017032.
HPA008272.
HPA042271.
MIM611054. gene.
neXtProtNX_Q13136.
PharmGKBPA33566.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322697.
HOGENOMHOG000017513.
HOVERGENHBG052330.
InParanoidQ13136.
OMASVPDFRF.
OrthoDBEOG7T7GS7.
PhylomeDBQ13136.
TreeFamTF314207.

Enzyme and pathway databases

SignaLinkQ13136.

Gene expression databases

ArrayExpressQ13136.
BgeeQ13136.
CleanExHS_PPFIA1.
GenevestigatorQ13136.

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. SSF47769. 3 hits.
PROSITEPS50105. SAM_DOMAIN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLiprin-alpha-1.
GenomeRNAi8500.
NextBio31805.
PMAP-CutDBQ13136.
PROQ13136.
SOURCESearch...

Entry information

Entry nameLIPA1_HUMAN
AccessionPrimary (citable) accession number: Q13136
Secondary accession number(s): A6NLE3 expand/collapse secondary AC list , Q13135, Q14567, Q8N4I2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 125 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM