Full text data of PWP1
PWP1
[Confidence: low (only semi-automatic identification from reviews)]
Periodic tryptophan protein 1 homolog (Keratinocyte protein IEF SSP 9502)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Periodic tryptophan protein 1 homolog (Keratinocyte protein IEF SSP 9502)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13610
ID PWP1_HUMAN Reviewed; 501 AA.
AC Q13610; A8K3R6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Periodic tryptophan protein 1 homolog;
DE AltName: Full=Keratinocyte protein IEF SSP 9502;
GN Name=PWP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828893; DOI=10.1016/0378-1119(94)90673-4;
RA Honore B., Leffers H., Madsen P., Celis J.E.;
RT "Cloning of a cDNA encoding a novel human nuclear phosphoprotein
RT belonging to the WD-40 family.";
RL Gene 151:291-296(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND SER-59,
RP AND MASS SPECTROMETRY.
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].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-55; SER-57 AND
RP SER-59, AND MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND THR-86,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play an important role in cell growth and/or
CC transcription.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: High levels seen in the placenta, skeletal
CC muscle, kidney and pancreas while lower levels were seen in the
CC heart, brain and lung.
CC -!- SIMILARITY: Belongs to the WD repeat PWP1 family.
CC -!- SIMILARITY: Contains 5 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L07758; AAA65201.1; -; mRNA.
DR EMBL; AK290681; BAF83370.1; -; mRNA.
DR EMBL; CH471054; EAW97802.1; -; Genomic_DNA.
DR PIR; I39360; I39360.
DR RefSeq; NP_008993.1; NM_007062.1.
DR UniGene; Hs.506652; -.
DR ProteinModelPortal; Q13610; -.
DR SMR; Q13610; 192-463.
DR IntAct; Q13610; 6.
DR MINT; MINT-3028185; -.
DR STRING; 9606.ENSP00000258531; -.
DR PhosphoSite; Q13610; -.
DR DMDM; 2494897; -.
DR PaxDb; Q13610; -.
DR PeptideAtlas; Q13610; -.
DR PRIDE; Q13610; -.
DR DNASU; 11137; -.
DR Ensembl; ENST00000412830; ENSP00000387365; ENSG00000136045.
DR GeneID; 11137; -.
DR KEGG; hsa:11137; -.
DR UCSC; uc001tmo.1; human.
DR CTD; 11137; -.
DR GeneCards; GC12P108079; -.
DR HGNC; HGNC:17015; PWP1.
DR HPA; HPA038707; -.
DR neXtProt; NX_Q13610; -.
DR PharmGKB; PA142671112; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000212580; -.
DR HOVERGEN; HBG001543; -.
DR InParanoid; Q13610; -.
DR KO; K14791; -.
DR OMA; EWLDFPP; -.
DR OrthoDB; EOG7X3QR1; -.
DR PhylomeDB; Q13610; -.
DR SignaLink; Q13610; -.
DR ChiTaRS; PWP1; human.
DR GeneWiki; PWP1; -.
DR GenomeRNAi; 11137; -.
DR NextBio; 42336; -.
DR PRO; PR:Q13610; -.
DR ArrayExpress; Q13610; -.
DR Bgee; Q13610; -.
DR CleanEx; HS_PWP1; -.
DR Genevestigator; Q13610; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 501 Periodic tryptophan protein 1 homolog.
FT /FTId=PRO_0000051171.
FT REPEAT 186 230 WD 1.
FT REPEAT 254 294 WD 2.
FT REPEAT 297 337 WD 3.
FT REPEAT 383 423 WD 4.
FT REPEAT 428 468 WD 5.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 55 55 Phosphothreonine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 59 59 Phosphoserine.
FT MOD_RES 86 86 Phosphothreonine.
FT VARIANT 288 288 L -> F (in dbSNP:rs11547907).
FT /FTId=VAR_033808.
SQ SEQUENCE 501 AA; 55828 MW; 16CC8EF2BAC8DFF0 CRC64;
MNRSRQVTCV AWVRCGVAKE TPDKVELSKE EVKRLIAEAK EKLQEEGGGS DEEETGSPSE
DGMQSARTQA RPREPLEDGD PEDDRTLDDD ELAEYDLDKY DEEGDPDAET LGESLLGLTV
YGSNDQDPYV TLKDTEQYER EDFLIKPSDN LIVCGRAEQD QCNLEVHVYN QEEDSFYVHH
DILLSAYPLS VEWLNFDPSP DDSTGNYIAV GNMTPVIEVW DLDIVDSLEP VFTLGSKLSK
KKKKKGKKSS SAEGHTDAVL DLSWNKLIRN VLASASADNT VILWDMSLGK PAASLAVHTD
KVQTLQFHPF EAQTLISGSY DKSVALYDCR SPDESHRMWR FSGQIERVTW NHFSPCHFLA
STDDGFVYNL DARSDKPIFT LNAHNDEISG LDLSSQIKGC LVTASADKYV KIWDILGDRP
SLVHSRDMKM GVLFCSSCCP DLPFIYAFGG QKEGLRVWDI STVSSVNEAF GRRERLVLGS
ARNSSISGPF GSRSSDTPME S
//
ID PWP1_HUMAN Reviewed; 501 AA.
AC Q13610; A8K3R6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Periodic tryptophan protein 1 homolog;
DE AltName: Full=Keratinocyte protein IEF SSP 9502;
GN Name=PWP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828893; DOI=10.1016/0378-1119(94)90673-4;
RA Honore B., Leffers H., Madsen P., Celis J.E.;
RT "Cloning of a cDNA encoding a novel human nuclear phosphoprotein
RT belonging to the WD-40 family.";
RL Gene 151:291-296(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND SER-59,
RP AND MASS SPECTROMETRY.
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].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-55; SER-57 AND
RP SER-59, AND MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND THR-86,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play an important role in cell growth and/or
CC transcription.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: High levels seen in the placenta, skeletal
CC muscle, kidney and pancreas while lower levels were seen in the
CC heart, brain and lung.
CC -!- SIMILARITY: Belongs to the WD repeat PWP1 family.
CC -!- SIMILARITY: Contains 5 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L07758; AAA65201.1; -; mRNA.
DR EMBL; AK290681; BAF83370.1; -; mRNA.
DR EMBL; CH471054; EAW97802.1; -; Genomic_DNA.
DR PIR; I39360; I39360.
DR RefSeq; NP_008993.1; NM_007062.1.
DR UniGene; Hs.506652; -.
DR ProteinModelPortal; Q13610; -.
DR SMR; Q13610; 192-463.
DR IntAct; Q13610; 6.
DR MINT; MINT-3028185; -.
DR STRING; 9606.ENSP00000258531; -.
DR PhosphoSite; Q13610; -.
DR DMDM; 2494897; -.
DR PaxDb; Q13610; -.
DR PeptideAtlas; Q13610; -.
DR PRIDE; Q13610; -.
DR DNASU; 11137; -.
DR Ensembl; ENST00000412830; ENSP00000387365; ENSG00000136045.
DR GeneID; 11137; -.
DR KEGG; hsa:11137; -.
DR UCSC; uc001tmo.1; human.
DR CTD; 11137; -.
DR GeneCards; GC12P108079; -.
DR HGNC; HGNC:17015; PWP1.
DR HPA; HPA038707; -.
DR neXtProt; NX_Q13610; -.
DR PharmGKB; PA142671112; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000212580; -.
DR HOVERGEN; HBG001543; -.
DR InParanoid; Q13610; -.
DR KO; K14791; -.
DR OMA; EWLDFPP; -.
DR OrthoDB; EOG7X3QR1; -.
DR PhylomeDB; Q13610; -.
DR SignaLink; Q13610; -.
DR ChiTaRS; PWP1; human.
DR GeneWiki; PWP1; -.
DR GenomeRNAi; 11137; -.
DR NextBio; 42336; -.
DR PRO; PR:Q13610; -.
DR ArrayExpress; Q13610; -.
DR Bgee; Q13610; -.
DR CleanEx; HS_PWP1; -.
DR Genevestigator; Q13610; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 501 Periodic tryptophan protein 1 homolog.
FT /FTId=PRO_0000051171.
FT REPEAT 186 230 WD 1.
FT REPEAT 254 294 WD 2.
FT REPEAT 297 337 WD 3.
FT REPEAT 383 423 WD 4.
FT REPEAT 428 468 WD 5.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 55 55 Phosphothreonine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 59 59 Phosphoserine.
FT MOD_RES 86 86 Phosphothreonine.
FT VARIANT 288 288 L -> F (in dbSNP:rs11547907).
FT /FTId=VAR_033808.
SQ SEQUENCE 501 AA; 55828 MW; 16CC8EF2BAC8DFF0 CRC64;
MNRSRQVTCV AWVRCGVAKE TPDKVELSKE EVKRLIAEAK EKLQEEGGGS DEEETGSPSE
DGMQSARTQA RPREPLEDGD PEDDRTLDDD ELAEYDLDKY DEEGDPDAET LGESLLGLTV
YGSNDQDPYV TLKDTEQYER EDFLIKPSDN LIVCGRAEQD QCNLEVHVYN QEEDSFYVHH
DILLSAYPLS VEWLNFDPSP DDSTGNYIAV GNMTPVIEVW DLDIVDSLEP VFTLGSKLSK
KKKKKGKKSS SAEGHTDAVL DLSWNKLIRN VLASASADNT VILWDMSLGK PAASLAVHTD
KVQTLQFHPF EAQTLISGSY DKSVALYDCR SPDESHRMWR FSGQIERVTW NHFSPCHFLA
STDDGFVYNL DARSDKPIFT LNAHNDEISG LDLSSQIKGC LVTASADKYV KIWDILGDRP
SLVHSRDMKM GVLFCSSCCP DLPFIYAFGG QKEGLRVWDI STVSSVNEAF GRRERLVLGS
ARNSSISGPF GSRSSDTPME S
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