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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)

 JIP4_HUMAN              Reviewed;        1321 AA.
O60271; A6H8U5; A8MSX0; B4DHH2; O60905; Q3KQU8; Q3MKM7; Q86WC7;
Q86WC8; Q8IZX7; Q96II0; Q9H811;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 4.
13-NOV-2019, entry version 169.
RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
Short=JIP-4;
Short=JNK-interacting protein 4;
AltName: Full=Cancer/testis antigen 89;
Short=CT89;
AltName: Full=Human lung cancer oncogene 6 protein;
Short=HLC-6;
AltName: Full=JNK-associated leucine-zipper protein;
Short=JLP;
AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
AltName: Full=Proliferation-inducing protein 6;
AltName: Full=Protein highly expressed in testis;
Short=PHET;
AltName: Full=Sperm surface protein;
AltName: Full=Sperm-associated antigen 9;
AltName: Full=Sperm-specific protein;
AltName: Full=Sunday driver 1;
Name=SPAG9; Synonyms=HSS, KIAA0516, MAPK8IP4, SYD1; ORFNames=HLC6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
Wells J.W., Banham A.H., Mufti G.J.;
"Humoral detection of leukaemia-associated antigens in presentation
acute myeloid leukaemia.";
Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
TISSUE=Brain, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORMS 2/4/5).
TISSUE=Eye, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), AND TISSUE
SPECIFICITY.
TISSUE=Testis;
PubMed=9480848; DOI=10.1006/bbrc.1997.7943;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
TISSUE=Testis;
PubMed=14662895; DOI=10.4049/jimmunol.171.12.6883;
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. Immunol. 171:6883-6890(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[11]
FUNCTION, AND INTERACTION WITH NFKB1.
PubMed=14743216; DOI=10.1038/ncb1086;
Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S.,
Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J.,
Schwab M., Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C.,
Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B.,
Superti-Furga G.;
"A physical and functional map of the human TNF-alpha/NF-kappa B
signal transduction pathway.";
Nat. Cell Biol. 6:97-105(2004).
[12]
FUNCTION (ISOFORM 5), INTERACTION WITH MAPK9; MAPK10 AND MAPK8
(ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5), AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=15693750; DOI=10.1042/bj20041577;
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S.,
Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.;
"Characterization of a novel human sperm-associated antigen 9 (SPAG9)
having structural homology with c-Jun N-terminal kinase-interacting
protein.";
Biochem. J. 389:73-82(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-272
AND THR-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; THR-217;
SER-311; SER-329; SER-332; THR-418; THR-586 AND SER-733, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217 AND
SER-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-194; SER-203;
THR-217; SER-251; SER-265; SER-268; SER-272; SER-329; SER-332;
SER-347; THR-348; THR-418; SER-730 AND SER-733, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; SER-329
AND SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-183; SER-185;
SER-203; THR-217; SER-238; SER-265; SER-311; THR-586; SER-588;
THR-595; SER-705; SER-728; SER-730; SER-733; SER-1188 AND THR-1264,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-203; THR-217;
SER-251; SER-588; SER-732 AND SER-733, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
FUNCTION, INTERACTION WITH PIP4P1, AND SUBCELLULAR LOCATION.
PubMed=29146937; DOI=10.1038/s41467-017-01871-z;
Willett R., Martina J.A., Zewe J.P., Wills R., Hammond G.R.V.,
Puertollano R.;
"TFEB regulates lysosomal positioning by modulating TMEM55B expression
and JIP4 recruitment to lysosomes.";
Nat. Commun. 8:1580-1580(2017).
[26]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH
ARF6, COILED COIL, SUBUNIT, AND INTERACTION WITH ARF6.
PubMed=19644450; DOI=10.1038/emboj.2009.209;
Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
"The structural basis of Arf effector specificity: the crystal
structure of ARF6 in a complex with JIP4.";
EMBO J. 28:2835-2845(2009).
-!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
proteins selectively mediates JNK signaling by aggregating
specific components of the MAPK cascade to form a functional JNK
signaling module (PubMed:14743216). Isoform 5 may play a role in
spermatozoa-egg-interaction (PubMed:15693750). Regulates lysosomal
positioning by acting as an adapter protein which links PIP4P1-
positive lysosomes to the dynein-dynactin complex
(PubMed:29146937). {ECO:0000269|PubMed:14743216,
ECO:0000269|PubMed:15693750, ECO:0000269|PubMed:29146937}.
-!- SUBUNIT: Homodimer (PubMed:19644450). The homodimer interacts with
ARF6, forming a heterotetramer (PubMed:19644450). Homooligomer
(PubMed:19644450). Interacts with MAX, MAPK14, MAP3K3, MYC, KNS2
and MAP2K4 (By similarity). Interaction with KNS2 is important in
the formation of ternary complex with MAPK8 (By similarity).
Interacts with NFKB1 (PubMed:14743216). Isoform 5 interacts with
MAPK8, MAPK9, MAPK10 (PubMed:15693750). Interacts with PIP4P1
(PubMed:29146937). {ECO:0000250|UniProtKB:Q58A65,
ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15693750,
ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:29146937}.
-!- INTERACTION:
P84077:ARF1; NbExp=3; IntAct=EBI-1023301, EBI-447171;
P62330:ARF6; NbExp=8; IntAct=EBI-1023301, EBI-638181;
P62331:Arf6 (xeno); NbExp=2; IntAct=EBI-1023301, EBI-988682;
Q96A65:EXOC4; NbExp=3; IntAct=EBI-1023301, EBI-355383;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q58A65}.
Lysosome membrane {ECO:0000269|PubMed:29146937}. Note=Perinuclear
distribution in response to stress signals such as UV radiation.
{ECO:0000250|UniProtKB:Q58A65}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000269|PubMed:15693750}. Note=Associated
with the plasma membrane of the acrosomal compartment and also
localizes in the acrosome matrix. {ECO:0000269|PubMed:15693750}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O60271-1; Sequence=Displayed;
Name=2;
IsoId=O60271-2; Sequence=VSP_018214, VSP_018220;
Name=3;
IsoId=O60271-3; Sequence=VSP_018221, VSP_018222;
Note=Due to intron retention.;
Name=4;
IsoId=O60271-4; Sequence=VSP_018214;
Name=5;
IsoId=O60271-5; Sequence=VSP_018214, VSP_018221, VSP_018222;
Name=6;
IsoId=O60271-9; Sequence=VSP_042253, VSP_018214, VSP_042254;
Note=No experimental confirmation available. Ref.5 (BAG58134)
sequence is in conflict in position: 9:F->S. {ECO:0000305};
-!- TISSUE SPECIFICITY: Isoform 5 is expressed only in testis on the
round spermatids of stage I, II and II. Isoform 5 is absent in
spermatogonia and spermatocyte. Isoform 3 is expressed in testis.
Isoform 4 is expressed in testis and in acute myeloid leukemia
(AML) patients. {ECO:0000269|PubMed:14662895,
ECO:0000269|PubMed:16112646, ECO:0000269|PubMed:9480848}.
-!- INDUCTION: Isoform 3 is increased in systemic sclerosis
fibroblasts. {ECO:0000269|PubMed:14662895}.
-!- PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000250}.
-!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH07524.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAH59946.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAI06049.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
Sequence=AAO66462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAA25442.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=BAB14812.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splicing.; Evidence={ECO:0000305};
Sequence=CAA62987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AF327452; AAN61565.1; -; mRNA.
EMBL; AY850123; AAX47276.1; -; mRNA.
EMBL; AB011088; BAA25442.3; ALT_INIT; mRNA.
EMBL; AK024068; BAB14812.1; ALT_SEQ; mRNA.
EMBL; AK295098; BAG58134.1; -; mRNA.
EMBL; AK302789; BAG63993.1; -; mRNA.
EMBL; AC005920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007524; AAH07524.1; ALT_SEQ; mRNA.
EMBL; BC059946; AAH59946.1; ALT_SEQ; mRNA.
EMBL; BC106048; AAI06049.1; ALT_SEQ; mRNA.
EMBL; BC146755; AAI46756.1; -; mRNA.
EMBL; BC153878; AAI53879.1; -; mRNA.
EMBL; X91879; CAA62987.1; ALT_INIT; mRNA.
EMBL; AY219897; AAO66462.1; ALT_INIT; mRNA.
EMBL; AY219898; AAO66463.1; -; mRNA.
CCDS; CCDS11577.1; -. [O60271-4]
CCDS; CCDS45740.1; -. [O60271-1]
CCDS; CCDS58577.1; -. [O60271-9]
CCDS; CCDS58578.1; -. [O60271-2]
PIR; JC5958; JC5958.
RefSeq; NP_001123999.1; NM_001130527.2. [O60271-2]
RefSeq; NP_001124000.1; NM_001130528.2. [O60271-1]
RefSeq; NP_001238900.1; NM_001251971.1. [O60271-9]
RefSeq; NP_003962.3; NM_003971.5. [O60271-4]
PDB; 2W83; X-ray; 1.93 A; C/D=406-476.
PDBsum; 2W83; -.
SMR; O60271; -.
BioGrid; 114505; 100.
CORUM; O60271; -.
IntAct; O60271; 42.
MINT; O60271; -.
STRING; 9606.ENSP00000262013; -.
iPTMnet; O60271; -.
PhosphoSitePlus; O60271; -.
BioMuta; SPAG9; -.
EPD; O60271; -.
jPOST; O60271; -.
MassIVE; O60271; -.
MaxQB; O60271; -.
PaxDb; O60271; -.
PeptideAtlas; O60271; -.
PRIDE; O60271; -.
ProteomicsDB; 49302; -. [O60271-1]
ProteomicsDB; 49303; -. [O60271-2]
ProteomicsDB; 49304; -. [O60271-3]
ProteomicsDB; 49305; -. [O60271-4]
ProteomicsDB; 49306; -. [O60271-5]
ProteomicsDB; 49307; -. [O60271-9]
DNASU; 9043; -.
Ensembl; ENST00000262013; ENSP00000262013; ENSG00000008294. [O60271-1]
Ensembl; ENST00000357122; ENSP00000349636; ENSG00000008294. [O60271-4]
Ensembl; ENST00000505279; ENSP00000426900; ENSG00000008294. [O60271-2]
Ensembl; ENST00000510283; ENSP00000423165; ENSG00000008294. [O60271-9]
GeneID; 9043; -.
KEGG; hsa:9043; -.
UCSC; uc002ita.4; human. [O60271-1]
CTD; 9043; -.
DisGeNET; 9043; -.
GeneCards; SPAG9; -.
HGNC; HGNC:14524; SPAG9.
HPA; HPA040446; -.
HPA; HPA061458; -.
MIM; 605430; gene.
neXtProt; NX_O60271; -.
OpenTargets; ENSG00000008294; -.
PharmGKB; PA37890; -.
eggNOG; KOG2077; Eukaryota.
eggNOG; ENOG410XQ19; LUCA.
GeneTree; ENSGT00940000153496; -.
HOGENOM; HOG000290716; -.
InParanoid; O60271; -.
KO; K20317; -.
OMA; SFIVCNS; -.
OrthoDB; 324912at2759; -.
PhylomeDB; O60271; -.
TreeFam; TF313096; -.
Reactome; R-HSA-525793; Myogenesis.
SignaLink; O60271; -.
SIGNOR; O60271; -.
ChiTaRS; SPAG9; human.
EvolutionaryTrace; O60271; -.
GeneWiki; SPAG9; -.
GenomeRNAi; 9043; -.
Pharos; O60271; -.
PMAP-CutDB; O60271; -.
PRO; PR:O60271; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000008294; Expressed in 233 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; O60271; baseline and differential.
Genevisible; O60271; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0034451; C:centriolar satellite; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008432; F:JUN kinase binding; IBA:GO_Central.
GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
GO; GO:0005078; F:MAP-kinase scaffold activity; IBA:GO_Central.
GO; GO:0030159; F:receptor signaling complex adaptor activity; IBA:GO_Central.
GO; GO:0007257; P:activation of JUN kinase activity; IBA:GO_Central.
GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR039911; JIP3/JIP4.
InterPro; IPR032486; JIP_LZII.
InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
InterPro; IPR034743; RH1.
InterPro; IPR034744; RH2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR13886; PTHR13886; 1.
Pfam; PF16471; JIP_LZII; 1.
Pfam; PF09744; Jnk-SapK_ap_N; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51776; RH1; 1.
PROSITE; PS51777; RH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Lysosome; Membrane;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 1321 C-Jun-amino-terminal kinase-interacting
protein 4.
/FTId=PRO_0000234076.
DOMAIN 7 95 RH1. {ECO:0000255|PROSITE-
ProRule:PRU01112}.
DOMAIN 500 571 RH2. {ECO:0000255|PROSITE-
ProRule:PRU01113}.
COILED 66 166 {ECO:0000255}.
COILED 408 534 {ECO:0000269|PubMed:19644450}.
COILED 724 758 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 217 217 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231}.
MOD_RES 292 292 Phosphothreonine.
{ECO:0000250|UniProtKB:Q58A65}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 365 365 Phosphothreonine.
{ECO:0000250|UniProtKB:Q58A65}.
MOD_RES 418 418 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 586 586 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 595 595 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1188 1188 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1264 1264 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 196 MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGR
YDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDN
EQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVES
LESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHT
EMIHNYMEHLERTKLHQLSGSDQLESTAHSRI -> MSPGC
MLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALT
QNLPRIL (in isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_042253.
VAR_SEQ 248 261 Missing (in isoform 2, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:12391307,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16112646,
ECO:0000303|PubMed:9480848}.
/FTId=VSP_018214.
VAR_SEQ 555 555 F -> FVPTR (in isoform 2).
{ECO:0000303|PubMed:12391307}.
/FTId=VSP_018220.
VAR_SEQ 938 945 SNDSDAYK -> RYNNGSST (in isoform 3 and
isoform 5). {ECO:0000303|PubMed:14662895,
ECO:0000303|PubMed:9480848}.
/FTId=VSP_018221.
VAR_SEQ 946 1321 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14662895,
ECO:0000303|PubMed:9480848}.
/FTId=VSP_018222.
VAR_SEQ 1175 1175 T -> TVILHQGRLLGLRA (in isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_042254.
VARIANT 1320 1320 N -> S (in dbSNP:rs9896965).
/FTId=VAR_059364.
CONFLICT 451 451 E -> G (in Ref. 9; AAO66462).
{ECO:0000305}.
CONFLICT 680 680 E -> K (in Ref. 8; CAA62987 and 9;
AAO66462). {ECO:0000305}.
HELIX 406 465 {ECO:0000244|PDB:2W83}.
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


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[MAPK8IP2 IB2 JIP2 PRKM8IPL] C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2)
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[Mapk8ip3 Jip3] C-Jun-amino-terminal kinase-interacting protein 3 (JIP-3) (JNK-interacting protein 3) (JNK MAP kinase scaffold protein 3)
[Mapk9 Jnk2 Prkm9] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2)
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAP4K2 GCK RAB8IP] Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (B lymphocyte serine/threonine-protein kinase) (Germinal center kinase) (GC kinase) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein)
[JUN] Transcription factor AP-1 (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39)
[MAEA EMP HLC10 PIG5] E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Cell proliferation-inducing gene 5 protein) (Erythroblast macrophage protein) (Human lung cancer oncogene 10 protein) (HLC-10) (Macrophage erythroblast attacher) (P44EMLP)
[Dab2ip Kiaa1743] Disabled homolog 2-interacting protein (DAB2-interacting protein) (ASK-interacting protein 1) (DOC-2/DAB-2 interactive protein)
[Map4k2 Rab8ip] Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (Germinal center kinase) (GCK) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein)
[Mapk10 Jnk3 Prkm10 Serk2] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)
[BRDT] Bromodomain testis-specific protein (Cancer/testis antigen 9) (CT9) (RING3-like protein)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Mapk9 Jnk2 Prkm9] Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (SAPK-alpha) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) (p54-alpha)
[AKAP13 BRX HT31 LBC] A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)
[KDM5B JARID1B PLU1 RBBP2H1] Lysine-specific demethylase 5B (EC 1.14.11.-) (Cancer/testis antigen 31) (CT31) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) (Retinoblastoma-binding protein 2 homolog 1) (RBP2-H1)
[Fas Apt1 Tnfrsf6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)

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