Full text data of HS1BP3
HS1BP3
[Confidence: low (only semi-automatic identification from reviews)]
HCLS1-binding protein 3 (HS1-binding protein 3; HSP1BP-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
HCLS1-binding protein 3 (HS1-binding protein 3; HSP1BP-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q53T59
ID H1BP3_HUMAN Reviewed; 392 AA.
AC Q53T59; B2RAW2; D6W529; Q86VC2; Q8N367;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2005, sequence version 1.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=HCLS1-binding protein 3;
DE AltName: Full=HS1-binding protein 3;
DE Short=HSP1BP-3;
GN Name=HS1BP3;
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 [LARGE SCALE MRNA], AND VARIANT MET-260.
RC TISSUE=Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-260 AND
RP THR-388.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-337, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3 AND SER-194, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be a modulator of IL-2 signaling (By similarity).
CC -!- SUBUNIT: Binds HCLS1. Interacts with the SH3 domain of HCLS1 in
CC vitro (By similarity).
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AK314383; BAG37009.1; -; mRNA.
DR EMBL; AC012065; AAX93235.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00814.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00816.1; -; Genomic_DNA.
DR EMBL; BC050636; AAH50636.1; -; mRNA.
DR RefSeq; NP_071905.3; NM_022460.3.
DR UniGene; Hs.531785; -.
DR ProteinModelPortal; Q53T59; -.
DR STRING; 9606.ENSP00000305193; -.
DR PhosphoSite; Q53T59; -.
DR DMDM; 74726842; -.
DR PaxDb; Q53T59; -.
DR PeptideAtlas; Q53T59; -.
DR PRIDE; Q53T59; -.
DR Ensembl; ENST00000304031; ENSP00000305193; ENSG00000118960.
DR GeneID; 64342; -.
DR KEGG; hsa:64342; -.
DR UCSC; uc002rdw.1; human.
DR CTD; 64342; -.
DR GeneCards; GC02M020760; -.
DR HGNC; HGNC:24979; HS1BP3.
DR HPA; HPA035050; -.
DR MIM; 609359; gene.
DR neXtProt; NX_Q53T59; -.
DR PharmGKB; PA162391602; -.
DR eggNOG; NOG27752; -.
DR HOGENOM; HOG000112839; -.
DR HOVERGEN; HBG098900; -.
DR InParanoid; Q53T59; -.
DR OMA; IRDHDTP; -.
DR PhylomeDB; Q53T59; -.
DR ChiTaRS; HS1BP3; human.
DR GenomeRNAi; 64342; -.
DR NextBio; 66275; -.
DR PRO; PR:Q53T59; -.
DR ArrayExpress; Q53T59; -.
DR Bgee; Q53T59; -.
DR CleanEx; HS_HS1BP3; -.
DR Genevestigator; Q53T59; -.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 392 HCLS1-binding protein 3.
FT /FTId=PRO_0000313802.
FT DOMAIN 19 142 PX.
FT COMPBIAS 196 199 Poly-Glu.
FT COMPBIAS 212 237 Pro-rich.
FT COMPBIAS 324 352 Pro-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 139 139 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 337 337 N6-acetyllysine.
FT VARIANT 260 260 V -> M (in dbSNP:rs2305458).
FT /FTId=VAR_037741.
FT VARIANT 273 273 G -> R (in dbSNP:rs35589938).
FT /FTId=VAR_037742.
FT VARIANT 348 348 P -> R (in dbSNP:rs35579164).
FT /FTId=VAR_037743.
FT VARIANT 388 388 A -> T (in dbSNP:rs3732149).
FT /FTId=VAR_037744.
SQ SEQUENCE 392 AA; 42780 MW; 2A360915F833FAE8 CRC64;
MQSPAVLVTS RRLQNAHTGL DLTVPQHQEV RGKMMSGHVE YQILVVTRLA AFKSAKHRPE
DVVQFLVSKK YSEIEEFYQK LSSRYAAASL PPLPRKVLFV GESDIRERRA VFNEILRCVS
KDAELAGSPE LLEFLGTRSP GAAGLTSRDS SVLDGTDSQT GNDEEAFDFF EEQDQVAEEG
PPVQSLKGED AEESLEEEEA LDPLGIMRSK KPKKHPKVAV KAKPSPRLTI FDEEVDPDEG
LFGPGRKLSP QDPSEDVSSV DPLKLFDDPD LGGAIPLGDS LLLPAACESG GPTPSLSHRD
ASKELFRVEE DLDQILNLGA EPKPKPQLKP KPPVAAKPVI PRKPAVPPKA GPAEAVAGQQ
KPQEQIQAMD EMDILQYIQD HDTPAQAAPS LF
//
ID H1BP3_HUMAN Reviewed; 392 AA.
AC Q53T59; B2RAW2; D6W529; Q86VC2; Q8N367;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2005, sequence version 1.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=HCLS1-binding protein 3;
DE AltName: Full=HS1-binding protein 3;
DE Short=HSP1BP-3;
GN Name=HS1BP3;
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 [LARGE SCALE MRNA], AND VARIANT MET-260.
RC TISSUE=Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-260 AND
RP THR-388.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-337, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3 AND SER-194, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be a modulator of IL-2 signaling (By similarity).
CC -!- SUBUNIT: Binds HCLS1. Interacts with the SH3 domain of HCLS1 in
CC vitro (By similarity).
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AK314383; BAG37009.1; -; mRNA.
DR EMBL; AC012065; AAX93235.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00814.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00816.1; -; Genomic_DNA.
DR EMBL; BC050636; AAH50636.1; -; mRNA.
DR RefSeq; NP_071905.3; NM_022460.3.
DR UniGene; Hs.531785; -.
DR ProteinModelPortal; Q53T59; -.
DR STRING; 9606.ENSP00000305193; -.
DR PhosphoSite; Q53T59; -.
DR DMDM; 74726842; -.
DR PaxDb; Q53T59; -.
DR PeptideAtlas; Q53T59; -.
DR PRIDE; Q53T59; -.
DR Ensembl; ENST00000304031; ENSP00000305193; ENSG00000118960.
DR GeneID; 64342; -.
DR KEGG; hsa:64342; -.
DR UCSC; uc002rdw.1; human.
DR CTD; 64342; -.
DR GeneCards; GC02M020760; -.
DR HGNC; HGNC:24979; HS1BP3.
DR HPA; HPA035050; -.
DR MIM; 609359; gene.
DR neXtProt; NX_Q53T59; -.
DR PharmGKB; PA162391602; -.
DR eggNOG; NOG27752; -.
DR HOGENOM; HOG000112839; -.
DR HOVERGEN; HBG098900; -.
DR InParanoid; Q53T59; -.
DR OMA; IRDHDTP; -.
DR PhylomeDB; Q53T59; -.
DR ChiTaRS; HS1BP3; human.
DR GenomeRNAi; 64342; -.
DR NextBio; 66275; -.
DR PRO; PR:Q53T59; -.
DR ArrayExpress; Q53T59; -.
DR Bgee; Q53T59; -.
DR CleanEx; HS_HS1BP3; -.
DR Genevestigator; Q53T59; -.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 392 HCLS1-binding protein 3.
FT /FTId=PRO_0000313802.
FT DOMAIN 19 142 PX.
FT COMPBIAS 196 199 Poly-Glu.
FT COMPBIAS 212 237 Pro-rich.
FT COMPBIAS 324 352 Pro-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 139 139 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 337 337 N6-acetyllysine.
FT VARIANT 260 260 V -> M (in dbSNP:rs2305458).
FT /FTId=VAR_037741.
FT VARIANT 273 273 G -> R (in dbSNP:rs35589938).
FT /FTId=VAR_037742.
FT VARIANT 348 348 P -> R (in dbSNP:rs35579164).
FT /FTId=VAR_037743.
FT VARIANT 388 388 A -> T (in dbSNP:rs3732149).
FT /FTId=VAR_037744.
SQ SEQUENCE 392 AA; 42780 MW; 2A360915F833FAE8 CRC64;
MQSPAVLVTS RRLQNAHTGL DLTVPQHQEV RGKMMSGHVE YQILVVTRLA AFKSAKHRPE
DVVQFLVSKK YSEIEEFYQK LSSRYAAASL PPLPRKVLFV GESDIRERRA VFNEILRCVS
KDAELAGSPE LLEFLGTRSP GAAGLTSRDS SVLDGTDSQT GNDEEAFDFF EEQDQVAEEG
PPVQSLKGED AEESLEEEEA LDPLGIMRSK KPKKHPKVAV KAKPSPRLTI FDEEVDPDEG
LFGPGRKLSP QDPSEDVSSV DPLKLFDDPD LGGAIPLGDS LLLPAACESG GPTPSLSHRD
ASKELFRVEE DLDQILNLGA EPKPKPQLKP KPPVAAKPVI PRKPAVPPKA GPAEAVAGQQ
KPQEQIQAMD EMDILQYIQD HDTPAQAAPS LF
//
MIM
609359
*RECORD*
*FIELD* NO
609359
*FIELD* TI
*609359 HS1-BINDING PROTEIN 3; HS1BP3
;;FLJ14249
*FIELD* TX
CLONING
Higgins et al. (2005) identified the HS1BP3 gene, corresponding to the
read moreFLJ14249 transcript, in a search for candidate genes for familial
essential tremor (see 190300). The full-length transcript consists of
3,323 basepairs. Two putative alternatively spliced variants encode
distinct protein isoforms; the first, of 2,376 basepairs, encodes a
protein with a divergent C terminus, and the second 1,795-basepair
variant lacks an internal region present in the first variant. By
RT-PCR, Higgins et al. (2005) demonstrated that the HS1BP3 gene and its
2 isoforms are expressed in human brain. The murine Hs1bp3 gene is
expressed in brain and binds to Hs1 protein (Takemoto et al., 1999).
GENE FUNCTION
HS1BP3 binds members of the 14-3-3 protein family (see 609009), which
are highly expressed in motor neurons and Purkinje cells and regulate
the Ca(2+)/calmodulin-dependent protein kinase activation of tyrosine
and tryptophan hydroxylase (Higgins et al., 2005; Takemoto et al.,
1999).
GENE STRUCTURE
Higgins et al. (2005) determined that the HS1BP3 gene contains 7 exons.
MAPPING
Higgins et al. (2005) identified the HS1BP3 gene within the candidate
region for familial essential tremor on chromosome 2p24.1 (ETM2;
602134).
MOLECULAR GENETICS
Although Higgins et al. (2005) suggested that a substitution in the
HS1BP3 gene was associated with familial essential tremor linked to
chromosome 2p24 (602134), Deng et al. (2005) found no association
between the reported substitution and essential tremor or Parkinson
disease (168600) among 222 and 285 affected patients, respectively.
Furthermore, the substitution allele was present in 12 (9.1%) of 132
control individuals, indicating it is a polymorphism.
*FIELD* RF
1. Deng, H.; Le, W. D.; Guo, Y.; Huang, M. S.; Xie, W. J.; Jankovic,
J.: Extended study of A265G variant of HS1BP3 in essential tremor
and Parkinson disease. Neurology 65: 651-652, 2005.
2. Higgins, J. J.; Lombardi, R. Q.; Pucilowska, J.; Jankovic, J.;
Tan, E. K.; Rooney, J. P.: A variant in the HS1-BP3 gene is associated
with familial essential tremor. Neurology 64: 417-421, 2005.
3. Takemoto, Y.; Furuta, M.; Sato, M.; Kubo, M.; Hashimoto, Y.: Isolation
and characterization of a novel HS1 SH3 domain binding protein, HS1BP3. Int.
Immun. 11: 1957-1964, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 11/2/2005
*FIELD* CD
Victor A. McKusick: 5/10/2005
*FIELD* ED
carol: 04/10/2006
ckniffin: 11/2/2005
wwang: 5/18/2005
alopez: 5/17/2005
wwang: 5/10/2005
*RECORD*
*FIELD* NO
609359
*FIELD* TI
*609359 HS1-BINDING PROTEIN 3; HS1BP3
;;FLJ14249
*FIELD* TX
CLONING
Higgins et al. (2005) identified the HS1BP3 gene, corresponding to the
read moreFLJ14249 transcript, in a search for candidate genes for familial
essential tremor (see 190300). The full-length transcript consists of
3,323 basepairs. Two putative alternatively spliced variants encode
distinct protein isoforms; the first, of 2,376 basepairs, encodes a
protein with a divergent C terminus, and the second 1,795-basepair
variant lacks an internal region present in the first variant. By
RT-PCR, Higgins et al. (2005) demonstrated that the HS1BP3 gene and its
2 isoforms are expressed in human brain. The murine Hs1bp3 gene is
expressed in brain and binds to Hs1 protein (Takemoto et al., 1999).
GENE FUNCTION
HS1BP3 binds members of the 14-3-3 protein family (see 609009), which
are highly expressed in motor neurons and Purkinje cells and regulate
the Ca(2+)/calmodulin-dependent protein kinase activation of tyrosine
and tryptophan hydroxylase (Higgins et al., 2005; Takemoto et al.,
1999).
GENE STRUCTURE
Higgins et al. (2005) determined that the HS1BP3 gene contains 7 exons.
MAPPING
Higgins et al. (2005) identified the HS1BP3 gene within the candidate
region for familial essential tremor on chromosome 2p24.1 (ETM2;
602134).
MOLECULAR GENETICS
Although Higgins et al. (2005) suggested that a substitution in the
HS1BP3 gene was associated with familial essential tremor linked to
chromosome 2p24 (602134), Deng et al. (2005) found no association
between the reported substitution and essential tremor or Parkinson
disease (168600) among 222 and 285 affected patients, respectively.
Furthermore, the substitution allele was present in 12 (9.1%) of 132
control individuals, indicating it is a polymorphism.
*FIELD* RF
1. Deng, H.; Le, W. D.; Guo, Y.; Huang, M. S.; Xie, W. J.; Jankovic,
J.: Extended study of A265G variant of HS1BP3 in essential tremor
and Parkinson disease. Neurology 65: 651-652, 2005.
2. Higgins, J. J.; Lombardi, R. Q.; Pucilowska, J.; Jankovic, J.;
Tan, E. K.; Rooney, J. P.: A variant in the HS1-BP3 gene is associated
with familial essential tremor. Neurology 64: 417-421, 2005.
3. Takemoto, Y.; Furuta, M.; Sato, M.; Kubo, M.; Hashimoto, Y.: Isolation
and characterization of a novel HS1 SH3 domain binding protein, HS1BP3. Int.
Immun. 11: 1957-1964, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 11/2/2005
*FIELD* CD
Victor A. McKusick: 5/10/2005
*FIELD* ED
carol: 04/10/2006
ckniffin: 11/2/2005
wwang: 5/18/2005
alopez: 5/17/2005
wwang: 5/10/2005