PRR11_HUMAN
ID PRR11_HUMAN Reviewed; 360 AA.
AC Q96HE9; Q9NUZ7; Q9NXE9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Proline-rich protein 11;
GN Name=PRR11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; SER-344; THR-346 AND
RP THR-348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND THR-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP TISSUE SPECIFICITY, INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23246489; DOI=10.1016/j.biocel.2012.12.002;
RA Ji Y., Xie M., Lan H., Zhang Y., Long Y., Weng H., Li D., Cai W., Zhu H.,
RA Niu Y., Yang Z., Zhang C., Song F., Bu Y.;
RT "PRR11 is a novel gene implicated in cell cycle progression and lung
RT cancer.";
RL Int. J. Biochem. Cell Biol. 45:645-656(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-40; THR-287 AND
RP SER-291, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP SUBCELLULAR LOCATION, CELL CYCLE REGULATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=23242552; DOI=10.1074/mcp.m112.024547;
RA Larance M., Ahmad Y., Kirkwood K.J., Ly T., Lamond A.I.;
RT "Global subcellular characterisation of protein degradation using
RT quantitative proteomics.";
RL Mol. Cell. Proteomics 12:638-650(2013).
CC -!- FUNCTION: Plays a critical role in cell cycle progression.
CC {ECO:0000269|PubMed:23246489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242552,
CC ECO:0000269|PubMed:23246489}. Nucleus {ECO:0000269|PubMed:23246489}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:23246489}.
CC -!- INDUCTION: Expression increases from G1 to G2/M phase.
CC {ECO:0000269|PubMed:23242552, ECO:0000269|PubMed:23246489}.
CC -!- PTM: Ubiquitinated (Probable). Rapidly degraded by the proteasome;
CC degradation may involve FBXW7-specific phosphorylated phosphodegron
CC motifs. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91064.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000296; BAA91064.1; ALT_INIT; mRNA.
DR EMBL; AK001891; BAA91964.1; -; mRNA.
DR EMBL; BC008669; AAH08669.1; -; mRNA.
DR CCDS; CCDS11614.1; -.
DR RefSeq; NP_060774.2; NM_018304.3.
DR AlphaFoldDB; Q96HE9; -.
DR SMR; Q96HE9; -.
DR BioGRID; 120888; 128.
DR IntAct; Q96HE9; 64.
DR STRING; 9606.ENSP00000262293; -.
DR iPTMnet; Q96HE9; -.
DR PhosphoSitePlus; Q96HE9; -.
DR BioMuta; PRR11; -.
DR DMDM; 74731920; -.
DR EPD; Q96HE9; -.
DR jPOST; Q96HE9; -.
DR MassIVE; Q96HE9; -.
DR MaxQB; Q96HE9; -.
DR PaxDb; Q96HE9; -.
DR PeptideAtlas; Q96HE9; -.
DR PRIDE; Q96HE9; -.
DR ProteomicsDB; 76741; -.
DR Antibodypedia; 18470; 228 antibodies from 18 providers.
DR DNASU; 55771; -.
DR Ensembl; ENST00000262293.9; ENSP00000262293.5; ENSG00000068489.13.
DR Ensembl; ENST00000578542.5; ENSP00000464171.1; ENSG00000068489.13.
DR Ensembl; ENST00000580177.5; ENSP00000463733.1; ENSG00000068489.13.
DR Ensembl; ENST00000614081.1; ENSP00000481852.1; ENSG00000068489.13.
DR GeneID; 55771; -.
DR KEGG; hsa:55771; -.
DR MANE-Select; ENST00000262293.9; ENSP00000262293.5; NM_018304.4; NP_060774.2.
DR UCSC; uc002ixf.3; human.
DR CTD; 55771; -.
DR DisGeNET; 55771; -.
DR GeneCards; PRR11; -.
DR HGNC; HGNC:25619; PRR11.
DR HPA; ENSG00000068489; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 615920; gene.
DR neXtProt; NX_Q96HE9; -.
DR OpenTargets; ENSG00000068489; -.
DR PharmGKB; PA142671131; -.
DR VEuPathDB; HostDB:ENSG00000068489; -.
DR eggNOG; ENOG502RZVF; Eukaryota.
DR GeneTree; ENSGT00510000046704; -.
DR HOGENOM; CLU_055832_0_0_1; -.
DR InParanoid; Q96HE9; -.
DR OMA; PMHITVK; -.
DR OrthoDB; 1169838at2759; -.
DR PhylomeDB; Q96HE9; -.
DR TreeFam; TF333428; -.
DR PathwayCommons; Q96HE9; -.
DR SignaLink; Q96HE9; -.
DR BioGRID-ORCS; 55771; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; PRR11; human.
DR GenomeRNAi; 55771; -.
DR Pharos; Q96HE9; Tbio.
DR PRO; PR:Q96HE9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96HE9; protein.
DR Bgee; ENSG00000068489; Expressed in endothelial cell and 209 other tissues.
DR ExpressionAtlas; Q96HE9; baseline and differential.
DR Genevisible; Q96HE9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..360
FT /note="Proline-rich protein 11"
FT /id="PRO_0000243943"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 285..291
FT /note="Phosphodegron"
FT MOTIF 296..304
FT /note="D-box"
FT MOTIF 316..318
FT /note="KEN box"
FT MOTIF 325..330
FT /note="Phosphodegron"
FT COMPBIAS 178..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT 307
FT /note="S -> R (in Ref. 1; BAA91964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40085 MW; 04757432CA0D9501 CRC64;
MPKFKQRRRK LKAKAERLFK KKEASHFQSK LITPPPPPPS PERVGISSID ISQSRSWLTS
SWNFNFPNIR DAIKLWTNRV WSIYSWCQNC ITQSLEVLKD TIFPSRICHR ELYSVKQQFC
ILESKLCKLQ EALKTISESS SCPSCGQTCH MSGKLTNVPA CVLITPGDSK AVLPPTLPQP
ASHFPPPPPP PPLPPPPPPL APVLLRKPSL AKALQAGPLK KDGPMQITVK DLLTVKLKKT
QSLDEKRKLI PSPKARNPLV TVSDLQHVTL KPNSKVLSTR VTNVLITPGK SQMDLRKLLR
KVDVERSPGG TPLTNKENME TGTGLTPVMT QALRRKFQLA HPRSPTPTLP LSTSSFDEQN
