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Q7Z3K3 (POGZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pogo transposable element with ZNF domain
Alternative name(s):
Suppressor of hairy wing homolog 5
Zinc finger protein 280E
Zinc finger protein 635
Gene names
Name:POGZ
Synonyms:KIAA0461, SUHW5, ZNF280E, ZNF635
ORF Names:Nbla00003
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1410 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. Ref.14

Subunit structure

Interacts with CBX1, CBX3, MAD2L2 and CHAMP1. Interacts with CBX5; POGZ competes with PXVXL motif-containing proteins such as INCENP and TRIM28 for interaction with CBX5. Interacts with PSIP1 isoform 1. Ref.6 Ref.11 Ref.13 Ref.14

Subcellular location

Nucleus. Chromosome. Cytoplasm. Note: According to some authors, it is not localized to mitotic chromatin (Ref.11). Recruited to trimethylated 'Lys-9' of histone H3 (H3K9me3). Ref.11 Ref.13 Ref.14

Sequence similarities

Contains 9 C2H2-type zinc fingers.

Contains 1 DDE domain.

Contains 1 HTH CENPB-type DNA-binding domain.

Sequence caution

The sequence BAE45744.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAI16808.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16810.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z3K3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7Z3K3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     42-94: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7Z3K3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     42-94: Missing.
     593-593: Q → QPYFPSYVTQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q7Z3K3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     360-363: VTSS → GTIT
     364-1410: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q7Z3K3-5)

Also known as: CRA_e;

The sequence of this isoform differs from the canonical sequence as follows:
     96-190: Missing.
Note: Gene prediction based on EST data.
Isoform 6 (identifier: Q7Z3K3-6)

The sequence of this isoform differs from the canonical sequence as follows:
     287-295: Missing.
Isoform 7 (identifier: Q7Z3K3-7)

The sequence of this isoform differs from the canonical sequence as follows:
     42-94: Missing.
     287-295: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14101410Pogo transposable element with ZNF domain
PRO_0000047224

Regions

Domain1015 – 108571HTH CENPB-type
Domain1117 – 1323207DDE
Zinc finger375 – 39723C2H2-type 1; atypical
Zinc finger494 – 51623C2H2-type 2
Zinc finger530 – 55324C2H2-type 3
Zinc finger560 – 58324C2H2-type 4
Zinc finger590 – 61324C2H2-type 5
Zinc finger619 – 64123C2H2-type 6
Zinc finger647 – 67024C2H2-type 7
Zinc finger771 – 79424C2H2-type 8
Zinc finger815 – 84026C2H2-type 9
Region810 – 85041Required for interaction with CBX5
Coiled coil1340 – 136021 Potential
Compositional bias875 – 93157Pro-rich

Amino acid modifications

Modified residue3331Phosphoserine Ref.9
Modified residue4251Phosphoserine Ref.9 Ref.15 Ref.16
Modified residue4391Phosphothreonine Ref.12
Modified residue4451Phosphoserine Ref.12
Modified residue13381Phosphoserine Ref.9

Natural variations

Alternative sequence42 – 9453Missing in isoform 2, isoform 3 and isoform 7.
VSP_010185
Alternative sequence96 – 19095Missing in isoform 5.
VSP_030150
Alternative sequence287 – 2959Missing in isoform 6 and isoform 7.
VSP_046785
Alternative sequence360 – 3634VTSS → GTIT in isoform 4.
VSP_010187
Alternative sequence364 – 14101047Missing in isoform 4.
VSP_010188
Alternative sequence5931Q → QPYFPSYVTQ in isoform 3.
VSP_010186
Natural variant13651E → D.
Corresponds to variant rs35198305 [ dbSNP | Ensembl ].
VAR_031476

Experimental info

Mutagenesis8171C → A: Diminishes interaction with CBX5 and abolishes interaction with CBX1 and CBX5; when associated with A-820; A-833 and A-840. Ref.14
Mutagenesis8201C → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with when associated with A-817; A-833 and A-840. Ref.14
Mutagenesis8331H → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-817; A-820 and A-840. Ref.14
Mutagenesis8401H → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-817; A-820 and A-833. Ref.14
Sequence conflict2131R → G in BAG63781. Ref.2
Sequence conflict3271I → F in BAG62060. Ref.2
Sequence conflict5031L → P in BAB87117. Ref.5
Sequence conflict5031L → P in BAE45744. Ref.5
Sequence conflict7271V → A in BAG63781. Ref.2
Sequence conflict7881N → T in CAB45136. Ref.6
Sequence conflict8881K → E in BAB87117. Ref.5
Sequence conflict8881K → E in BAE45744. Ref.5
Sequence conflict9331A → V in CAD97850. Ref.1
Sequence conflict10261E → G in CAD97850. Ref.1
Sequence conflict10781R → W in BAB87117. Ref.5
Sequence conflict10781R → W in BAE45744. Ref.5
Sequence conflict1092 – 110716TLPKD…LFIDF → PTLLFCLFVFSSPSTL in BAB87117. Ref.5
Sequence conflict1092 – 110716TLPKD…LFIDF → PTLLFCLFVFSSPSTL in BAE45744. Ref.5
Sequence conflict12481T → A in BAG63781. Ref.2
Sequence conflict13041W → R in CAD97850. Ref.1

Secondary structure

....... 1410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 58F672EDCD57CCD8

FASTA1,410155,344
        10         20         30         40         50         60 
MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT TVSVSQQPVS APVPIAAHAS 

        70         80         90        100        110        120 
VAGHLSTSTT VSSSGAQNSD STKKTLVTLI ANNNAGNPLV QQGGQPLILT QNPAPGLGTM 

       130        140        150        160        170        180 
VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ 

       190        200        210        220        230        240 
TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST 

       250        260        270        280        290        300 
VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AVQSPGQSNQ TTNPKLAPSF PSPPAVSIAS 

       310        320        330        340        350        360 
FVTVKRPGVT GENSNEVAKL VNTLNTIPSL GQSPGPVVVS NNSSAHGSQR TSGPESSMKV 

       370        380        390        400        410        420 
TSSIPVFDLQ DGGRKICPRC NAQFRVTEAL RGHMCYCCPE MVEYQKKGKS LDSEPSVPSA 

       430        440        450        460        470        480 
AKPPSPEKTA PVASTPSSTP IPALSPPTKV PEPNENVGDA VQTKLIMLVD DFYYGRDGGK 

       490        500        510        520        530        540 
VAQLTNFPKV ATSFRCPHCT KRLKNNIRFM NHMKHHVELD QQNGEVDGHT ICQHCYRQFS 

       550        560        570        580        590        600 
TPFQLQCHLE NVHSPYESTT KCKICEWAFE SEPLFLQHMK DTHKPGEMPY VCQVCQYRSS 

       610        620        630        640        650        660 
LYSEVDVHFR MIHEDTRHLL CPYCLKVFKN GNAFQQHYMR HQKRNVYHCN KCRLQFLFAK 

       670        680        690        700        710        720 
DKIEHKLQHH KTFRKPKQLE GLKPGTKVTI RASRGQPRTV PVSSNDTPPS ALQEAAPLTS 

       730        740        750        760        770        780 
SMDPLPVFLY PPVQRSIQKR AVRKMSVMGR QTCLECSFEI PDFPNHFPTY VHCSLCRYST 

       790        800        810        820        830        840 
CCSRAYANHM INNHVPRKSP KYLALFKNSV SGIKLACTSC TFVTSVGDAM AKHLVFNPSH 

       850        860        870        880        890        900 
RSSSILPRGL TWIAHSRHGQ TRDRVHDRNV KNMYPPPSFP TNKAATVKSA GATPAEPEEL 

       910        920        930        940        950        960 
LTPLAPALPS PASTATPPPT PTHPQALALP PLATEGAECL NVDDQDEGSP VTQEPELASG 

       970        980        990       1000       1010       1020 
GGGSGGVGKK EQLSVKKLRV VLFALCCNTE QAAEHFRNPQ RRIRRWLRRF QASQGENLEG 

      1030       1040       1050       1060       1070       1080 
KYLSFEAEEK LAEWVLTQRE QQLPVNEETL FQKATKIGRS LEGGFKISYE WAVRFMLRHH 

      1090       1100       1110       1120       1130       1140 
LTPHARRAVA HTLPKDVAEN AGLFIDFVQR QIHNQDLPLS MIVAIDEISL FLDTEVLSSD 

      1150       1160       1170       1180       1190       1200 
DRKENALQTV GTGEPWCDVV LAILADGTVL PTLVFYRGQM DQPANMPDSI LLEAKESGYS 

      1210       1220       1230       1240       1250       1260 
DDEIMELWST RVWQKHTACQ RSKGMLVMDC HRTHLSEEVL AMLSASSTLP AVVPAGCSSK 

      1270       1280       1290       1300       1310       1320 
IQPLDVCIKR TVKNFLHKKW KEQAREMADT ACDSDVLLQL VLVWLGEVLG VIGDCPELVQ 

      1330       1340       1350       1360       1370       1380 
RSFLVASVLP GPDGNINSPT RNADMQEELI ASLEEQLKLS GEHSESSTPR PRSSPEETIE 

      1390       1400       1410 
PESLHQLFEG ESETESFYGF EEADLDLMEI 

« Hide

Isoform 2 [UniParc].

Checksum: 3EC92965C8E95A98
Show »

FASTA1,357150,130
Isoform 3 [UniParc].

Checksum: C88635F4469B70AA
Show »

FASTA1,366151,213
Isoform 4 [UniParc].

Checksum: E4CA34C166CC3E78
Show »

FASTA36337,882
Isoform 5 (CRA_e) [UniParc].

Checksum: 457D70CDC875B81C
Show »

FASTA1,315145,295
Isoform 6 [UniParc].

Checksum: 99537C2A84842376
Show »

FASTA1,401154,492
Isoform 7 [UniParc].

Checksum: 0016C4CF1C9CB146
Show »

FASTA1,348149,278

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Retina.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
Tissue: Placenta and Testis.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1107 (ISOFORM 3).
Tissue: Neuroblastoma.
[6]"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
Gunther M., Laithier M., Brison O.
Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-788 (ISOFORM 1), INTERACTION WITH SP1.
Tissue: Colon.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363 (ISOFORM 4).
Tissue: Placenta.
[8]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1410 (ISOFORM 2).
Tissue: Brain.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-425 AND SER-1338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Lens epithelium-derived growth factor/p75 interacts with the transposase-derived DDE domain of PogZ."
Bartholomeeusen K., Christ F., Hendrix J., Rain J.C., Emiliani S., Benarous R., Debyser Z., Gijsbers R., De Rijck J.
J. Biol. Chem. 284:11467-11477(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PSIP1.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHAMP1; MAD2L2; CBX1; CBX3 AND CBX5.
[14]"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CBX1; CBX3 AND CBX5, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-817; CYS-820; HIS-833 AND HIS-840.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of the zinc finger domain of human KIAA0461."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 352-405.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX537838 mRNA. Translation: CAD97850.1.
AK300307 mRNA. Translation: BAG62060.1.
AK302501 mRNA. Translation: BAG63781.1.
AL589764 Genomic DNA. Translation: CAI16807.1.
AL589764 Genomic DNA. Translation: CAI16808.2. Sequence problems.
AL589764 Genomic DNA. Translation: CAI16809.1.
AL589764 Genomic DNA. Translation: CAI16810.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53440.1.
AB037911 mRNA. Translation: BAB87117.1.
AB075477 mRNA. Translation: BAE45744.1. Different initiation.
AJ242979 mRNA. Translation: CAB45136.1.
BC057773 mRNA. Translation: AAH57773.1.
AB007930 mRNA. Translation: BAA32306.1.
PIRT00075.
RefSeqNP_001181866.1. NM_001194937.1.
NP_001181867.1. NM_001194938.1.
NP_055915.2. NM_015100.3.
NP_665739.3. NM_145796.3.
NP_997054.1. NM_207171.2.
XP_005245056.1. XM_005244999.1.
XP_005245057.1. XM_005245000.2.
XP_005245058.1. XM_005245001.1.
XP_005245060.1. XM_005245003.1.
XP_005245061.1. XM_005245004.1.
XP_005245062.1. XM_005245005.1.
XP_005245063.1. XM_005245006.2.
UniGeneHs.489873.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E72NMR-A370-405[»]
ProteinModelPortalQ7Z3K3.
SMRQ7Z3K3. Positions 374-405, 493-682, 970-1080.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116745. 14 interactions.
DIPDIP-38044N.
IntActQ7Z3K3. 55 interactions.
MINTMINT-144501.

PTM databases

PhosphoSiteQ7Z3K3.

Polymorphism databases

DMDM143811442.

Proteomic databases

PaxDbQ7Z3K3.
PRIDEQ7Z3K3.

Protocols and materials databases

DNASU23126.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271715; ENSP00000271715; ENSG00000143442. [Q7Z3K3-1]
ENST00000361398; ENSP00000354467; ENSG00000143442. [Q7Z3K3-2]
ENST00000368863; ENSP00000357856; ENSG00000143442. [Q7Z3K3-5]
ENST00000392723; ENSP00000376484; ENSG00000143442. [Q7Z3K3-2]
ENST00000409503; ENSP00000386836; ENSG00000143442. [Q7Z3K3-6]
ENST00000491586; ENSP00000418408; ENSG00000143442. [Q7Z3K3-3]
ENST00000531094; ENSP00000431259; ENSG00000143442. [Q7Z3K3-7]
GeneID23126.
KEGGhsa:23126.
UCSCuc001eyd.2. human. [Q7Z3K3-1]
uc001eyf.2. human. [Q7Z3K3-3]
uc001eyg.2. human. [Q7Z3K3-4]
uc009wmv.2. human. [Q7Z3K3-5]
uc021oyq.1. human. [Q7Z3K3-2]

Organism-specific databases

CTD23126.
GeneCardsGC01M151375.
HGNCHGNC:18801. POGZ.
HPAHPA006800.
HPA008781.
MIM614787. gene.
neXtProtNX_Q7Z3K3.
PharmGKBPA38685.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239493.
HOVERGENHBG049435.
InParanoidQ7Z3K3.
OMATPTHPQP.
OrthoDBEOG7QVM24.
PhylomeDBQ7Z3K3.
TreeFamTF331707.

Gene expression databases

ArrayExpressQ7Z3K3.
BgeeQ7Z3K3.
CleanExHS_POGZ.
GenevestigatorQ7Z3K3.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR004875. DDE_SF_endonuclease_CENPB-like.
IPR009057. Homeodomain-like.
IPR006600. HTH_CenpB_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF03184. DDE_1. 1 hit.
PF03221. HTH_Tnp_Tc5. 1 hit.
[Graphical view]
SMARTSM00674. CENPB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS51253. HTH_CENPB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7Z3K3.
GeneWikiPOGZ.
GenomeRNAi23126.
NextBio44359.
PROQ7Z3K3.
SOURCESearch...

Entry information

Entry namePOGZ_HUMAN
AccessionPrimary (citable) accession number: Q7Z3K3
Secondary accession number(s): B4DTP8 expand/collapse secondary AC list , B4DYL9, B7ZBY5, E9PM80, O75049, Q3LIC4, Q5SZS1, Q5SZS2, Q5SZS3, Q5SZS4, Q8TDZ7, Q9Y4X7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM