LIPB2_HUMAN
ID LIPB2_HUMAN Reviewed; 876 AA.
AC Q8ND30; B7Z433; E9PK77; O75337; Q8WW26;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Liprin-beta-2;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 2;
DE Short=PTPRF-interacting protein-binding protein 2;
GN Name=PPFIBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-658.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-658.
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-658.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-876, TISSUE SPECIFICITY, FUNCTION, AND
RP VARIANT GLY-658.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-363; SER-387 AND
RP SER-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10] {ECO:0007744|PDB:3QH9}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 198-263, AND SUBUNIT.
RX PubMed=21462929; DOI=10.1021/bi200141e;
RA Stafford R.L., Tang M.Y., Sawaya M.R., Phillips M.L., Bowie J.U.;
RT "Crystal structure of the central coiled-coil domain from human liprin-
RT beta2.";
RL Biochemistry 50:3807-3815(2011).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. Did not bind
CC receptor-like tyrosine phosphatases type 2A.
CC {ECO:0000269|PubMed:9624153}.
CC -!- SUBUNIT: Forms homodimers and heterodimers (PubMed:21462929).
CC {ECO:0000269|PubMed:21462929}.
CC -!- INTERACTION:
CC Q8ND30; P46108: CRK; NbExp=5; IntAct=EBI-744056, EBI-886;
CC Q8ND30; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-744056, EBI-12056251;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8ND30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8ND30-2; Sequence=VSP_047383, VSP_047384;
CC Name=3;
CC IsoId=Q8ND30-3; Sequence=VSP_047382, VSP_047385;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9624153}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type beta/beta. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type beta/alpha (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC {ECO:0000305}.
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DR EMBL; AK296718; BAH12419.1; -; mRNA.
DR EMBL; AL834426; CAD39087.2; -; mRNA.
DR EMBL; AC104237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021714; AAH21714.1; -; mRNA.
DR EMBL; AF034803; AAC26104.1; -; mRNA.
DR CCDS; CCDS31419.1; -. [Q8ND30-1]
DR CCDS; CCDS58116.1; -. [Q8ND30-2]
DR CCDS; CCDS58117.1; -. [Q8ND30-3]
DR RefSeq; NP_001243497.1; NM_001256568.1. [Q8ND30-2]
DR RefSeq; NP_003612.2; NM_003621.3. [Q8ND30-1]
DR RefSeq; XP_016873932.1; XM_017018443.1.
DR PDB; 3QH9; X-ray; 2.01 A; A=198-263.
DR PDBsum; 3QH9; -.
DR AlphaFoldDB; Q8ND30; -.
DR SMR; Q8ND30; -.
DR BioGRID; 114067; 40.
DR DIP; DIP-42373N; -.
DR IntAct; Q8ND30; 16.
DR MINT; Q8ND30; -.
DR STRING; 9606.ENSP00000299492; -.
DR GlyGen; Q8ND30; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8ND30; -.
DR PhosphoSitePlus; Q8ND30; -.
DR BioMuta; PPFIBP2; -.
DR DMDM; 296439314; -.
DR EPD; Q8ND30; -.
DR jPOST; Q8ND30; -.
DR MassIVE; Q8ND30; -.
DR MaxQB; Q8ND30; -.
DR PaxDb; Q8ND30; -.
DR PeptideAtlas; Q8ND30; -.
DR PRIDE; Q8ND30; -.
DR ProteomicsDB; 21373; -.
DR ProteomicsDB; 72978; -. [Q8ND30-1]
DR Antibodypedia; 1168; 141 antibodies from 24 providers.
DR DNASU; 8495; -.
DR Ensembl; ENST00000299492.9; ENSP00000299492.4; ENSG00000166387.14. [Q8ND30-1]
DR Ensembl; ENST00000528883.5; ENSP00000435469.1; ENSG00000166387.14. [Q8ND30-2]
DR Ensembl; ENST00000530181.5; ENSP00000437321.1; ENSG00000166387.14. [Q8ND30-3]
DR GeneID; 8495; -.
DR KEGG; hsa:8495; -.
DR MANE-Select; ENST00000299492.9; ENSP00000299492.4; NM_003621.5; NP_003612.3.
DR UCSC; uc001mfj.6; human. [Q8ND30-1]
DR CTD; 8495; -.
DR DisGeNET; 8495; -.
DR GeneCards; PPFIBP2; -.
DR HGNC; HGNC:9250; PPFIBP2.
DR HPA; ENSG00000166387; Low tissue specificity.
DR MIM; 603142; gene.
DR neXtProt; NX_Q8ND30; -.
DR OpenTargets; ENSG00000166387; -.
DR PharmGKB; PA33571; -.
DR VEuPathDB; HostDB:ENSG00000166387; -.
DR eggNOG; KOG1899; Eukaryota.
DR GeneTree; ENSGT01050000244951; -.
DR HOGENOM; CLU_011689_2_1_1; -.
DR InParanoid; Q8ND30; -.
DR OMA; FMSQFTP; -.
DR OrthoDB; 558442at2759; -.
DR PhylomeDB; Q8ND30; -.
DR TreeFam; TF314207; -.
DR PathwayCommons; Q8ND30; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q8ND30; -.
DR BioGRID-ORCS; 8495; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; PPFIBP2; human.
DR GenomeRNAi; 8495; -.
DR Pharos; Q8ND30; Tbio.
DR PRO; PR:Q8ND30; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8ND30; protein.
DR Bgee; ENSG00000166387; Expressed in parotid gland and 176 other tissues.
DR ExpressionAtlas; Q8ND30; baseline and differential.
DR Genevisible; Q8ND30; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR InterPro; IPR030435; PPFIBP2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF18; PTHR12587:SF18; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..876
FT /note="Liprin-beta-2"
FT /id="PRO_0000191036"
FT DOMAIN 558..622
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 630..693
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 718..783
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..313
FT /evidence="ECO:0000269|PubMed:21462929"
FT COMPBIAS 470..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047382"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047383"
FT VAR_SEQ 113..124
FT /note="RLEGDKESLILQ -> MSSEQWPRLPGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047384"
FT VAR_SEQ 144..162
FT /note="VCLEGHQVKLNAAEEMLQQ -> MGKLITRMWKLLRRRSAPK (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047385"
FT VARIANT 658
FT /note="R -> G (in dbSNP:rs4758209)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9624153"
FT /id="VAR_049999"
FT CONFLICT 128
FT /note="L -> I (in Ref. 2; AAH21714)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Q -> H (in Ref. 1; BAH12419)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="R -> L (in Ref. 4; AAC26104)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="E -> V (in Ref. 4; AAC26104)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="R -> L (in Ref. 4; AAC26104)"
FT /evidence="ECO:0000305"
FT HELIX 199..261
FT /evidence="ECO:0007829|PDB:3QH9"
SQ SEQUENCE 876 AA; 98544 MW; B01BF9286C6C1417 CRC64;
MASDASHALE AALEQMDGII AGTKTGADLS DGTCEPGLAS PASYMNPFPV LHLIEDLRLA
LEMLELPQER AALLSQIPGP TAAYIKEWFE ESLSQVNHHS AASNETYQER LARLEGDKES
LILQVSVLTD QVEAQGEKIR DLEVCLEGHQ VKLNAAEEML QQELLSRTSL ETQKLDLMTE
VSELKLKLVG MEKEQREQEE KQRKAEELLQ ELRHLKIKVE ELENERNQYE WKLKATKAEV
AQLQEQVALK DAEIERLHSQ LSRTAALHSE SHTERDQEIQ RLKMGMETLL LANEDKDRRI
EELTGLLNQY RKVKEIVMVT QGPSERTLSI NEEEPEGGFS KWNATNKDPE ELFKQEMPPR
CSSPTVGPPP LPQKSLETRA QKKLSCSLED LRSESVDKCM DGNQPFPVLE PKDSPFLAEH
KYPTLPGKLS GATPNGEAAK SPPTICQPDA TGSSLLRLRD TESGWDDTAV VNDLSSTSSG
TESGPQSPLT PDGKRNPKGI KKFWGKIRRT QSGNFYTDTL GMAEFRRGGL RATAGPRLSR
TRDSKGQKSD ANAPFAQWST ERVCAWLEDF GLAQYVIFAR QWVSSGHTLL TATPQDMEKE
LGIKHPLHRK KLVLAVKAIN TKQEEKSALL DHIWVTRWLD DIGLPQYKDQ FHESRVDRRM
LQYLTVNDLL FLKVTSQLHH LSIKCAIHVL HVNKFNPHCL HRRPADESNL SPSEVVQWSN
HRVMEWLRSV DLAEYAPNLR GSGVHGGLII LEPRFTGDTL AMLLNIPPQK TLLRRHLTTK
FNALIGPEAE QEKREKMASP AYTPLTTTAK VRPRKLGFSH FGNIRKKKFD ESTDYICPME
PSDGVSDSHR VYSGYRGLSP LDAPELDGLD QVGQIS
