GLCI1_HUMAN
ID GLCI1_HUMAN Reviewed; 547 AA.
AC Q86VQ1; A4D103; Q96FD0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glucocorticoid-induced transcript 1 protein;
GN Name=GLCCI1;
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 GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Testis;
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 TISSUE SPECIFICITY.
RX PubMed=12557054; DOI=10.1007/s00251-002-0513-1;
RA Miazek A., Malissen B.;
RT "Two genes, three messengers: hybrid transcript between a gene expressed at
RT specific stages of T-cell and sperm maturation and an unrelated adjacent
RT gene.";
RL Immunogenetics 54:681-692(2003).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-172;
RP THR-175 AND SER-345, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP IDENTIFICATION BY MASS 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-258; SER-398 AND
RP SER-480, AND 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 [12]
RP INVOLVEMENT IN ASTHMA RESPONSE TO GLUCOCORTICOID TREATMENT, AND TISSUE
RP SPECIFICITY.
RX PubMed=21991891; DOI=10.1056/nejmoa0911353;
RA Tantisira K.G., Lasky-Su J., Harada M., Murphy A., Litonjua A.A.,
RA Himes B.E., Lange C., Lazarus R., Sylvia J., Klanderman B., Duan Q.L.,
RA Qiu W., Hirota T., Martinez F.D., Mauger D., Sorkness C., Szefler S.,
RA Lazarus S.C., Lemanske R.F. Jr., Peters S.P., Lima J.J., Nakamura Y.,
RA Tamari M., Weiss S.T.;
RT "Genomewide association between GLCCI1 and response to glucocorticoid
RT therapy in asthma.";
RL N. Engl. J. Med. 365:1173-1183(2011).
RN [13]
RP INVOLVEMENT IN CHRONIC OBSTRUCTIVE PULMONARY DISEASE RESPONSE TO
RP GLUCOCORTICOID TREATMENT.
RX PubMed=22187997; DOI=10.1056/nejmc1112547;
RA Van den Berge M., Hiemstra P.S., Postma D.S.;
RT "Genetics of glucocorticoids in asthma.";
RL N. Engl. J. Med. 365:2434-2435(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-258 AND SER-398, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-79; SER-105; SER-108;
RP SER-171; SER-172; SER-258; SER-303; THR-343; SER-345 AND SER-406, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lung, spleen, thymus and
CC testis and, at lower levels, in brain, bone marrow, peripheral
CC leukocytes, skin and trachea. {ECO:0000269|PubMed:12557054,
CC ECO:0000269|PubMed:21991891}.
CC -!- POLYMORPHISM: Polymorphisms dbSNP:rs37972 and dbSNP:rs37973, located in
CC GLCCI1 promoter region, are associated with a decreased response to
CC glucorticoid treatment [MIM:614400] in asthma patients
CC (PubMed:21991891), as well as in chronic obstructive pulmonary disease
CC patients (PubMed:22187997). The mean increase in forced expiratory
CC volume in 1 second in glucorticoid treated subjects who are homozygous
CC for the mutant (G) rs37973 allele is only about one-third of that seen
CC in similarly treated subjects who are homozygous for the wild-type
CC allele (A) (PubMed:21991891). These polymorphisms affect GLCCI1
CC transcription level. {ECO:0000269|PubMed:21991891,
CC ECO:0000269|PubMed:22187997}.
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DR EMBL; CH236948; EAL24302.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93607.1; -; Genomic_DNA.
DR EMBL; BC011254; AAH11254.1; -; mRNA.
DR EMBL; BC050291; AAH50291.1; -; mRNA.
DR CCDS; CCDS34601.1; -.
DR RefSeq; NP_612435.1; NM_138426.3.
DR AlphaFoldDB; Q86VQ1; -.
DR SMR; Q86VQ1; -.
DR BioGRID; 125239; 19.
DR IntAct; Q86VQ1; 12.
DR MINT; Q86VQ1; -.
DR STRING; 9606.ENSP00000223145; -.
DR GlyGen; Q86VQ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86VQ1; -.
DR PhosphoSitePlus; Q86VQ1; -.
DR BioMuta; GLCCI1; -.
DR DMDM; 74727602; -.
DR EPD; Q86VQ1; -.
DR jPOST; Q86VQ1; -.
DR MassIVE; Q86VQ1; -.
DR MaxQB; Q86VQ1; -.
DR PaxDb; Q86VQ1; -.
DR PeptideAtlas; Q86VQ1; -.
DR PRIDE; Q86VQ1; -.
DR ProteomicsDB; 70055; -.
DR Antibodypedia; 945; 183 antibodies from 20 providers.
DR DNASU; 113263; -.
DR Ensembl; ENST00000223145.10; ENSP00000223145.5; ENSG00000106415.13.
DR GeneID; 113263; -.
DR KEGG; hsa:113263; -.
DR MANE-Select; ENST00000223145.10; ENSP00000223145.5; NM_138426.4; NP_612435.1.
DR UCSC; uc003srk.5; human.
DR CTD; 113263; -.
DR DisGeNET; 113263; -.
DR GeneCards; GLCCI1; -.
DR HGNC; HGNC:18713; GLCCI1.
DR HPA; ENSG00000106415; Tissue enhanced (lymphoid).
DR MalaCards; GLCCI1; -.
DR MIM; 614283; gene.
DR MIM; 614400; phenotype.
DR neXtProt; NX_Q86VQ1; -.
DR OpenTargets; ENSG00000106415; -.
DR PharmGKB; PA38657; -.
DR VEuPathDB; HostDB:ENSG00000106415; -.
DR eggNOG; ENOG502QRQF; Eukaryota.
DR GeneTree; ENSGT00950000183046; -.
DR HOGENOM; CLU_033432_3_1_1; -.
DR InParanoid; Q86VQ1; -.
DR OMA; CRADRAK; -.
DR OrthoDB; 1132072at2759; -.
DR PhylomeDB; Q86VQ1; -.
DR TreeFam; TF333159; -.
DR PathwayCommons; Q86VQ1; -.
DR SignaLink; Q86VQ1; -.
DR BioGRID-ORCS; 113263; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; GLCCI1; human.
DR GeneWiki; GLCCI1; -.
DR GenomeRNAi; 113263; -.
DR Pharos; Q86VQ1; Tbio.
DR PRO; PR:Q86VQ1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86VQ1; protein.
DR Bgee; ENSG00000106415; Expressed in thymus and 188 other tissues.
DR ExpressionAtlas; Q86VQ1; baseline and differential.
DR Genevisible; Q86VQ1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR InterPro; IPR026639; Glcci1.
DR InterPro; IPR026642; Glcci1/FAM117.
DR PANTHER; PTHR14972; PTHR14972; 1.
DR PANTHER; PTHR14972:SF3; PTHR14972:SF3; 1.
DR Pfam; PF15388; FAM117; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..547
FT /note="Glucocorticoid-induced transcript 1 protein"
FT /id="PRO_0000256128"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..254
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I9"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I9"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I9"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I9"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I9"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 547 AA; 58024 MW; 51B6AF7788E8800D CRC64;
MSTASSSSSS SSSQTPHPPS QRMRRSAAGS PPAVAAAGSG NGAGGGGGVG CAPAAGAGRL
LQPIRATVPY QLLRGSQHSP TRPPVAAAAA SLGSLPGPGA ARGPSPSSPT PPAAAAPAEQ
APRAKGRPRR SPESHRRSSS PERRSPGSPV CRADKAKSQQ VRTSSTIRRT SSLDTITGPY
LTGQWPRDPH VHYPSCMKDK ATQTPSCWAE EGAEKRSHQR SASWGSADQL KEQIAKLRQQ
LQRSKQSSRH SKEKDRQSPL HGNHITISHT QATGSRSVPM PLSNISVPKS SVSRVPCNVE
GISPELEKVF IKENNGKEEV SKPLDIPDGR RAPLPAHYRS SSTRSIDTQT PSVQERSSSC
SSHSPCVSPF CPPESQDGSP CSTEDLLYDR DKDSGSSSPL PKYASSPKPN NSYMFKREPP
EGCERVKVFE EMASRQPISA PLFSCPDKNK VNFIPTGSAF CPVKLLGPLL PASDLMLKNS
PNSGQSSALA TLTVEQLSSR VSFTSLSDDT STAGSMEASV QQPSQQQQLL QELQGEDHIS
AQNYVII
