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Q86W92 (LIPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-beta-1
Alternative name(s):
Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1
Short name=PTPRF-interacting protein-binding protein 1
hSGT2
Gene names
Name:PPFIBP1
Synonyms:KIAA1230
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1011 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. Ref.1

Subunit structure

Forms homodimers and heterodimers. Interacts with S100A4 in a calcium-dependent mode. Ref.7

Tissue specificity

Widely expressed. Absent in liver. Ref.1

Domain

The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type beta/beta. The C-terminal, non-coiled coil regions mediate heterodimerization type beta/alpha and interaction with S100A4.

Sequence similarities

Belongs to the liprin family. Liprin-beta subfamily.

Contains 3 SAM (sterile alpha motif) domains.

Sequence caution

The sequence AAH46159.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA86544.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentplasma membrane

Non-traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86W92-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q86W92-2)

The sequence of this isoform differs from the canonical sequence as follows:
     233-263: Missing.
     302-302: D → DENFKKKLKEKN
     349-349: K → KKGK
     544-544: L → LDRKRSASAPTL
Note: No experimental confirmation available. Contains a phosphoserine at position 523.
Isoform 3 (identifier: Q86W92-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86W92-4)

The sequence of this isoform differs from the canonical sequence as follows:
     233-263: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q86W92-5)

Also known as: L2;

The sequence of this isoform differs from the canonical sequence as follows:
     158-170: ELLSRTSLETQKL → VCAEARTKMGFPC
     171-1011: Missing.
Note: Due to intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10111011Liprin-beta-1
PRO_0000191034

Regions

Domain647 – 71165SAM 1
Domain719 – 78264SAM 2
Domain804 – 87673SAM 3
Coiled coil156 – 405250 Potential

Amino acid modifications

Modified residue371Phosphoserine Ref.9 Ref.13
Modified residue391Phosphothreonine Ref.9
Modified residue401Phosphoserine Ref.9 Ref.13
Modified residue3091N6-acetyllysine Ref.12
Modified residue3221N6-acetyllysine Ref.12
Modified residue4661Phosphoserine Ref.9
Modified residue5791Phosphoserine Ref.9
Modified residue6011Phosphoserine Ref.9 Ref.11
Modified residue6361Phosphoserine By similarity
Modified residue9991Phosphoserine Ref.9 Ref.13 Ref.15
Modified residue10011Phosphoserine Ref.9 Ref.13
Modified residue10031Phosphoserine Ref.9
Modified residue10051Phosphothreonine Ref.9

Natural variations

Alternative sequence1 – 153153Missing in isoform 3.
VSP_009394
Alternative sequence158 – 17013ELLSR…ETQKL → VCAEARTKMGFPC in isoform 5.
VSP_009395
Alternative sequence171 – 1011841Missing in isoform 5.
VSP_009396
Alternative sequence233 – 26331Missing in isoform 2 and isoform 4.
VSP_009397
Alternative sequence3021D → DENFKKKLKEKN in isoform 2.
VSP_009398
Alternative sequence3491K → KKGK in isoform 2.
VSP_009399
Alternative sequence5441L → LDRKRSASAPTL in isoform 2.
VSP_009400
Natural variant1481V → L. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2194816 [ dbSNP | Ensembl ].
VAR_017758

Experimental info

Sequence conflict3081M → K in AAH46159. Ref.6
Sequence conflict4531C → R in AAC26103. Ref.1
Sequence conflict5531E → A in AAC26103. Ref.1

Sequences

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

Last modified March 7, 2006. Version 2.
Checksum: 20E30DD99ACD5A92

FASTA1,011114,024
        10         20         30         40         50         60 
MMSDASDMLA AALEQMDGII AGSKALEYSN GIFDCQSPTS PFMGSLRALH LVEDLRGLLE 

        70         80         90        100        110        120 
MMETDEKEGL RCQIPDSTAE TLVEWLQSQM TNGHLPGNGD VYQERLARLE NDKESLVLQV 

       130        140        150        160        170        180 
SVLTDQVEAQ GEKIRDLEFC LEEHREKVNA TEEMLQQELL SRTSLETQKL DLMAEISNLK 

       190        200        210        220        230        240 
LKLTAVEKDR LDYEDKFRDT EGLIQEINDL RLKVSEMDSE RLQYEKKLKS TKSLMAKLSS 

       250        260        270        280        290        300 
MKIKVGQMQY EKQRMEQKWE SLKDELASLK EQLEEKESEV KRLQEKLVCK MKGEGVEIVD 

       310        320        330        340        350        360 
RDIEVQKMKK AVESLMAANE EKDRKIEDLR QCLNRYKKMQ DTVVLAQGKD GEYEELLNSS 

       370        380        390        400        410        420 
SISSLLDAQG FSDLEKSPSP TPVMGSPSCD PFNTSVPEEF HTTILQVSIP SLLPATVSME 

       430        440        450        460        470        480 
TSEKSKLTPK PETSFEENDG NIILGATVDT QLCDKLLTSS LQKSSSLGNL KKETSDGEKE 

       490        500        510        520        530        540 
TIQKTSEDRA PAESRPFGTL PPRPPGQDTS MDDNPFGTRK VRSSFGRGFF KIKSNKRTAS 

       550        560        570        580        590        600 
APNLAETEKE TAEHLDLAGA SSRPKDSQRN SPFQIPPPSP DSKKKSRGIM KLFGKLRRSQ 

       610        620        630        640        650        660 
STTFNPDDMS EPEFKRGGTR ATAGPRLGWS RDLGQSNSDL DMPFAKWTKE QVCNWLMEQG 

       670        680        690        700        710        720 
LGSYLNSGKH WIASGQTLLQ ASQQDLEKEL GIKHSLHRKK LQLALQALGS EEETNHGKLD 

       730        740        750        760        770        780 
FNWVTRWLDD IGLPQYKTQF DEGRVDGRML HYMTVDDLLS LKVVSVLHHL SIKRAIQVLR 

       790        800        810        820        830        840 
INNFEPNCLR RRPSDENTIA PSEVQKWTNH RVMEWLRSVD LAEYAPNLRG SGVHGGLMVL 

       850        860        870        880        890        900 
EPRFNVETMA QLLNIPPNKT LLRRHLATHF NLLIGAEAQH QKRDAMELPD YVLLTATAKV 

       910        920        930        940        950        960 
KPKKLAFSNF GNLRKKKQED GEEYVCPMEL GQASGSASKK GFKPGLDMRL YEEDDLDRLE 

       970        980        990       1000       1010 
QMEDSEGTVR QIGAFSEGIN NLTHMLKEDD MFKDFAARSP SASITDEDSN V 

« Hide

Isoform 2 [UniParc].

Checksum: E399A3BB86F46BAE
Show »

FASTA1,005113,181
Isoform 3 [UniParc].

Checksum: D5BE6B7D1D47C76A
Show »

FASTA85896,965
Isoform 4 [UniParc].

Checksum: A521EFCC0589E24B
Show »

FASTA980110,297
Isoform 5 (L2) [UniParc].

Checksum: C281D0F4E7896A7B
Show »

FASTA17018,972

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 2), VARIANT LEU-148, TISSUE SPECIFICITY, FUNCTION.
[2]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-148.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"L2, a different isoform of Liprin beta 1, is expressed in high level in liver tissue."
Junjian L., Cheng J., Rouli Z., Jie Z.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT LEU-148.
[5]"hSGT2, a liprin related human gene, restores the glycolytic gene expression of the gcr2 mutant of Saccharomyces cerevisiae."
Sato T., Jigami Y., Uemura H.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT LEU-148.
Tissue: Brain.
[6]"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 1 AND 4), VARIANT LEU-148.
Tissue: Brain and Skin.
[7]"Liprin beta 1, a member of the family of LAR transmembrane tyrosine phosphatase-interacting proteins, is a new target for the metastasis-associated protein S100A4 (Mts1)."
Kriajevska M., Fischer-Larsen M., Moertz E., Vorm O., Tulchinsky E., Grigorian M., Ambartsumian N., Lukanidin E.
J. Biol. Chem. 277:5229-5235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A4.
[8]"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.
[9]"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 SER-37; THR-39; SER-40; SER-466; SER-579; SER-601; SER-999; SER-1001; SER-1003 AND THR-1005, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-309 AND LYS-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; SER-999 AND SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-999, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF034802 mRNA. Translation: AAC26103.1.
AB033056 mRNA. Translation: BAA86544.2. Different initiation.
AJ276680 mRNA. Translation: CAB77544.1.
AB049149 mRNA. Translation: BAB39690.1.
BC046159 mRNA. Translation: AAH46159.1. Different initiation.
BC050281 mRNA. Translation: AAH50281.1.
RefSeqNP_001185844.1. NM_001198915.1.
NP_001185845.1. NM_001198916.1.
NP_003613.3. NM_003622.3.
NP_803193.2. NM_177444.2.
UniGeneHs.172445.

3D structure databases

ProteinModelPortalQ86W92.
SMRQ86W92. Positions 642-894.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114068. 13 interactions.
DIPDIP-42195N.
IntActQ86W92. 4 interactions.
MINTMINT-1683640.
STRING9606.ENSP00000228425.

PTM databases

PhosphoSiteQ86W92.

Polymorphism databases

DMDM90185247.

Proteomic databases

PaxDbQ86W92.
PRIDEQ86W92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228425; ENSP00000228425; ENSG00000110841. [Q86W92-2]
ENST00000318304; ENSP00000314724; ENSG00000110841. [Q86W92-1]
ENST00000535047; ENSP00000444046; ENSG00000110841. [Q86W92-5]
ENST00000537927; ENSP00000445425; ENSG00000110841. [Q86W92-3]
ENST00000542629; ENSP00000443442; ENSG00000110841. [Q86W92-4]
GeneID8496.
KEGGhsa:8496.
UCSCuc001rhz.2. human. [Q86W92-5]
uc001ria.3. human. [Q86W92-4]
uc001rib.2. human. [Q86W92-2]
uc001ric.2. human. [Q86W92-1]
uc001rif.2. human. [Q86W92-3]

Organism-specific databases

CTD8496.
GeneCardsGC12P027677.
HGNCHGNC:9249. PPFIBP1.
HPAHPA001924.
MIM603141. gene.
neXtProtNX_Q86W92.
PharmGKBPA33570.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308732.
HOGENOMHOG000082535.
HOVERGENHBG052331.
InParanoidQ86W92.
OMAVPEEFHT.
PhylomeDBQ86W92.
TreeFamTF314207.

Gene expression databases

ArrayExpressQ86W92.
BgeeQ86W92.
CleanExHS_PPFIBP1.
GenevestigatorQ86W92.

Family and domain databases

Gene3D1.10.150.50. 3 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. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPFIBP1. human.
GeneWikiPPFIBP1.
GenomeRNAi8496.
NextBio31783.
PROQ86W92.
SOURCESearch...

Entry information

Entry nameLIPB1_HUMAN
AccessionPrimary (citable) accession number: Q86W92
Secondary accession number(s): O75336 expand/collapse secondary AC list , Q86X70, Q9NY03, Q9ULJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 7, 2006
Last modified: March 19, 2014
This is version 108 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

SIMILARITY comments

Index of protein domains and families

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 12

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