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Unconventional prefoldin RPB5 interactor 1 (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein)

 RMP_HUMAN               Reviewed;         535 AA.
O94763; A8K805; H7BY42; Q8TC23; Q9UNU3;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
10-OCT-2018, entry version 153.
RecName: Full=Unconventional prefoldin RPB5 interactor 1;
AltName: Full=Protein NNX3;
AltName: Full=Protein phosphatase 1 regulatory subunit 19;
AltName: Full=RNA polymerase II subunit 5-mediating protein;
Short=RPB5-mediating protein;
Name=URI1; Synonyms=C19orf2, NNX3, PPP1R19, RMP, URI;
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), PHOSPHORYLATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9878255; DOI=10.1006/geno.1998.5609;
Van Leuven F., Torrekens S., Moechars D., Hilliker C., Buellens M.,
Bollen M., Delabie J.;
"Molecular cloning of a gene on chromosome 19q12 coding for a novel
intracellular protein: analysis of expression in human and mouse
tissues and in human tumor cells, particularly Reed-Sternberg cells in
Hodgkin disease.";
Genomics 54:511-520(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2E, AND
TISSUE SPECIFICITY.
TISSUE=Hepatoma;
PubMed=9819440; DOI=10.1128/MCB.18.12.7546;
Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N.,
Murakami S.;
"RMP, a novel RNA polymerase II subunit 5-interacting protein,
counteracts transactivation by hepatitis B virus X protein.";
Mol. Cell. Biol. 18:7546-7555(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Testis;
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).
[6]
FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH GTF2F1
AND GTF2F2.
PubMed=12737519; DOI=10.1038/sj.cr.7290155;
Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y.,
Murakami S.;
"Interaction with general transcription factor IIF (TFIIF) is required
for the suppression of activated transcription by RPB5-mediating
protein (RMP).";
Cell Res. 13:111-120(2003).
[7]
FUNCTION, AND IDENTIFICATION IN THE URI COMPLEX.
PubMed=14615539; DOI=10.1126/science.1088401;
Gstaiger M., Luke B., Hess D., Oakeley E.J., Wirbelauer C.,
Blondel M., Vigneron M., Peter M., Krek W.;
"Control of nutrient-sensitive transcription programs by the
unconventional prefoldin URI.";
Science 302:1208-1212(2003).
[8]
FUNCTION, INTERACTION WITH DMAP1, AND SUBCELLULAR LOCATION.
PubMed=15367675; DOI=10.1128/MCB.24.19.8556-8566.2004;
Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T.,
Murakami S.;
"Subcellular localization of RPB5-mediating protein and its putative
functional partner.";
Mol. Cell. Biol. 24:8556-8566(2004).
[9]
FUNCTION IN DEPHOSPHORYLATION OF PPP1CC, PHOSPHORYLATION AT SER-372 BY
RPS6KB1, MUTAGENESIS OF SER-372, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
Aebersold R., Hess D., Krek W.;
"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
activates a negative feedback program that counters S6K1 survival
signaling.";
Mol. Cell 28:28-40(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, 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).
[11]
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).
[12]
FUNCTION, INTERACTION WITH PPP1CC, PHOSPHORYLATION AT SER-372,
MUTAGENESIS OF SER-372, AND TISSUE SPECIFICITY.
PubMed=21397856; DOI=10.1016/j.ccr.2011.01.019;
Theurillat J.P., Metzler S.C., Henzi N., Djouder N., Helbling M.,
Zimmermann A.K., Jacob F., Soltermann A., Caduff R.,
Heinzelmann-Schwarz V., Moch H., Krek W.;
"URI is an oncogene amplified in ovarian cancer cells and is required
for their survival.";
Cancer Cell 19:317-332(2011).
[13]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH UXT,
PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=21730289; DOI=10.1128/MCB.05429-11;
Mita P., Savas J.N., Djouder N., Yates J.R. III, Ha S., Ruoff R.,
Schafler E.D., Nwachukwu J.C., Tanese N., Cowan N.J., Zavadil J.,
Garabedian M.J., Logan S.K.;
"Regulation of androgen receptor-mediated transcription by RPB5
binding protein URI/RMP.";
Mol. Cell. Biol. 31:3639-3652(2011).
[14]
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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; THR-373 AND
SER-442, 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).
-!- FUNCTION: Involved in gene transcription regulation. Acts as a
transcriptional repressor in concert with the corepressor UXT to
regulate androgen receptor (AR) transcription. May act as a tumor
suppressor to repress AR-mediated gene transcription and to
inhibit anchorage-independent growth in prostate cancer cells.
Required for cell survival in ovarian cancer cells. Together with
UXT, associates with chromatin to the NKX3-1 promoter region.
Antagonizes transcriptional modulation via hepatitis B virus X
protein.
-!- FUNCTION: Plays a central role in maintaining S6K1 signaling and
BAD phosphorylation under normal growth conditions thereby
protecting cells from potential deleterious effects of sustained
S6K1 signaling. The URI1-PPP1CC complex acts as a central
component of a negative feedback mechanism that counteracts
excessive S6K1 survival signaling to BAD in response to growth
factors. Mediates inhibition of PPP1CC phosphatase activity in
mitochondria. Coordinates the regulation of nutrient-sensitive
gene expression availability in a mTOR-dependent manner. Seems to
be a scaffolding protein able to assemble a prefoldin-like complex
that contains PFDs and proteins with roles in transcription and
ubiquitination.
-!- SUBUNIT: Homodimer. Component of the URI complex that contains
PFDN2, POLR2E/RPB5, RUVBL2, RUVBL1 and URI1. Interacts with
PPP1CC; the interaction is phosphorylation-dependent and occurs in
a growth factor-dependent manner. Interacts with PFDN2, PFDN4 and
STAP1; the interactions are phosphorylation-dependent and occur in
a growth-dependent manner in the mitochondrion. Interacts (via the
middle C-terminal region) with GTF2F1 and GTF2F2. Interacts with
DMAP1, POLR2E/RPB5 and UXT. {ECO:0000269|PubMed:12737519,
ECO:0000269|PubMed:14615539, ECO:0000269|PubMed:15367675,
ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
ECO:0000269|PubMed:9819440}.
-!- INTERACTION:
P30561:Ahr (xeno); NbExp=2; IntAct=EBI-357067, EBI-78863;
P19785:Esr1 (xeno); NbExp=2; IntAct=EBI-357067, EBI-346765;
P35269:GTF2F1; NbExp=3; IntAct=EBI-357067, EBI-457886;
P13984:GTF2F2; NbExp=4; IntAct=EBI-357067, EBI-1030560;
O15294:OGT; NbExp=10; IntAct=EBI-357067, EBI-539828;
Q9UHV9:PFDN2; NbExp=2; IntAct=EBI-357067, EBI-359873;
P19388:POLR2E; NbExp=2; IntAct=EBI-357067, EBI-395189;
P36873:PPP1CC; NbExp=17; IntAct=EBI-357067, EBI-356283;
Q9H6T3:RPAP3; NbExp=2; IntAct=EBI-357067, EBI-356928;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cell
projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2,
PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O94763-1; Sequence=Displayed;
Name=2;
IsoId=O94763-2; Sequence=VSP_032773;
Name=3;
IsoId=O94763-3; Sequence=VSP_042259;
Note=No experimental confirmation available.;
Name=4;
IsoId=O94763-4; Sequence=VSP_044769, VSP_044770;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in ovarian cancers (at
protein level). Expressed strongly in skeletal muscle. Expressed
weakly in brain, heart, pancreas and in prostate epithelial cells.
{ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
ECO:0000269|PubMed:9819440, ECO:0000269|PubMed:9878255}.
-!- PTM: Phosphorylated. Phosphorylation occurs essentially on serine
residues. Phosphorylation occurs in response to androgen treatment
in prostate cancer cells in a mTOR-dependent manner.
Phosphorylated; hyperhosphorylated in mitochondria in a mTORC-
dependent signaling pathway. Phosphorylated at Ser-372 by RPS6KB1
in a growth factor- and rapamycin-dependent manner. S6K1-mediated
mitochondrial phosphorylation at Ser-372 disrupts the URI1-PPP1CC
complex in the mitochondrion, relieves PPP1CC phosphatase
inhibition activity and hence engages a negative feedback
diminishing RPS6KB1 kinase activity, preventing sustained S6K1-
dependent signaling. {ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
ECO:0000269|PubMed:9878255}.
-!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
protein family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH26184.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF091095; AAD08679.1; -; mRNA.
EMBL; AB006572; BAA34781.1; -; mRNA.
EMBL; AK292170; BAF84859.1; -; mRNA.
EMBL; AC008507; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC026184; AAH26184.2; ALT_INIT; mRNA.
CCDS; CCDS12420.1; -. [O94763-1]
CCDS; CCDS58658.1; -. [O94763-4]
RefSeq; NP_001239570.1; NM_001252641.1. [O94763-4]
RefSeq; NP_003787.2; NM_003796.3. [O94763-1]
UniGene; Hs.466391; -.
ProteinModelPortal; O94763; -.
SMR; O94763; -.
BioGrid; 114264; 82.
CORUM; O94763; -.
IntAct; O94763; 52.
STRING; 9606.ENSP00000442436; -.
iPTMnet; O94763; -.
PhosphoSitePlus; O94763; -.
SwissPalm; O94763; -.
BioMuta; URI1; -.
EPD; O94763; -.
MaxQB; O94763; -.
PaxDb; O94763; -.
PeptideAtlas; O94763; -.
PRIDE; O94763; -.
ProteomicsDB; 50428; -.
ProteomicsDB; 50429; -. [O94763-2]
ProteomicsDB; 50430; -. [O94763-3]
Ensembl; ENST00000360605; ENSP00000353817; ENSG00000105176. [O94763-4]
Ensembl; ENST00000392271; ENSP00000376097; ENSG00000105176. [O94763-1]
GeneID; 8725; -.
KEGG; hsa:8725; -.
UCSC; uc002nsq.4; human. [O94763-1]
CTD; 8725; -.
DisGeNET; 8725; -.
EuPathDB; HostDB:ENSG00000105176.17; -.
GeneCards; URI1; -.
H-InvDB; HIX0014980; -.
HGNC; HGNC:13236; URI1.
HPA; HPA071709; -.
MIM; 603494; gene.
neXtProt; NX_O94763; -.
OpenTargets; ENSG00000105176; -.
PharmGKB; PA134962614; -.
eggNOG; KOG3130; Eukaryota.
eggNOG; ENOG41101NF; LUCA.
GeneTree; ENSGT00390000002362; -.
HOGENOM; HOG000154150; -.
HOVERGEN; HBG007610; -.
InParanoid; O94763; -.
KO; K17560; -.
OMA; ADFDDRR; -.
OrthoDB; EOG091G0E72; -.
PhylomeDB; O94763; -.
TreeFam; TF332816; -.
ChiTaRS; URI1; human.
GeneWiki; C19orf2; -.
GenomeRNAi; 8725; -.
PRO; PR:O94763; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105176; Expressed in 226 organ(s), highest expression level in adrenal tissue.
CleanEx; HS_C19orf2; -.
ExpressionAtlas; O94763; baseline and differential.
Genevisible; O94763; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0019212; F:phosphatase inhibitor activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.287.370; -; 1.
InterPro; IPR009053; Prefoldin.
InterPro; IPR004127; Prefoldin_subunit_alpha.
Pfam; PF02996; Prefoldin; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell projection; Complete proteome;
Cytoplasm; Mitochondrion; Nucleus; Oncogene; Phosphoprotein;
Polymorphism; Protein phosphatase inhibitor; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 535 Unconventional prefoldin RPB5 interactor
1.
/FTId=PRO_0000097365.
COMPBIAS 299 311 Poly-Asp.
COMPBIAS 314 321 Poly-Asp.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 372 372 Phosphoserine; by RPS6KB1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:21397856}.
MOD_RES 373 373 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 76 Missing (in isoform 2).
{ECO:0000303|PubMed:9878255}.
/FTId=VSP_032773.
VAR_SEQ 1 51 MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVV
TNCQERIQHW -> MRLGNVDFTLGSNVPCVYLVFSVNR
(in isoform 3).
{ECO:0000303|PubMed:9819440}.
/FTId=VSP_042259.
VAR_SEQ 1 39 MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEK
-> MTTWSSLQGSHVSKRALAYAL (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044769.
VAR_SEQ 476 535 AFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEAS
EETGKRVSKFKAARLQQKD -> VLRLVGYSRNLAPLNVIL
(in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044770.
VARIANT 22 22 L -> P (in dbSNP:rs189187).
/FTId=VAR_056978.
MUTAGEN 372 372 S->A: Does not lead to dissociation of
the URI1-PPP1CC complex. Enhances
phosphorylation of RPS6KB1 after IGF1
stimulation. Confers a cell survival
increase. {ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:21397856}.
CONFLICT 7 7 E -> G (in Ref. 3; BAF84859).
{ECO:0000305}.
CONFLICT 232 232 D -> N (in Ref. 5; AAH26184).
{ECO:0000305}.
CONFLICT 311 311 Missing (in Ref. 1; AAD08679, 2;
BAA34781, 3; BAF84859 and 5; AAH26184).
{ECO:0000305}.
CONFLICT 315 315 D -> E (in Ref. 3; BAF84859).
{ECO:0000305}.
CONFLICT 434 434 R -> G (in Ref. 2; BAA34781).
{ECO:0000305}.
SEQUENCE 535 AA; 59832 MW; DBB046A392E3C752 CRC64;
MEAPTVETPP DPSPPSAPAP ALVPLRAPDV ARLREEQEKV VTNCQERIQH WKKVDNDYNA
LRERLSTLPD KLSYNIMVPF GPFAFMPGKL VHTNEVTVLL GDNWFAKCSA KQAVGLVEHR
KEHVRKTIDD LKKVMKNFES RVEFTEDLQK MSDAAGDIVD IREEIKCDFE FKAKHRIAHK
PHSKPKTSDI FEADIANDVK SKDLLADKEL WARLEELERQ EELLGELDSK PDTVIANGED
TTSSEEEKED RNTNVNAMHQ VTDSHTPCHK DVASSEPFSG QVNSQLNCSV NGSSSYHSDD
DDDDDDDDDD DNIDDDDGDN DHEALGVGDN SIPTIYFSHT VEPKRVRINT GKNTTLKFSE
KKEEAKRKRK NSTGSGHSAQ ELPTIRTPAD IYRAFVDVVN GEYVPRKSIL KSRSRENSVC
SDTSESSAAE FDDRRGVLRS ISCEEATCSD TSESILEEEP QENQKKLLPL SVTPEAFSGT
VIEKEFVSPS LTPPPAIAHP ALPTIPERKE VLLEASEETG KRVSKFKAAR LQQKD


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