Q13136 (LIPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1202 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell-matrix adhesion Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MBIP	Q9NS73	3	EBI-745426,EBI-741953
PPP2R5D	Q14738	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1202	1202	Liprin-alpha-1		PRO_0000191026
Regions
	Domain	878 – 944	67	SAM 1
	Domain	963 – 1027	65	SAM 2
	Domain	1051 – 1120	70	SAM 3
	Coiled coil	34 – 141	108	Potential
	Coiled coil	176 – 214	39	Potential
	Coiled coil	249 – 521	273	Potential
	Coiled coil	623 – 669	47	Potential
	Coiled coil	847 – 871	25	Potential
	Coiled coil	1021 – 1050	30	Potential
	Compositional bias	17 – 25	9	Poly-Gly
Amino acid modifications
	Modified residue	230	1	Phosphothreonine Ref.11
	Modified residue	239	1	Phosphoserine Ref.7 Ref.11 Ref.13
	Modified residue	242	1	Phosphoserine Ref.7 Ref.11 Ref.13
	Modified residue	244	1	Phosphoserine Ref.11 Ref.13
	Modified residue	668	1	Phosphoserine Ref.12
	Modified residue	684	1	Phosphotyrosine Ref.8
	Modified residue	693	1	Phosphoserine Ref.12 Ref.13
	Modified residue	741	1	Phosphoserine Ref.11
	Modified residue	745	1	Phosphoserine Ref.11
	Modified residue	763	1	Phosphoserine Ref.10
	Modified residue	776	1	Phosphoserine Ref.9
	Modified residue	1159	1	Phosphothreonine Ref.13
	Modified residue	1172	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	1185 – 1202	18	NVSGT…RTYSC → M in isoform 2.		VSP_009391
	Natural variant	71	1	V → I. Corresponds to variant rs546502 [ dbSNP | Ensembl ].		VAR_017756
	Natural variant	1072	1	L → F. Corresponds to variant rs11236045 [ dbSNP | Ensembl ].		VAR_049998
Experimental info
	Sequence conflict	492	1	E → G in AAH34046. Ref.3
	Sequence conflict	555	1	P → T in AAH34046. Ref.3
	Sequence conflict	672 – 674	3	LGR → EFG in BAA08353. Ref.4
	Sequence conflict	800 – 801	2	KK → EE in BAA08353. Ref.4
	Sequence conflict	866	1	E → G in AAH34046. Ref.3
	Sequence conflict	994	1	L → Q in BAA08353. Ref.4
	Sequence conflict	1023	1	C → S in BAA08353. Ref.4
	Sequence conflict	1044	1	E → EVRV in BAA08353. Ref.4
	Sequence conflict	1121 – 1123	3	GTD → PEF in BAA08353. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LAR-interacting protein 1b) (LIP.1b) (b) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C8CF7C20B298BFB1	FASTA	1,202	135,779
	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
	Isoform 2 (LAR-interacting protein 1a) (LIP.1a) (a) [UniParc]. Checksum: 00E9FA5C94C8217C	FASTA	1,185	133,970
	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 RKKFRPKDIR GLAAGSAETL PANFRVTSSM SSPSMQPKKM QMDGM

References

	« Hide 'large scale' referencesShow '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: 7796809] [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. , 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: 16554811] [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: 15489334] [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: 8524829] [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: 9624153] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-242, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-684, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230; SER-239; SER-242; SER-244; SER-741 AND SER-745, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668; SER-693 AND SER-1172, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-244; SER-693 AND THR-1159, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00163496. IPI00219754.
PIR	S55553.
RefSeq	NP_003617.1. NM_003626.3. NP_803172.1. NM_177423.2.
UniGene	Hs.530749.
3D structure databases
ProteinModelPortal	Q13136.
SMR	Q13136. Positions 872-1108.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13136. 10 interactions.
MINT	MINT-1460222.
STRING	Q13136.
PTM databases
PhosphoSite	Q13136.
Polymorphism databases
DMDM	42558969.
Proteomic databases
PRIDE	Q13136.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253925; ENSP00000253925; ENSG00000131626.
GeneID	8500.
KEGG	hsa:8500.
UCSC	uc001opn.1. human. uc001opo.1. human.
Organism-specific databases
CTD	8500.
GeneCards	GC11P070116.
H-InvDB	HIX0201681.
HGNC	HGNC:9245. PPFIA1.
HPA	CAB017032.
MIM	611054. gene.
neXtProt	NX_Q13136.
PharmGKB	PA33566.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11873.
HOGENOM	HBG356868.
HOVERGEN	HBG052330.
InParanoid	Q13136.
OMA	DEPSKVQ.
OrthoDB	EOG40GCQ1.
PhylomeDB	Q13136.
Gene expression databases
ArrayExpress	Q13136.
Bgee	Q13136.
CleanEx	HS_PPFIA1.
Genevestigator	Q13136.
GermOnline	ENSG00000131626. Homo sapiens.
Family and domain databases
InterPro	IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR021129. SAM_type1. [Graphical view]
Gene3D	G3DSA:1.10.150.50. SAM_type. 3 hits.
Pfam	PF00536. SAM_1. 2 hits. PF07647. SAM_2. 1 hit. [Graphical view]
SMART	SM00454. SAM. 3 hits. [Graphical view]
SUPFAM	SSF47769. SAM_homology. 3 hits.
PROSITE	PS50105. SAM_DOMAIN. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	31805.
PMAP-CutDB	Q13136.
SOURCE	Search...

Entry information

Entry name

LIPA1_HUMAN

Accession

Primary (citable) accession number: Q13136
Secondary accession number(s): A6NLE3 , Q13135, Q14567, Q8N4I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.