POGZ_MOUSE
ID POGZ_MOUSE Reviewed; 1409 AA.
AC Q8BZH4; Q4VA94; Q80TZ8; Q8C0K1; Q8K294;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Pogo transposable element with ZNF domain;
GN Name=Pogz; Synonyms=Kiaa0461;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mammary tumor, and Mesenchymal stem cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 557-1409.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in mitotic cell cycle progression and is
CC involved in kinetochore assembly and mitotic sister chromatid cohesion.
CC Probably through its association with CBX5 plays a role in mitotic
CC chromosome segregation by regulating aurora kinase B/AURKB activation
CC and AURKB and CBX5 dissociation from chromosome arms (By similarity).
CC Promotes the repair of DNA double-strand breaks through the homologous
CC recombination pathway (By similarity). {ECO:0000250|UniProtKB:Q7Z3K3}.
CC -!- SUBUNIT: Interacts with CBX1, CBX3, MAD2L2 and CHAMP1. Interacts with
CC CBX5; POGZ competes with PXVXL motif-containing proteins such as INCENP
CC and TRIM28 for interaction with CBX5 (By similarity). Interacts (via
CC IBM motif) with PSIP1 (via IBD domain); phosphorylation increases its
CC affinity for PSIP1 (By similarity). Interacts with HDGFL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z3K3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
CC Chromosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to
CC trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q7Z3K3}.
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DR EMBL; AK030880; BAC27169.1; -; mRNA.
DR EMBL; AK035255; BAC29003.1; -; mRNA.
DR EMBL; BC032176; AAH32176.1; -; mRNA.
DR EMBL; BC096492; AAH96492.1; -; mRNA.
DR EMBL; AK122288; BAC65570.1; -; mRNA.
DR CCDS; CCDS17596.1; -.
DR RefSeq; NP_766271.2; NM_172683.3.
DR RefSeq; XP_011238392.1; XM_011240090.2.
DR AlphaFoldDB; Q8BZH4; -.
DR BMRB; Q8BZH4; -.
DR BioGRID; 230865; 9.
DR IntAct; Q8BZH4; 1.
DR STRING; 10090.ENSMUSP00000102891; -.
DR iPTMnet; Q8BZH4; -.
DR PhosphoSitePlus; Q8BZH4; -.
DR EPD; Q8BZH4; -.
DR jPOST; Q8BZH4; -.
DR MaxQB; Q8BZH4; -.
DR PaxDb; Q8BZH4; -.
DR PRIDE; Q8BZH4; -.
DR ProteomicsDB; 289360; -.
DR Antibodypedia; 1872; 152 antibodies from 28 providers.
DR DNASU; 229584; -.
DR Ensembl; ENSMUST00000107270; ENSMUSP00000102891; ENSMUSG00000038902.
DR GeneID; 229584; -.
DR KEGG; mmu:229584; -.
DR UCSC; uc008qhc.2; mouse.
DR CTD; 23126; -.
DR MGI; MGI:2442117; Pogz.
DR VEuPathDB; HostDB:ENSMUSG00000038902; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG3105; Eukaryota.
DR GeneTree; ENSGT00940000160649; -.
DR InParanoid; Q8BZH4; -.
DR OMA; QIMQNAN; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q8BZH4; -.
DR TreeFam; TF331707; -.
DR BioGRID-ORCS; 229584; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Pogz; mouse.
DR PRO; PR:Q8BZH4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BZH4; protein.
DR Bgee; ENSMUSG00000038902; Expressed in embryonic post-anal tail and 229 other tissues.
DR ExpressionAtlas; Q8BZH4; baseline and differential.
DR Genevisible; Q8BZH4; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR SMART; SM00674; CENPB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51253; HTH_CENPB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1409
FT /note="Pogo transposable element with ZNF domain"
FT /id="PRO_0000047225"
FT DOMAIN 1011..1081
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT DOMAIN 1113..1319
FT /note="DDE-1"
FT /evidence="ECO:0000255"
FT ZN_FING 372..394
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 491..513
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 527..550
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 557..580
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 587..610
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 616..638
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 644..667
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 767..790
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 811..836
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 238..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..846
FT /note="Required for interaction with CBX5"
FT /evidence="ECO:0000250"
FT REGION 904..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1336..1364
FT /evidence="ECO:0000255"
FT MOTIF 1379..1403
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT COMPBIAS 238..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1393
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 674
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT CONFLICT 513..515
FT /note="HVE -> TRP (in Ref. 2; AAH32176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="Q -> E (in Ref. 1; BAC29003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1409 AA; 154910 MW; ED08A5E2C1E719A5 CRC64;
MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT SVSVSQQPVS APVPIAAHAS
VAGHLSTSTT VSNSGAQNSD STKKTLVTLI ANNNAGNTLV QQGGQPLILT QNPAPGLGTM
VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ
TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST
VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AGQPPGQSNQ TSNPKLAPSF PSPPAVSIAS
FVTVKRPGVT GENSNEVAKL VNTLNTVPSL GQSPGPVVVS NNSSAQRTSG PESSVKVTSS
IPVFDLQDGG RKICPRCNAQ FRVTEALRGH MCYCCPEMVE YQKKGKSLDA EPSVPSAAKP
SSPEKTAPVT STPSSTPIPA LSPPTKVPEP NENAGDAVQT KLIMLVDDFY YGRDGGKAAQ
LTSFPKVATS FRCPHCTKRL KNNIRFMNHM KHHVELDQQN GEVDGHTICQ HCYRQFSTPF
QLQCHLENVH SPYESTTKCK ICEWAFESEP LFLQHMKDTH KPGEMPYVCQ VCQYRSSLYS
EVDVHFRMIH EDTRHLLCPY CLKVFKNGNA FQQHYMRHQK RNVYHCNKCR LQFLFAKDKI
EHKLQHHKTF RKPKQLEGLK PGTKVTIRAS RGQPRTVPVS SNDAPSGTLQ EAAALTSTDP
LPVFLYPPVQ RNIQKRAVRK MSVMGRQTCL ECSFEIPDFP NHFPTYVHCS LCRYSTCCSR
AYANHMINNH VPRKSPKYLA LFKNSVSGIK LACTSCTFAT SVGDAMAKHL VFNPSHRSSN
ILPRGLSWMS HLRPGQASER VFDWSMKNTY LPPPLVPNKA ATVKPVGVTP AEPQELAGPV
LQALPSPAST ATPPATPTHP QPSALPPSAT EGTECLNVSE QEEGSPVTQD PEPASGGGGG
SGVGKKEQLS VKKLRVVLFA LCCNTEQAAE HFRNPQRRIR RWLRRFQASQ GENLEGKYLS
FEAEEKLAEW VLIQREQQLP VNEETLFQKA TKIGRSLEGG FKISYEWAVR FMLRHHLTPH
ARRAVAHTLP KHVAENAGLF IEFVQRQIHN QDLPLSMIVA IDEISLFLDT EVLSSDDRKE
NALQTVGTGE PWCDVVLAIL ADGTVLPTLV FFRGQANRFA NVPDSILLEA KDSGYSDDEI
MELWSTRVWK KHTACQHSKS MLVMDCHRTH LSEEVLALLS ASSTLPAVVP AGCSSKIQPL
DVCIKRTVKN FLHKKWKEQA REMADAACDS DVLLQLVLVW LGEVLGVIGD SPELVQRSFL
VASVLPGPDG NVNSPTRNAD MQEELIASLE EQLKLNGEQS EEHSASAPRP RSSPEETVEP
ESLHQLFEGE SETESFYGFE EADLDLMEI
