Full text data of SPAG9
SPAG9
(HSS, KIAA0516, MAPK8IP4, SYD1)
[Confidence: low (only semi-automatic identification from reviews)]
C-Jun-amino-terminal kinase-interacting protein 4; JIP-4; JNK-interacting protein 4 (Cancer/testis antigen 89; CT89; Human lung cancer oncogene 6 protein; HLC-6; JNK-associated leucine-zipper protein; JLP; Mitogen-activated protein kinase 8-interacting protein 4; Proliferation-inducing protein 6; Protein highly expressed in testis; PHET; Sperm surface protein; Sperm-associated antigen 9; Sperm-specific protein; Sunday driver 1)
C-Jun-amino-terminal kinase-interacting protein 4; JIP-4; JNK-interacting protein 4 (Cancer/testis antigen 89; CT89; Human lung cancer oncogene 6 protein; HLC-6; JNK-associated leucine-zipper protein; JLP; Mitogen-activated protein kinase 8-interacting protein 4; Proliferation-inducing protein 6; Protein highly expressed in testis; PHET; Sperm surface protein; Sperm-associated antigen 9; Sperm-specific protein; Sunday driver 1)
UniProt
O60271
ID JIP4_HUMAN Reviewed; 1321 AA.
AC O60271; A6H8U5; A8MSX0; B4DHH2; O60905; Q3KQU8; Q3MKM7; Q86WC7;
read moreAC Q86WC8; Q8IZX7; Q96II0; Q9H811;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 4.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE Short=JIP-4;
DE Short=JNK-interacting protein 4;
DE AltName: Full=Cancer/testis antigen 89;
DE Short=CT89;
DE AltName: Full=Human lung cancer oncogene 6 protein;
DE Short=HLC-6;
DE AltName: Full=JNK-associated leucine-zipper protein;
DE Short=JLP;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE AltName: Full=Proliferation-inducing protein 6;
DE AltName: Full=Protein highly expressed in testis;
DE Short=PHET;
DE AltName: Full=Sperm surface protein;
DE AltName: Full=Sperm-associated antigen 9;
DE AltName: Full=Sperm-specific protein;
DE AltName: Full=Sunday driver 1;
GN Name=SPAG9; Synonyms=HSS, KIAA0516, MAPK8IP4, SYD1; ORFNames=HLC6;
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] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
RT and transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
RA Wells J.W., Banham A.H., Mufti G.J.;
RT "Humoral detection of leukaemia-associated antigens in presentation
RT acute myeloid leukaemia.";
RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Brain, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORMS 2/4/5).
RC TISSUE=Eye, and Kidney;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9480848; DOI=10.1006/bbrc.1997.7943;
RA Shankar S., Mohapatra B., Suri A.;
RT "Cloning of a novel human testis mRNA specifically expressed in
RT testicular haploid germ cells, having unique palindromic sequences and
RT encoding a leucine zipper dimerization motif.";
RL Biochem. Biophys. Res. Commun. 243:561-565(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Testis;
RX PubMed=14662895;
RA Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y.,
RA Ikeda Y., Kuwana M.;
RT "A novel protein highly expressed in testis is overexpressed in
RT systemic sclerosis fibroblasts and targeted by autoantibodies.";
RL J. Immunol. 171:6883-6890(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH NFKB1.
RX PubMed=14743216; DOI=10.1038/ncb1086;
RA Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
RA Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S.,
RA Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J.,
RA Schwab M., Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C.,
RA Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B.,
RA Superti-Furga G.;
RT "A physical and functional map of the human TNF-alpha/NF-kappa B
RT signal transduction pathway.";
RL Nat. Cell Biol. 6:97-105(2004).
RN [12]
RP FUNCTION, INTERACTION WITH MAPK9; MAPK10 AND MAPK8, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RX PubMed=15693750; DOI=10.1042/BJ20041577;
RA Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
RA Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
RT "Characterization of a novel human sperm-associated antigen 9 (SPAG9)
RT having structural homology with c-Jun N-terminal kinase-interacting
RT protein.";
RL Biochem. J. 389:73-82(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, AND
RP MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-272
RP AND THR-418, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; THR-217;
RP SER-311; SER-329; SER-332; THR-418; THR-586 AND SER-733, AND MASS
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217 AND
RP SER-733, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-194; SER-203;
RP THR-217; SER-251; SER-265; SER-268; SER-272; SER-329; SER-332;
RP SER-347; THR-348; THR-418; SER-730 AND SER-733, 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; SER-329
RP AND SER-332, AND MASS 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 [22]
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).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH
RP ARF6, COILED COIL, SUBUNIT, AND INTERACTION WITH ARF6.
RX PubMed=19644450; DOI=10.1038/emboj.2009.209;
RA Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
RA England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
RT "The structural basis of Arf effector specificity: the crystal
RT structure of ARF6 in a complex with JIP4.";
RL EMBO J. 28:2835-2845(2009).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC proteins selectively mediates JNK signaling by aggregating
CC specific components of the MAPK cascade to form a functional JNK
CC signaling module. Isoform 5 may play a role in spermatozoa-egg-
CC interaction.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with ARF6, forming a
CC heterotetramer. Homooligomer. Interacts with MAX, MAPK8, MAPK9,
CC MAPK10, MAPK14, MAP3K3, MYC, KNS2 and MAP2K4. Interaction with
CC KNS2 is important in the formation of ternary complex with MAPK8.
CC Interacts with NFKB1.
CC -!- INTERACTION:
CC P84077:ARF1; NbExp=3; IntAct=EBI-1023301, EBI-447171;
CC P62330:ARF6; NbExp=8; IntAct=EBI-1023301, EBI-638181;
CC P62331:Arf6 (xeno); NbExp=2; IntAct=EBI-1023301, EBI-988682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Note=Perinuclear distribution in response to stress signals such
CC as UV radiation.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle, secretory
CC vesicle, acrosome. Note=Associated with the plasma membrane of the
CC acrosomal compartment and also localizes in the acrosome matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O60271-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60271-2; Sequence=VSP_018214, VSP_018220;
CC Name=3;
CC IsoId=O60271-3; Sequence=VSP_018221, VSP_018222;
CC Note=Due to intron retention;
CC Name=4;
CC IsoId=O60271-4; Sequence=VSP_018214;
CC Name=5;
CC IsoId=O60271-5; Sequence=VSP_018214, VSP_018221, VSP_018222;
CC Name=6;
CC IsoId=O60271-9; Sequence=VSP_042253, VSP_018214, VSP_042254;
CC Note=No experimental confirmation available. Ref.5 (BAG58134)
CC sequence is in conflict in position: 9:F->S;
CC -!- TISSUE SPECIFICITY: Isoform 5 is expressed only in testis on the
CC round spermatids of stage I, II and II. Isoform 5 is absent in
CC spermatogonia and spermatocyte. Isoform 3 is expressed in testis.
CC Isoform 4 is expressed in testis and in acute myeloid leukemia
CC (AML) patients.
CC -!- INDUCTION: Isoform 3 is increased in systemic sclerosis
CC fibroblasts.
CC -!- PTM: Phosphorylated by MAPK8 and MAPK14 (By similarity).
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07524.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAH59946.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAI06049.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part;
CC Sequence=AAO66462.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA25442.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB14812.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splicing;
CC Sequence=CAA62987.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF327452; AAN61565.1; -; mRNA.
DR EMBL; AY850123; AAX47276.1; -; mRNA.
DR EMBL; AB011088; BAA25442.3; ALT_INIT; mRNA.
DR EMBL; AK024068; BAB14812.1; ALT_SEQ; mRNA.
DR EMBL; AK295098; BAG58134.1; -; mRNA.
DR EMBL; AK302789; BAG63993.1; -; mRNA.
DR EMBL; AC005920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007524; AAH07524.1; ALT_SEQ; mRNA.
DR EMBL; BC059946; AAH59946.1; ALT_SEQ; mRNA.
DR EMBL; BC106048; AAI06049.1; ALT_SEQ; mRNA.
DR EMBL; BC146755; AAI46756.1; -; mRNA.
DR EMBL; BC153878; AAI53879.1; -; mRNA.
DR EMBL; X91879; CAA62987.1; ALT_INIT; mRNA.
DR EMBL; AY219897; AAO66462.1; ALT_INIT; mRNA.
DR EMBL; AY219898; AAO66463.1; -; mRNA.
DR PIR; JC5958; JC5958.
DR RefSeq; NP_001123999.1; NM_001130527.2.
DR RefSeq; NP_001124000.1; NM_001130528.2.
DR RefSeq; NP_001238900.1; NM_001251971.1.
DR RefSeq; NP_003962.3; NM_003971.5.
DR UniGene; Hs.463439; -.
DR PDB; 2W83; X-ray; 1.93 A; C/D=406-476.
DR PDBsum; 2W83; -.
DR ProteinModelPortal; O60271; -.
DR SMR; O60271; 406-466, 1066-1116.
DR IntAct; O60271; 10.
DR MINT; MINT-1136008; -.
DR PhosphoSite; O60271; -.
DR PaxDb; O60271; -.
DR PRIDE; O60271; -.
DR DNASU; 9043; -.
DR Ensembl; ENST00000262013; ENSP00000262013; ENSG00000008294.
DR Ensembl; ENST00000357122; ENSP00000349636; ENSG00000008294.
DR Ensembl; ENST00000505279; ENSP00000426900; ENSG00000008294.
DR Ensembl; ENST00000510283; ENSP00000423165; ENSG00000008294.
DR GeneID; 9043; -.
DR KEGG; hsa:9043; -.
DR UCSC; uc002itc.3; human.
DR CTD; 9043; -.
DR GeneCards; GC17M049039; -.
DR HGNC; HGNC:14524; SPAG9.
DR HPA; HPA040446; -.
DR MIM; 605430; gene.
DR neXtProt; NX_O60271; -.
DR PharmGKB; PA37890; -.
DR eggNOG; NOG270333; -.
DR HOGENOM; HOG000290716; -.
DR HOVERGEN; HBG024110; -.
DR InParanoid; O60271; -.
DR OMA; GSDQLES; -.
DR OrthoDB; EOG7GXP9P; -.
DR Reactome; REACT_111045; Developmental Biology.
DR SignaLink; O60271; -.
DR ChiTaRS; SPAG9; human.
DR EvolutionaryTrace; O60271; -.
DR GeneWiki; SPAG9; -.
DR GenomeRNAi; 9043; -.
DR NextBio; 33871; -.
DR PMAP-CutDB; O60271; -.
DR PRO; PR:O60271; -.
DR ArrayExpress; O60271; -.
DR Bgee; O60271; -.
DR Genevestigator; O60271; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0007257; P:activation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; TAS:Reactome.
DR GO; GO:0090074; P:negative regulation of protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 1321 C-Jun-amino-terminal kinase-interacting
FT protein 4.
FT /FTId=PRO_0000234076.
FT COILED 66 166 Potential.
FT COILED 408 534
FT COILED 724 758 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 109 109 Phosphoserine.
FT MOD_RES 183 183 Phosphoserine.
FT MOD_RES 185 185 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 217 217 Phosphothreonine.
FT MOD_RES 251 251 Phosphoserine.
FT MOD_RES 265 265 Phosphoserine.
FT MOD_RES 268 268 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 311 311 Phosphoserine.
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 348 348 Phosphothreonine.
FT MOD_RES 365 365 Phosphothreonine (By similarity).
FT MOD_RES 418 418 Phosphothreonine.
FT MOD_RES 586 586 Phosphothreonine.
FT MOD_RES 730 730 Phosphoserine.
FT MOD_RES 733 733 Phosphoserine.
FT VAR_SEQ 1 196 MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGR
FT YDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDN
FT EQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVES
FT LESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHT
FT EMIHNYMEHLERTKLHQLSGSDQLESTAHSRI -> MSPGC
FT MLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALT
FT QNLPRIL (in isoform 6).
FT /FTId=VSP_042253.
FT VAR_SEQ 248 261 Missing (in isoform 2, isoform 4, isoform
FT 5 and isoform 6).
FT /FTId=VSP_018214.
FT VAR_SEQ 555 555 F -> FVPTR (in isoform 2).
FT /FTId=VSP_018220.
FT VAR_SEQ 938 945 SNDSDAYK -> RYNNGSST (in isoform 3 and
FT isoform 5).
FT /FTId=VSP_018221.
FT VAR_SEQ 946 1321 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_018222.
FT VAR_SEQ 1175 1175 T -> TVILHQGRLLGLRA (in isoform 6).
FT /FTId=VSP_042254.
FT VARIANT 1320 1320 N -> S (in dbSNP:rs9896965).
FT /FTId=VAR_059364.
FT CONFLICT 451 451 E -> G (in Ref. 9; AAO66462).
FT CONFLICT 680 680 E -> K (in Ref. 8; CAA62987 and 9;
FT AAO66462).
FT HELIX 406 465
SQ SEQUENCE 1321 AA; 146205 MW; 5CAE349FBDF91B40 CRC64;
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
QLSGSDQLES TAHSRIRKER PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP
RSHTSLKVSN SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE LDMDKDLSGY
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
LETKNALNIV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEEKNRELE EELRKARAEA
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
NPAMQEKKRS SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVTNG
QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDVAGLD
TEGSKQRSAS QSSLDKLDQE LKEQQKELKN QEELSSLVWI CTSTHSATKV LIIDAVQPGN
ILDSFTVCNS HVLCIASVPG ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG
GITVVGCSAE GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV LPNEQDLVRE
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG DKAGPSAQEP
GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMYGN
E
//
ID JIP4_HUMAN Reviewed; 1321 AA.
AC O60271; A6H8U5; A8MSX0; B4DHH2; O60905; Q3KQU8; Q3MKM7; Q86WC7;
read moreAC Q86WC8; Q8IZX7; Q96II0; Q9H811;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 4.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE Short=JIP-4;
DE Short=JNK-interacting protein 4;
DE AltName: Full=Cancer/testis antigen 89;
DE Short=CT89;
DE AltName: Full=Human lung cancer oncogene 6 protein;
DE Short=HLC-6;
DE AltName: Full=JNK-associated leucine-zipper protein;
DE Short=JLP;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE AltName: Full=Proliferation-inducing protein 6;
DE AltName: Full=Protein highly expressed in testis;
DE Short=PHET;
DE AltName: Full=Sperm surface protein;
DE AltName: Full=Sperm-associated antigen 9;
DE AltName: Full=Sperm-specific protein;
DE AltName: Full=Sunday driver 1;
GN Name=SPAG9; Synonyms=HSS, KIAA0516, MAPK8IP4, SYD1; ORFNames=HLC6;
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] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
RT and transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
RA Wells J.W., Banham A.H., Mufti G.J.;
RT "Humoral detection of leukaemia-associated antigens in presentation
RT acute myeloid leukaemia.";
RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Brain, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORMS 2/4/5).
RC TISSUE=Eye, and Kidney;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9480848; DOI=10.1006/bbrc.1997.7943;
RA Shankar S., Mohapatra B., Suri A.;
RT "Cloning of a novel human testis mRNA specifically expressed in
RT testicular haploid germ cells, having unique palindromic sequences and
RT encoding a leucine zipper dimerization motif.";
RL Biochem. Biophys. Res. Commun. 243:561-565(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Testis;
RX PubMed=14662895;
RA Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y.,
RA Ikeda Y., Kuwana M.;
RT "A novel protein highly expressed in testis is overexpressed in
RT systemic sclerosis fibroblasts and targeted by autoantibodies.";
RL J. Immunol. 171:6883-6890(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH NFKB1.
RX PubMed=14743216; DOI=10.1038/ncb1086;
RA Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
RA Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S.,
RA Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J.,
RA Schwab M., Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C.,
RA Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B.,
RA Superti-Furga G.;
RT "A physical and functional map of the human TNF-alpha/NF-kappa B
RT signal transduction pathway.";
RL Nat. Cell Biol. 6:97-105(2004).
RN [12]
RP FUNCTION, INTERACTION WITH MAPK9; MAPK10 AND MAPK8, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RX PubMed=15693750; DOI=10.1042/BJ20041577;
RA Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
RA Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
RT "Characterization of a novel human sperm-associated antigen 9 (SPAG9)
RT having structural homology with c-Jun N-terminal kinase-interacting
RT protein.";
RL Biochem. J. 389:73-82(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, AND
RP MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-272
RP AND THR-418, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; THR-217;
RP SER-311; SER-329; SER-332; THR-418; THR-586 AND SER-733, AND MASS
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217 AND
RP SER-733, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-194; SER-203;
RP THR-217; SER-251; SER-265; SER-268; SER-272; SER-329; SER-332;
RP SER-347; THR-348; THR-418; SER-730 AND SER-733, 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; SER-329
RP AND SER-332, AND MASS 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 [22]
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).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH
RP ARF6, COILED COIL, SUBUNIT, AND INTERACTION WITH ARF6.
RX PubMed=19644450; DOI=10.1038/emboj.2009.209;
RA Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
RA England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
RT "The structural basis of Arf effector specificity: the crystal
RT structure of ARF6 in a complex with JIP4.";
RL EMBO J. 28:2835-2845(2009).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC proteins selectively mediates JNK signaling by aggregating
CC specific components of the MAPK cascade to form a functional JNK
CC signaling module. Isoform 5 may play a role in spermatozoa-egg-
CC interaction.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with ARF6, forming a
CC heterotetramer. Homooligomer. Interacts with MAX, MAPK8, MAPK9,
CC MAPK10, MAPK14, MAP3K3, MYC, KNS2 and MAP2K4. Interaction with
CC KNS2 is important in the formation of ternary complex with MAPK8.
CC Interacts with NFKB1.
CC -!- INTERACTION:
CC P84077:ARF1; NbExp=3; IntAct=EBI-1023301, EBI-447171;
CC P62330:ARF6; NbExp=8; IntAct=EBI-1023301, EBI-638181;
CC P62331:Arf6 (xeno); NbExp=2; IntAct=EBI-1023301, EBI-988682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Note=Perinuclear distribution in response to stress signals such
CC as UV radiation.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle, secretory
CC vesicle, acrosome. Note=Associated with the plasma membrane of the
CC acrosomal compartment and also localizes in the acrosome matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O60271-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60271-2; Sequence=VSP_018214, VSP_018220;
CC Name=3;
CC IsoId=O60271-3; Sequence=VSP_018221, VSP_018222;
CC Note=Due to intron retention;
CC Name=4;
CC IsoId=O60271-4; Sequence=VSP_018214;
CC Name=5;
CC IsoId=O60271-5; Sequence=VSP_018214, VSP_018221, VSP_018222;
CC Name=6;
CC IsoId=O60271-9; Sequence=VSP_042253, VSP_018214, VSP_042254;
CC Note=No experimental confirmation available. Ref.5 (BAG58134)
CC sequence is in conflict in position: 9:F->S;
CC -!- TISSUE SPECIFICITY: Isoform 5 is expressed only in testis on the
CC round spermatids of stage I, II and II. Isoform 5 is absent in
CC spermatogonia and spermatocyte. Isoform 3 is expressed in testis.
CC Isoform 4 is expressed in testis and in acute myeloid leukemia
CC (AML) patients.
CC -!- INDUCTION: Isoform 3 is increased in systemic sclerosis
CC fibroblasts.
CC -!- PTM: Phosphorylated by MAPK8 and MAPK14 (By similarity).
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07524.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAH59946.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAI06049.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part;
CC Sequence=AAO66462.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA25442.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB14812.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splicing;
CC Sequence=CAA62987.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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DR EMBL; AF327452; AAN61565.1; -; mRNA.
DR EMBL; AY850123; AAX47276.1; -; mRNA.
DR EMBL; AB011088; BAA25442.3; ALT_INIT; mRNA.
DR EMBL; AK024068; BAB14812.1; ALT_SEQ; mRNA.
DR EMBL; AK295098; BAG58134.1; -; mRNA.
DR EMBL; AK302789; BAG63993.1; -; mRNA.
DR EMBL; AC005920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007524; AAH07524.1; ALT_SEQ; mRNA.
DR EMBL; BC059946; AAH59946.1; ALT_SEQ; mRNA.
DR EMBL; BC106048; AAI06049.1; ALT_SEQ; mRNA.
DR EMBL; BC146755; AAI46756.1; -; mRNA.
DR EMBL; BC153878; AAI53879.1; -; mRNA.
DR EMBL; X91879; CAA62987.1; ALT_INIT; mRNA.
DR EMBL; AY219897; AAO66462.1; ALT_INIT; mRNA.
DR EMBL; AY219898; AAO66463.1; -; mRNA.
DR PIR; JC5958; JC5958.
DR RefSeq; NP_001123999.1; NM_001130527.2.
DR RefSeq; NP_001124000.1; NM_001130528.2.
DR RefSeq; NP_001238900.1; NM_001251971.1.
DR RefSeq; NP_003962.3; NM_003971.5.
DR UniGene; Hs.463439; -.
DR PDB; 2W83; X-ray; 1.93 A; C/D=406-476.
DR PDBsum; 2W83; -.
DR ProteinModelPortal; O60271; -.
DR SMR; O60271; 406-466, 1066-1116.
DR IntAct; O60271; 10.
DR MINT; MINT-1136008; -.
DR PhosphoSite; O60271; -.
DR PaxDb; O60271; -.
DR PRIDE; O60271; -.
DR DNASU; 9043; -.
DR Ensembl; ENST00000262013; ENSP00000262013; ENSG00000008294.
DR Ensembl; ENST00000357122; ENSP00000349636; ENSG00000008294.
DR Ensembl; ENST00000505279; ENSP00000426900; ENSG00000008294.
DR Ensembl; ENST00000510283; ENSP00000423165; ENSG00000008294.
DR GeneID; 9043; -.
DR KEGG; hsa:9043; -.
DR UCSC; uc002itc.3; human.
DR CTD; 9043; -.
DR GeneCards; GC17M049039; -.
DR HGNC; HGNC:14524; SPAG9.
DR HPA; HPA040446; -.
DR MIM; 605430; gene.
DR neXtProt; NX_O60271; -.
DR PharmGKB; PA37890; -.
DR eggNOG; NOG270333; -.
DR HOGENOM; HOG000290716; -.
DR HOVERGEN; HBG024110; -.
DR InParanoid; O60271; -.
DR OMA; GSDQLES; -.
DR OrthoDB; EOG7GXP9P; -.
DR Reactome; REACT_111045; Developmental Biology.
DR SignaLink; O60271; -.
DR ChiTaRS; SPAG9; human.
DR EvolutionaryTrace; O60271; -.
DR GeneWiki; SPAG9; -.
DR GenomeRNAi; 9043; -.
DR NextBio; 33871; -.
DR PMAP-CutDB; O60271; -.
DR PRO; PR:O60271; -.
DR ArrayExpress; O60271; -.
DR Bgee; O60271; -.
DR Genevestigator; O60271; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0007257; P:activation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; TAS:Reactome.
DR GO; GO:0090074; P:negative regulation of protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 1321 C-Jun-amino-terminal kinase-interacting
FT protein 4.
FT /FTId=PRO_0000234076.
FT COILED 66 166 Potential.
FT COILED 408 534
FT COILED 724 758 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 109 109 Phosphoserine.
FT MOD_RES 183 183 Phosphoserine.
FT MOD_RES 185 185 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 217 217 Phosphothreonine.
FT MOD_RES 251 251 Phosphoserine.
FT MOD_RES 265 265 Phosphoserine.
FT MOD_RES 268 268 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 311 311 Phosphoserine.
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 348 348 Phosphothreonine.
FT MOD_RES 365 365 Phosphothreonine (By similarity).
FT MOD_RES 418 418 Phosphothreonine.
FT MOD_RES 586 586 Phosphothreonine.
FT MOD_RES 730 730 Phosphoserine.
FT MOD_RES 733 733 Phosphoserine.
FT VAR_SEQ 1 196 MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGR
FT YDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDN
FT EQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVES
FT LESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHT
FT EMIHNYMEHLERTKLHQLSGSDQLESTAHSRI -> MSPGC
FT MLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALT
FT QNLPRIL (in isoform 6).
FT /FTId=VSP_042253.
FT VAR_SEQ 248 261 Missing (in isoform 2, isoform 4, isoform
FT 5 and isoform 6).
FT /FTId=VSP_018214.
FT VAR_SEQ 555 555 F -> FVPTR (in isoform 2).
FT /FTId=VSP_018220.
FT VAR_SEQ 938 945 SNDSDAYK -> RYNNGSST (in isoform 3 and
FT isoform 5).
FT /FTId=VSP_018221.
FT VAR_SEQ 946 1321 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_018222.
FT VAR_SEQ 1175 1175 T -> TVILHQGRLLGLRA (in isoform 6).
FT /FTId=VSP_042254.
FT VARIANT 1320 1320 N -> S (in dbSNP:rs9896965).
FT /FTId=VAR_059364.
FT CONFLICT 451 451 E -> G (in Ref. 9; AAO66462).
FT CONFLICT 680 680 E -> K (in Ref. 8; CAA62987 and 9;
FT AAO66462).
FT HELIX 406 465
SQ SEQUENCE 1321 AA; 146205 MW; 5CAE349FBDF91B40 CRC64;
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
QLSGSDQLES TAHSRIRKER PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP
RSHTSLKVSN SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE LDMDKDLSGY
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
LETKNALNIV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEEKNRELE EELRKARAEA
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
NPAMQEKKRS SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVTNG
QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDVAGLD
TEGSKQRSAS QSSLDKLDQE LKEQQKELKN QEELSSLVWI CTSTHSATKV LIIDAVQPGN
ILDSFTVCNS HVLCIASVPG ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG
GITVVGCSAE GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV LPNEQDLVRE
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG DKAGPSAQEP
GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMYGN
E
//
MIM
605430
*RECORD*
*FIELD* NO
605430
*FIELD* TI
*605430 SPERM-ASSOCIATED ANTIGEN 9; SPAG9
;;SUNDAY DRIVER, DROSOPHILA, HOMOLOG OF, 1; SYD1;;
read morePROTEIN HIGHLY EXPRESSED IN TESTIS; PHET;;
KIAA0516
*FIELD* TX
CLONING
Shankar et al. (1998) cloned SPAG9 from a human testis cDNA library
using antibodies against sperm proteins showing surface localization as
probe. The deduced 766-amino acid protein has a calculated molecular
mass of 84 kD and contains a large N-terminal extracellular domain, a
short transmembrane helical domain, and a cytoplasmic domain. There are
6 putative N-glycosylation sites, several putative phosphorylation sites
for cAMP/cGMP-dependent protein kinase, protein kinase C, and casein
kinase II, and 10 putative myristoylation sites. There is also a leucine
zipper motif, with 6 leucine repeats, that may aid in dimerization since
there is no upstream basic domain characteristic of DNA binding
proteins. Northern blot analysis detected testis-restricted expression
of a 3-kb SPAG9 transcript. In situ hybridization of human testis
sections revealed SPAG9 on round spermatids of stages I, II, and III of
the human seminiferous cycle. Immunohistochemical staining showed that
SPAG9 is exclusively associated with elongated spermatids and not with
round spermatids, indicating posttranscriptional delay in expression.
Analysis of the cDNA revealed 3 putative hairpin loop structures at key
positions within the open reading frame that could stabilize the mRNA in
vivo.
Bowman et al. (2000) identified a broadly conserved membrane-associated
protein, which they termed 'sunday driver' (syd), required for the
functional interaction of kinesin I (see 148760) with axonal cargo in
Drosophila. Mutations in syd and the axonal transport motor kinesin I
were found to cause similar phenotypes in Drosophila, including aberrant
accumulations of axonal cargoes. By searching genomic and EST sequence
databases for proteins similar to syd, Bowman et al. (2000) obtained
full-length cDNAs encoding human SYD1 and mouse Syd2, as well as partial
cDNAs encoding human SYD2 (605431) and mouse Syd1. Human SYD1 is 69%
similar to mouse Syd2 and 55% similar to Drosophila syd. The predicted
SYD proteins have a transmembrane region flanked by an N-terminal domain
containing 2 coiled-coil regions and a C-terminal domain containing a
conserved hydrophobic core. GFP-tagged mouse Syd2 localized to
tubulovesicular structures that costained for kinesin I and a marker of
the secretory pathway.
By immunoscreening a liver cell line cDNA library with systemic
sclerosis (see 181750) serum, Yasuoka et al. (2003) identified a partial
cDNA encoding PHET. RT-PCR detected PHET expression in testis only.
Serum autoantibodies to a recombinant PHET fragment were detected in 8%
of systemic sclerosis patients, but were not present in systemic lupus
erythematosus (SLE; 152700) patients or healthy controls. In systemic
sclerosis patients, anti-PHET autoantibodies were associated with
diffuse cutaneous or lung disease. RT-PCR analysis detected increased
PHET expression in systemic sclerosis patient fibroblasts compared with
controls. Immunofluorescence microscopy demonstrated more intense
cytoplasmic staining for PHET in patient fibroblasts. Yasuoka et al.
(2003) concluded that PHET is a testicular antigenic variant of SPAG9
that is overexpressed in systemic sclerosis patient dermal fibroblasts.
GENE FUNCTION
By coimmunoprecipitation analysis, Bowman et al. (2000) found that Syd2
forms a complex with kinesin I in vivo. Yeast 2-hybrid analysis and in
vitro interaction studies revealed that Syd2 directly binds kinesin I
via the tetratricopeptide repeat (TPR) domain of kinesin light chain
(KLC; 600025). The authors proposed that the SYD proteins mediate the
axonal transport of at least 1 class of vesicles by interacting directly
with KLC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SPAG9
gene to chromosome 17 (TMAP WI-9550). Scott (2002) refined the
localization to 17q21.33 based on sequence similarity between the SPAG9
sequence (GenBank GENBANK NM003971) and a chromosome 17 clone (GenBank
GENBANK AC005920).
*FIELD* RF
1. Bowman, A. B.; Kamal, A.; Ritchings, B. W.; Philp, A. V.; McGrail,
M.; Gindhart, J. G.; Goldstein, L. S. B.: Kinesin-dependent axonal
transport is mediated by the sunday driver (SYD) protein. Cell 103:
583-594, 2000.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 2002.
3. Shankar, S.; Mohapatra, B.; Suri, A.: Cloning of a novel human
testis mRNA specifically expressed in testicular haploid germ cells,
having unique palindromic sequences and encoding a leucine zipper
dimerization motif. Biochem. Biophys. Res. Commun. 243: 561-565,
1998.
4. Yasuoka, H.; Ihn, H.; Medsger, T. A., Jr.; Hirakata, M.; Kawakami,
Y.; Ikeda, Y.; Kuwana, M.: A novel protein highly expressed in testis
is overexpressed in systemic sclerosis fibroblasts and targeted by
autoantibodies. J. Immun. 171: 6883-6890, 2003.
*FIELD* CN
Paul J. Converse - updated: 5/5/2006
Patricia A. Hartz - updated: 4/17/2002
*FIELD* CD
Stylianos E. Antonarakis: 11/28/2000
*FIELD* ED
mgross: 05/08/2006
mgross: 5/8/2006
terry: 5/5/2006
carol: 4/17/2002
mgross: 3/14/2001
mgross: 11/28/2000
*RECORD*
*FIELD* NO
605430
*FIELD* TI
*605430 SPERM-ASSOCIATED ANTIGEN 9; SPAG9
;;SUNDAY DRIVER, DROSOPHILA, HOMOLOG OF, 1; SYD1;;
read morePROTEIN HIGHLY EXPRESSED IN TESTIS; PHET;;
KIAA0516
*FIELD* TX
CLONING
Shankar et al. (1998) cloned SPAG9 from a human testis cDNA library
using antibodies against sperm proteins showing surface localization as
probe. The deduced 766-amino acid protein has a calculated molecular
mass of 84 kD and contains a large N-terminal extracellular domain, a
short transmembrane helical domain, and a cytoplasmic domain. There are
6 putative N-glycosylation sites, several putative phosphorylation sites
for cAMP/cGMP-dependent protein kinase, protein kinase C, and casein
kinase II, and 10 putative myristoylation sites. There is also a leucine
zipper motif, with 6 leucine repeats, that may aid in dimerization since
there is no upstream basic domain characteristic of DNA binding
proteins. Northern blot analysis detected testis-restricted expression
of a 3-kb SPAG9 transcript. In situ hybridization of human testis
sections revealed SPAG9 on round spermatids of stages I, II, and III of
the human seminiferous cycle. Immunohistochemical staining showed that
SPAG9 is exclusively associated with elongated spermatids and not with
round spermatids, indicating posttranscriptional delay in expression.
Analysis of the cDNA revealed 3 putative hairpin loop structures at key
positions within the open reading frame that could stabilize the mRNA in
vivo.
Bowman et al. (2000) identified a broadly conserved membrane-associated
protein, which they termed 'sunday driver' (syd), required for the
functional interaction of kinesin I (see 148760) with axonal cargo in
Drosophila. Mutations in syd and the axonal transport motor kinesin I
were found to cause similar phenotypes in Drosophila, including aberrant
accumulations of axonal cargoes. By searching genomic and EST sequence
databases for proteins similar to syd, Bowman et al. (2000) obtained
full-length cDNAs encoding human SYD1 and mouse Syd2, as well as partial
cDNAs encoding human SYD2 (605431) and mouse Syd1. Human SYD1 is 69%
similar to mouse Syd2 and 55% similar to Drosophila syd. The predicted
SYD proteins have a transmembrane region flanked by an N-terminal domain
containing 2 coiled-coil regions and a C-terminal domain containing a
conserved hydrophobic core. GFP-tagged mouse Syd2 localized to
tubulovesicular structures that costained for kinesin I and a marker of
the secretory pathway.
By immunoscreening a liver cell line cDNA library with systemic
sclerosis (see 181750) serum, Yasuoka et al. (2003) identified a partial
cDNA encoding PHET. RT-PCR detected PHET expression in testis only.
Serum autoantibodies to a recombinant PHET fragment were detected in 8%
of systemic sclerosis patients, but were not present in systemic lupus
erythematosus (SLE; 152700) patients or healthy controls. In systemic
sclerosis patients, anti-PHET autoantibodies were associated with
diffuse cutaneous or lung disease. RT-PCR analysis detected increased
PHET expression in systemic sclerosis patient fibroblasts compared with
controls. Immunofluorescence microscopy demonstrated more intense
cytoplasmic staining for PHET in patient fibroblasts. Yasuoka et al.
(2003) concluded that PHET is a testicular antigenic variant of SPAG9
that is overexpressed in systemic sclerosis patient dermal fibroblasts.
GENE FUNCTION
By coimmunoprecipitation analysis, Bowman et al. (2000) found that Syd2
forms a complex with kinesin I in vivo. Yeast 2-hybrid analysis and in
vitro interaction studies revealed that Syd2 directly binds kinesin I
via the tetratricopeptide repeat (TPR) domain of kinesin light chain
(KLC; 600025). The authors proposed that the SYD proteins mediate the
axonal transport of at least 1 class of vesicles by interacting directly
with KLC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SPAG9
gene to chromosome 17 (TMAP WI-9550). Scott (2002) refined the
localization to 17q21.33 based on sequence similarity between the SPAG9
sequence (GenBank GENBANK NM003971) and a chromosome 17 clone (GenBank
GENBANK AC005920).
*FIELD* RF
1. Bowman, A. B.; Kamal, A.; Ritchings, B. W.; Philp, A. V.; McGrail,
M.; Gindhart, J. G.; Goldstein, L. S. B.: Kinesin-dependent axonal
transport is mediated by the sunday driver (SYD) protein. Cell 103:
583-594, 2000.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 2002.
3. Shankar, S.; Mohapatra, B.; Suri, A.: Cloning of a novel human
testis mRNA specifically expressed in testicular haploid germ cells,
having unique palindromic sequences and encoding a leucine zipper
dimerization motif. Biochem. Biophys. Res. Commun. 243: 561-565,
1998.
4. Yasuoka, H.; Ihn, H.; Medsger, T. A., Jr.; Hirakata, M.; Kawakami,
Y.; Ikeda, Y.; Kuwana, M.: A novel protein highly expressed in testis
is overexpressed in systemic sclerosis fibroblasts and targeted by
autoantibodies. J. Immun. 171: 6883-6890, 2003.
*FIELD* CN
Paul J. Converse - updated: 5/5/2006
Patricia A. Hartz - updated: 4/17/2002
*FIELD* CD
Stylianos E. Antonarakis: 11/28/2000
*FIELD* ED
mgross: 05/08/2006
mgross: 5/8/2006
terry: 5/5/2006
carol: 4/17/2002
mgross: 3/14/2001
mgross: 11/28/2000