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GPTC4_HUMAN
ID   GPTC4_HUMAN             Reviewed;         446 AA.
AC   Q5T3I0; Q5T3I1; Q6ZUE7; Q8IWG8; Q9NXH4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=G patch domain-containing protein 4;
GN   Name=GPATCH4; Synonyms=GPATC4;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-207 (ISOFORM 1).
RC   TISSUE=Colon mucosa;
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 GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix, Kidney, and Ovary;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-174 (ISOFORM 3).
RX   PubMed=16712791; DOI=10.1016/j.bbrc.2006.04.175;
RA   Wang A.G., Yoon S.Y., Oh J.H., Jeon Y.J., Kim M., Kim J.M., Byun S.S.,
RA   Yang J.O., Kim J.H., Kim D.G., Yeom Y.I., Yoo H.S., Kim Y.S., Kim N.S.;
RT   "Identification of intrahepatic cholangiocarcinoma related genes by
RT   comparison with normal liver tissues using expressed sequence tags.";
RL   Biochem. Biophys. Res. Commun. 345:1022-1032(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116; SER-128; SER-130 AND
RP   SER-139, 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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT THR-4, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-130, AND
RP   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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- INTERACTION:
CC       Q5T3I0; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-2372076, EBI-739624;
CC       Q5T3I0; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-2372076, EBI-749265;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5T3I0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T3I0-2; Sequence=VSP_025479, VSP_025480, VSP_025481;
CC       Name=3;
CC         IsoId=Q5T3I0-3; Sequence=VSP_040831;
CC   -!- POLYMORPHISM: This gene contains polymorphic substitutions in the last
CC       exon causing a frameshift variant C-terminal sequence compared to the
CC       official human genome. However, this variant sequence is in agreement
CC       with ortholog sequences.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH40147.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK000256; BAA91036.1; -; mRNA.
DR   EMBL; AK125763; BAC86278.1; -; mRNA.
DR   EMBL; AL365181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032436; AAH32436.1; -; mRNA.
DR   EMBL; BC040147; AAH40147.1; ALT_INIT; mRNA.
DR   EMBL; BC056904; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CB109133; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q5T3I0; -.
DR   IntAct; Q5T3I0; 122.
DR   MINT; Q5T3I0; -.
DR   STRING; 9606.ENSP00000396441; -.
DR   GlyGen; Q5T3I0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5T3I0; -.
DR   MetOSite; Q5T3I0; -.
DR   PhosphoSitePlus; Q5T3I0; -.
DR   BioMuta; GPATCH4; -.
DR   DMDM; 147644784; -.
DR   EPD; Q5T3I0; -.
DR   jPOST; Q5T3I0; -.
DR   MassIVE; Q5T3I0; -.
DR   MaxQB; Q5T3I0; -.
DR   PaxDb; Q5T3I0; -.
DR   PeptideAtlas; Q5T3I0; -.
DR   PRIDE; Q5T3I0; -.
DR   ProteomicsDB; 64394; -. [Q5T3I0-1]
DR   ProteomicsDB; 64395; -. [Q5T3I0-2]
DR   ProteomicsDB; 64396; -. [Q5T3I0-3]
DR   DNASU; 54865; -.
DR   GeneCards; GPATCH4; -.
DR   HGNC; HGNC:25982; GPATCH4.
DR   neXtProt; NX_Q5T3I0; -.
DR   PharmGKB; PA162390084; -.
DR   eggNOG; KOG2809; Eukaryota.
DR   InParanoid; Q5T3I0; -.
DR   PhylomeDB; Q5T3I0; -.
DR   PathwayCommons; Q5T3I0; -.
DR   SignaLink; Q5T3I0; -.
DR   ChiTaRS; GPATCH4; human.
DR   Pharos; Q5T3I0; Tdark.
DR   PRO; PR:Q5T3I0; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q5T3I0; protein.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0090069; P:regulation of ribosome biogenesis; IBA:GO_Central.
DR   InterPro; IPR000467; G_patch_dom.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..446
FT                   /note="G patch domain-containing protein 4"
FT                   /id="PRO_0000287462"
FT   DOMAIN          11..57
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          116..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..251
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        209..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT   MOD_RES         4
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        46
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..51
FT                   /note="MNVTPEVKSRGMKFAEEQLLKHGWTQGKGLGRKENGITQALRVTLKQDTHG
FT                   -> MDGLK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025479"
FT   VAR_SEQ         1..5
FT                   /note="MNVTP -> MFPRSGPSND (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16712791"
FT                   /id="VSP_040831"
FT   VAR_SEQ         112..185
FT                   /note="MATLTSGGEKPNKDLESCSDDDNQGSKSPKILTDEMLLQACEGRTAHKAARL
FT                   GITMKAKLARLEAQEQAFLARL -> VLEAVGNRVHPFSLPWFPWGLNSCLVCLINSQN
FT                   FPNIVGSCDQPCCCLLRLPRPSAGIEIFRFRGSCHLLREQQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025480"
FT   VAR_SEQ         186..446
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025481"
SQ   SEQUENCE   446 AA;  50381 MW;  51D64BF5B4AEB3C6 CRC64;
     MNVTPEVKSR GMKFAEEQLL KHGWTQGKGL GRKENGITQA LRVTLKQDTH GVGHDPAKEF
     TNHWWNELFN KTAANLVVET GQDGVQIRSL SKETTRYNHP KPNLLYQKFV KMATLTSGGE
     KPNKDLESCS DDDNQGSKSP KILTDEMLLQ ACEGRTAHKA ARLGITMKAK LARLEAQEQA
     FLARLKGQDP GAPQLQSESK PPKKKKKKRR QKEEEEATAS ERNDADEKHP EHAEQNIRKS
     KKKKRRHQEG KVSDEREGTT KGNEKEDAAG TSGLGELNSR EQTNQSLRKG KKKKRWHHEE
     EKMGVLEEGG KGKEAAGSVR TEEVESRAYA DPCSRRKKRQ QQEEEDLNLE DRGEETVLGG
     GTREAESRAC SDGRSRKSKK KRQQHQEEED ILDVRDEKDG GAREAESRAH TGSSSRGKRK
     RQQHPKKERA GVSTVQKAKK KQKKRD
 
 
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