LOCUS       NP_057396                641 aa            linear   PRI 28-APR-2025
DEFINITION  WW domain-binding protein 11 [Homo sapiens].
ACCESSION   NP_057396
VERSION     NP_057396.1
DBSOURCE    REFSEQ: accession NM_016312.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Martin,E.M.M.A., Enriquez,A., Sparrow,D.B., Humphreys,D.T.,
            McInerney-Leo,A.M., Leo,P.J., Duncan,E.L., Iyer,K.R., Greasby,J.A.,
            Ip,E., Giannoulatou,E., Sheng,D., Wohler,E., Dimartino,C.,
            Amiel,J., Capri,Y., Lehalle,D., Mory,A., Wilnai,Y., Lebenthal,Y.,
            Gharavi,A.G., Krzemien,G.G., Miklaszewska,M., Steiner,R.D.,
            Raggio,C., Blank,R., Baris Feldman,H., Milo Rasouly,H.,
            Sobreira,N.L.M., Jobling,R., Gordon,C.T., Giampietro,P.F.,
            Dunwoodie,S.L. and Chapman,G.
  TITLE     Heterozygous loss of WBP11 function causes multiple congenital
            defects in humans and mice
  JOURNAL   Hum Mol Genet 29 (22), 3662-3678 (2020)
   PUBMED   33276377
  REMARK    GeneRIF: Heterozygous loss of WBP11 function causes multiple
            congenital defects in humans and mice.
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Henning,L.M., Santos,K.F., Sticht,J., Jehle,S., Lee,C.T.,
            Wittwer,M., Urlaub,H., Stelzl,U., Wahl,M.C. and Freund,C.
  TITLE     A new role for FBP21 as regulator of Brr2 helicase activity
  JOURNAL   Nucleic Acids Res 45 (13), 7922-7937 (2017)
   PUBMED   28838205
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   7  (residues 1 to 641)
  AUTHORS   Llorian,M., Beullens,M., Andres,I., Ortiz,J.M. and Bollen,M.
  TITLE     SIPP1, a novel pre-mRNA splicing factor and interactor of protein
            phosphatase-1
  JOURNAL   Biochem J 378 (Pt 1), 229-238 (2004)
   PUBMED   14640981
REFERENCE   8  (residues 1 to 641)
  AUTHORS   Craggs,G., Finan,P.M., Lawson,D., Wingfield,J., Perera,T.,
            Gadher,S., Totty,N.F. and Kellie,S.
  TITLE     A nuclear SH3 domain-binding protein that colocalizes with mRNA
            splicing factors and intermediate filament-containing perinuclear
            networks
  JOURNAL   J Biol Chem 276 (32), 30552-30560 (2001)
   PUBMED   11375989
REFERENCE   9  (residues 1 to 641)
  AUTHORS   Bedford,M.T., Sarbassova,D., Xu,J., Leder,P. and Yaffe,M.B.
  TITLE     A novel pro-Arg motif recognized by WW domains
  JOURNAL   J Biol Chem 275 (14), 10359-10369 (2000)
   PUBMED   10744724
REFERENCE   10 (residues 1 to 641)
  AUTHORS   Komuro,A., Saeki,M. and Kato,S.
  TITLE     Association of two nuclear proteins, Npw38 and NpwBP, via the
            interaction between the WW domain and a novel proline-rich motif
            containing glycine and arginine
  JOURNAL   J Biol Chem 274 (51), 36513-36519 (1999)
   PUBMED   10593949
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007655.1 and AC010168.6.
            
            Summary: This gene encodes a nuclear protein, which colocalizes
            with mRNA splicing factors and intermediate filament-containing
            perinuclear networks. This protein has 95% amino acid sequence
            identity to the mouse Wbp11 protein. It contains two proline-rich
            regions that bind to the WW domain of Npw38, a nuclear protein, and
            thus this protein is also called Npw38-binding protein NpwBP. The
            Npw38-NpwBP complex may function as a component of an mRNA factory
            in the nucleus. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.155094.1,
                                           SRR1803616.79110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261167.7/ ENSP00000261167.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..641
                     /product="WW domain-binding protein 11"
                     /note="Npw38-binding protein NpwBP; splicing factor, PQBP1
                     and PP1 interacting; SH3 domain-binding protein SNP70;
                     splicing factor that interacts with PQBP-1 and PP1;
                     protein phosphatase 1, regulatory subunit 165"
                     /calculated_mol_wt=69867
     Region          1..45
                     /region_name="Required for nuclear import.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          12..92
                     /region_name="Wbp11"
                     /note="WW domain binding protein 11; pfam09429"
                     /db_xref="CDD:462795"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          191..209
                     /region_name="proline-rich region"
     Site            192
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          217..221
                     /region_name="Interaction with PP1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q923D5; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          306..310
                     /region_name="Interaction with PP1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          404..538
                     /region_name="proline-rich region"
     Site            565
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923D5; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Region          587..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W2.1)"
     CDS             1..641
                     /gene="WBP11"
                     /gene_synonym="BUG13; CFAP90; FAP90; NPWBP; PPP1R165;
                     SIPP1; VCTERL; VCTRL; WBP-11"
                     /coded_by="NM_016312.3:173..2098"
                     /db_xref="CCDS:CCDS8666.1"
                     /db_xref="GeneID:51729"
                     /db_xref="HGNC:HGNC:16461"
                     /db_xref="MIM:618083"
ORIGIN      
        1 mgrrstsstk sgkfmnptdq arkearkrel kknkkqrmmv raavlkmkdp kqiirdmekl
       61 demefnpvqq pqlnekvlkd krkklretfe rilrlyeken pdiykelrkl eveyeqkraq
      121 lsqyfdavkn aqhvevesip lpdmphapsn iliqdiplpg aqppsilkkt saygpptrav
      181 silpllghgv prlppgrkpp gpppgppppq vvqmygrkvg faldlpprrr dedmlyspel
      241 aqrghdddvs stseddgype dmdqdkhdds tddsdtdksd gesdgdefvh rdngerdnne
      301 ekksglsvrf admpgksrkk kknmkeltpl qammlrmagq eipeegreve efsedddedd
      361 sddseaekqs qkqhkeeshs dgtstassqq qappqsvpps qiqappmpgp pplgpppapp
      421 lrppgpptgl ppgpppgapp flrppgmpgl rgplprllpp gpppgrppgp ppgpppglpp
      481 gppprgpppr lpppappgip pprpgmmrpp lvpplgpapp glfppaplpn pgvlsappnl
      541 iqrpkaddts aatiekkata tisakpqitn pkaeitrfvp talrvrrenk gataapqrks
      601 eddsavplak aapksgpsvp vsvqtkddvy eafmkemegl l
//
