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Protein

Liprin-alpha-1

Gene

PPFIA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • signal transducer activity Source: ProtInc

GO - Biological processi

  • cell-matrix adhesion Source: ProtInc
  • glutamate secretion Source: Reactome
  • negative regulation of establishment of protein localization to plasma membrane Source: MGI
  • negative regulation of stress fiber assembly Source: MGI
  • neurotransmitter secretion Source: Reactome
  • signal transduction Source: ProtInc
  • synaptic transmission Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
SignaLinkiQ13136.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PPFIA1
Synonyms:LIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9245. PPFIA1.

Subcellular locationi

  • Cytoplasm 1 Publication

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

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • focal adhesion Source: HPA
  • presynaptic active zone Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33566.

Polymorphism and mutation databases

BioMutaiPPFIA1.
DMDMi42558969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12021202Liprin-alpha-1PRO_0000191026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301Phosphothreonine1 Publication
Modified residuei239 – 2391Phosphoserine2 Publications
Modified residuei242 – 2421Phosphoserine3 Publications
Modified residuei244 – 2441Phosphoserine2 Publications
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei668 – 6681Phosphoserine1 Publication
Modified residuei693 – 6931Phosphoserine1 Publication
Modified residuei761 – 7611Phosphothreonine1 Publication
Modified residuei1159 – 11591Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13136.
PaxDbiQ13136.
PRIDEiQ13136.

PTM databases

PhosphoSiteiQ13136.

Miscellaneous databases

PMAP-CutDBQ13136.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiQ13136.
CleanExiHS_PPFIA1.
ExpressionAtlasiQ13136. baseline and differential.
GenevisibleiQ13136. HS.

Organism-specific databases

HPAiCAB017032.
HPA008272.
HPA042271.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNHP519463EBI-745426,EBI-741406
DTNBO609413EBI-745426,EBI-740402
FAM161AQ3B8203EBI-745426,EBI-719941
Gria2P194912EBI-745426,EBI-77718From a different organism.
Grip1P978794EBI-745426,EBI-936113From a different organism.
MBIPQ9NS733EBI-745426,EBI-741953
PPP2R5DQ147382EBI-745426,EBI-396563
TXLNAP402223EBI-745426,EBI-359793

Protein-protein interaction databases

BioGridi114072. 46 interactions.
IntActiQ13136. 20 interactions.
MINTiMINT-1460222.
STRINGi9606.ENSP00000253925.

Structurei

Secondary structure

1
1202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1198 – 12014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7FX-ray1.80C/D1195-1202[»]
ProteinModelPortaliQ13136.
SMRiQ13136. Positions 851-1120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini878 – 94467SAM 1PROSITE-ProRule annotationAdd
BLAST
Domaini963 – 102765SAM 2PROSITE-ProRule annotationAdd
BLAST
Domaini1051 – 112070SAM 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili34 – 141108Sequence AnalysisAdd
BLAST
Coiled coili176 – 21439Sequence AnalysisAdd
BLAST
Coiled coili249 – 521273Sequence AnalysisAdd
BLAST
Coiled coili623 – 66947Sequence AnalysisAdd
BLAST
Coiled coili847 – 87125Sequence AnalysisAdd
BLAST
Coiled coili1021 – 105030Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 259Poly-Gly

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.
GeneTreeiENSGT00760000119138.
HOGENOMiHOG000017513.
HOVERGENiHBG052330.
InParanoidiQ13136.
OMAiFRFPMAD.
OrthoDBiEOG7T7GS7.
PhylomeDBiQ13136.
TreeFamiTF314207.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR029515. Liprin.
IPR030438. PPFIA1.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR021129. SAM_type1.
[Graphical view]
PANTHERiPTHR12587. PTHR12587. 1 hit.
PTHR12587:SF15. PTHR12587:SF15. 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. AlignAdd to basket

Isoform 1 (identifier: Q13136-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MMCEVMPTIS EAEGPPGGGG GHGSGSPSQP DADSHFEQLM VSMLEERDRL
60 70 80 90 100
LDTLRETQET LALTQGKLHE VGHERDSLQR QLNTALPQEF AALTKELNVC
110 120 130 140 150
REQLLEREEE IAELKAERNN TRLLLEHLEC LVSRHERSLR MTVVKRQAQS
160 170 180 190 200
PAGVSSEVEV LKALKSLFEH HKALDEKVRE RLRVALERCS LLEEELGATH
210 220 230 240 250
KELMILKEQN NQKKTLTDGV LDINHEQENT PSTSGKRSSD GSLSHEEDLA
260 270 280 290 300
KVIELQEIIS KQSREQSQMK ERLASLSSHV TELEEDLDTA RKDLIKSEEM
310 320 330 340 350
NTKLQRDVRE AMAQKEDMEE RITTLEKRYL AAQREATSVH DLNDKLENEI
360 370 380 390 400
ANKDSMHRQT EDKNRQLQER LELAEQKLQQ TLRKAETLPE VEAELAQRVA
410 420 430 440 450
ALSKAEERHG NIEERLRQME AQLEEKNQEL QRARQREKMN EEHNKRLSDT
460 470 480 490 500
VDKLLSESNE RLQLHLKERM AALEDKNSLL REVESAKKQL EETQHDKDQL
510 520 530 540 550
VLNIEALRAE LDHMRLRGAS LHHGRPHLGS VPDFRFPMAD GHTDSYSTSA
560 570 580 590 600
VLRRPQKGRL AALRDEPSKV QTLNEQDWER AQQASVLANV AQAFESDADV
610 620 630 640 650
SDGEDDRDTL LSSVDLLSPS GQADAHTLAM MLQEQLDAIN KEIRLIQEEK
660 670 680 690 700
ENTEQRAEEI ESRVGSGSLD NLGRFRSMSS IPPYPASSLA SSSPPGSGRS
710 720 730 740 750
TPRRIPHSPA REVDRLGVMT LLPPSREEVR DDKTTIKCET SPPSSPRALR
760 770 780 790 800
LDRLHKGALH TVSHEDIRDI RNSTGSQDGP VSNPSSSNSS QDSLHKAPKK
810 820 830 840 850
KGIKSSIGRL FGKKEKGRPG QTGKEALGQA GVSETDNSSQ DALGLSKLGG
860 870 880 890 900
QAEKNRKLQK KHELLEEARR QGLPFAQWDG PTVVVWLELW VGMPAWYVAA
910 920 930 940 950
CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE IMSLTSPSAP
960 970 980 990 1000
PTSRTTLAYG DMNHEWIGNE WLPSLGLPQY RSYFMECLVD ARMLDHLTKK
1010 1020 1030 1040 1050
DLRGQLKMVD SFHRNSFQCG IMCLRRLNYD RKELERKREE SQSEIKDVLV
1060 1070 1080 1090 1100
WSNDRVIRWI LSIGLKEYAN NLIESGVHGA LLALDETFDF SALALLLQIP
1110 1120 1130 1140 1150
TQNTQARAVL EREFNNLLVM GTDRRFDEDD DKSFRRAPSW RKKFRPKDIR
1160 1170 1180 1190 1200
GLAAGSAETL PANFRVTSSM SSPSMQPKKM QMDGNVSGTQ RLDSATVRTY

SC
Length:1,202
Mass (Da):135,779
Last modified:November 1, 1996 - v1
Checksum:iC8CF7C20B298BFB1
GO
Isoform 2 (identifier: Q13136-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:1,185
Mass (Da):133,970
Checksum:i00E9FA5C94C8217C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti492 – 4921E → G in AAH34046 (PubMed:15489334).Curated
Sequence conflicti555 – 5551P → T in AAH34046 (PubMed:15489334).Curated
Sequence conflicti672 – 6743LGR → EFG in BAA08353 (Ref. 4) Curated
Sequence conflicti800 – 8012KK → EE in BAA08353 (Ref. 4) Curated
Sequence conflicti866 – 8661E → G in AAH34046 (PubMed:15489334).Curated
Sequence conflicti994 – 9941L → Q in BAA08353 (Ref. 4) Curated
Sequence conflicti1023 – 10231C → S in BAA08353 (Ref. 4) Curated
Sequence conflicti1044 – 10441E → EVRV in BAA08353 (Ref. 4) Curated
Sequence conflicti1121 – 11233GTD → PEF in BAA08353 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711V → I.
Corresponds to variant rs546502 [ dbSNP | Ensembl ].
VAR_017756
Natural varianti1072 – 10721L → F.
Corresponds to variant rs11236045 [ dbSNP | Ensembl ].
VAR_049998

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1185 – 120218NVSGT…RTYSC → M in isoform 2. 1 PublicationVSP_009391Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31627.1. [Q13136-1]
CCDS31628.1. [Q13136-2]
PIRiS55553.
RefSeqiNP_003617.1. NM_003626.3. [Q13136-1]
NP_803172.1. NM_177423.2. [Q13136-2]
UniGeneiHs.530749.
Hs.708791.

Genome annotation databases

EnsembliENST00000253925; ENSP00000253925; ENSG00000131626.
ENST00000389547; ENSP00000374198; ENSG00000131626. [Q13136-2]
GeneIDi8500.
KEGGihsa:8500.
UCSCiuc001opn.2. human. [Q13136-2]
uc001opo.3. human. [Q13136-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31627.1. [Q13136-1]
CCDS31628.1. [Q13136-2]
PIRiS55553.
RefSeqiNP_003617.1. NM_003626.3. [Q13136-1]
NP_803172.1. NM_177423.2. [Q13136-2]
UniGeneiHs.530749.
Hs.708791.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7FX-ray1.80C/D1195-1202[»]
ProteinModelPortaliQ13136.
SMRiQ13136. Positions 851-1120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114072. 46 interactions.
IntActiQ13136. 20 interactions.
MINTiMINT-1460222.
STRINGi9606.ENSP00000253925.

PTM databases

PhosphoSiteiQ13136.

Polymorphism and mutation databases

BioMutaiPPFIA1.
DMDMi42558969.

Proteomic databases

MaxQBiQ13136.
PaxDbiQ13136.
PRIDEiQ13136.

Protocols and materials databases

DNASUi8500.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253925; ENSP00000253925; ENSG00000131626.
ENST00000389547; ENSP00000374198; ENSG00000131626. [Q13136-2]
GeneIDi8500.
KEGGihsa:8500.
UCSCiuc001opn.2. human. [Q13136-2]
uc001opo.3. human. [Q13136-1]

Organism-specific databases

CTDi8500.
GeneCardsiGC11P070116.
HGNCiHGNC:9245. PPFIA1.
HPAiCAB017032.
HPA008272.
HPA042271.
MIMi611054. gene.
neXtProtiNX_Q13136.
PharmGKBiPA33566.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322697.
GeneTreeiENSGT00760000119138.
HOGENOMiHOG000017513.
HOVERGENiHBG052330.
InParanoidiQ13136.
OMAiFRFPMAD.
OrthoDBiEOG7T7GS7.
PhylomeDBiQ13136.
TreeFamiTF314207.

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
SignaLinkiQ13136.

Miscellaneous databases

ChiTaRSiPPFIA1. human.
GeneWikiiLiprin-alpha-1.
GenomeRNAii8500.
NextBioi31805.
PMAP-CutDBQ13136.
PROiQ13136.
SOURCEiSearch...

Gene expression databases

BgeeiQ13136.
CleanExiHS_PPFIA1.
ExpressionAtlasiQ13136. baseline and differential.
GenevisibleiQ13136. HS.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR029515. Liprin.
IPR030438. PPFIA1.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR021129. SAM_type1.
[Graphical view]
PANTHERiPTHR12587. PTHR12587. 1 hit.
PTHR12587:SF15. PTHR12587:SF15. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND THR-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLIPA1_HUMAN
AccessioniPrimary (citable) accession number: Q13136
Secondary accession number(s): A6NLE3
, Q13135, Q14567, Q8N4I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 137 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.