Full text data of GNL1
GNL1
(HSR1)
[Confidence: low (only semi-automatic identification from reviews)]
Guanine nucleotide-binding protein-like 1 (GTP-binding protein HSR1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanine nucleotide-binding protein-like 1 (GTP-binding protein HSR1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P36915
ID GNL1_HUMAN Reviewed; 607 AA.
AC P36915; B0S838; Q96CT5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JUL-2007, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
DE AltName: Full=GTP-binding protein HSR1;
GN Name=GNL1; Synonyms=HSR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=8180467; DOI=10.1007/BF00292335;
RA Vernet C., Ribouchon M.-T., Chimini G., Pontarotti P.;
RT "Structure and evolution of a member of a new subfamily of GTP-binding
RT proteins mapping to the human MHC class I region.";
RL Mamm. Genome 5:100-105(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-34;
RP THR-48; THR-50; SER-51 AND SER-324, AND MASS SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51,
RP AND MASS SPECTROMETRY.
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 [10]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36915-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36915-2; Sequence=VSP_026992, VSP_026993;
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs
CC described by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the MMR1/HSR1 GTP-binding protein family.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L25665; AAA66492.1; -; mRNA.
DR EMBL; BT006648; AAP35294.1; -; mRNA.
DR EMBL; AL662825; CAI17831.1; -; Genomic_DNA.
DR EMBL; AL662800; CAI18152.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18558.1; -; Genomic_DNA.
DR EMBL; BX248518; CAM26012.1; -; Genomic_DNA.
DR EMBL; CR388372; CAQ07868.1; -; Genomic_DNA.
DR EMBL; CR936927; CAQ08501.1; -; Genomic_DNA.
DR EMBL; BX927220; CAQ09053.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03294.1; -; Genomic_DNA.
DR EMBL; BC013959; AAH13959.1; -; mRNA.
DR EMBL; BC018366; AAH18366.1; -; mRNA.
DR PIR; I57013; I57013.
DR RefSeq; NP_005266.2; NM_005275.3.
DR RefSeq; XP_005249072.1; XM_005249015.1.
DR RefSeq; XP_005272850.1; XM_005272793.1.
DR RefSeq; XP_005274996.1; XM_005274939.1.
DR RefSeq; XP_005275150.1; XM_005275093.1.
DR RefSeq; XP_005275292.1; XM_005275235.1.
DR RefSeq; XP_005275426.1; XM_005275369.1.
DR RefSeq; XP_005275586.1; XM_005275529.1.
DR UniGene; Hs.118354; -.
DR UniGene; Hs.83147; -.
DR ProteinModelPortal; P36915; -.
DR SMR; P36915; 363-414.
DR IntAct; P36915; 3.
DR STRING; 9606.ENSP00000394290; -.
DR DMDM; 158939140; -.
DR PaxDb; P36915; -.
DR PRIDE; P36915; -.
DR DNASU; 2794; -.
DR Ensembl; ENST00000376621; ENSP00000365806; ENSG00000204590.
DR Ensembl; ENST00000383596; ENSP00000373090; ENSG00000206492.
DR Ensembl; ENST00000417834; ENSP00000403576; ENSG00000226882.
DR Ensembl; ENST00000428189; ENSP00000409074; ENSG00000229470.
DR Ensembl; ENST00000437917; ENSP00000411162; ENSG00000228581.
DR Ensembl; ENST00000441604; ENSP00000394290; ENSG00000235986.
DR Ensembl; ENST00000454829; ENSP00000409367; ENSG00000232143.
DR GeneID; 2794; -.
DR KEGG; hsa:2794; -.
DR UCSC; uc003nqh.3; human.
DR CTD; 2794; -.
DR GeneCards; GC06M030509; -.
DR GeneCards; GC06Mj30498; -.
DR GeneCards; GC06Mk30499; -.
DR GeneCards; GC06Ml30553; -.
DR GeneCards; GC06Mm30587; -.
DR GeneCards; GC06Mn30498; -.
DR GeneCards; GC06Mo30500; -.
DR HGNC; HGNC:4413; GNL1.
DR HPA; CAB033575; -.
DR HPA; HPA043338; -.
DR MIM; 143024; gene.
DR neXtProt; NX_P36915; -.
DR PharmGKB; PA28792; -.
DR eggNOG; COG1161; -.
DR HOGENOM; HOG000007598; -.
DR HOVERGEN; HBG005865; -.
DR InParanoid; P36915; -.
DR OMA; CIGFPNV; -.
DR PhylomeDB; P36915; -.
DR ChiTaRS; GNL1; human.
DR GenomeRNAi; 2794; -.
DR NextBio; 11009; -.
DR PMAP-CutDB; P36915; -.
DR PRO; PR:P36915; -.
DR ArrayExpress; P36915; -.
DR Bgee; P36915; -.
DR CleanEx; HS_GNL1; -.
DR Genevestigator; P36915; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:RefGenome.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:RefGenome.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0002456; P:T cell mediated immunity; NAS:UniProtKB.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 607 Guanine nucleotide-binding protein-like
FT 1.
FT /FTId=PRO_0000122441.
FT DOMAIN 372 419 G.
FT NP_BIND 225 228 GTP (Potential).
FT NP_BIND 367 374 GTP (Potential).
FT NP_BIND 411 415 GTP (Potential).
FT COMPBIAS 551 607 Asp/Glu-rich (highly acidic).
FT MOD_RES 32 32 Phosphoserine.
FT MOD_RES 33 33 Phosphoserine.
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 48 48 Phosphothreonine.
FT MOD_RES 50 50 Phosphothreonine.
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 324 324 Phosphoserine.
FT VAR_SEQ 1 177 Missing (in isoform 2).
FT /FTId=VSP_026992.
FT VAR_SEQ 178 183 WRQLWR -> MEAAVA (in isoform 2).
FT /FTId=VSP_026993.
FT CONFLICT 232 233 PA -> RR (in Ref. 1; AAA66492).
FT CONFLICT 315 315 Missing (in Ref. 1; AAA66492).
FT CONFLICT 339 339 E -> EQ (in Ref. 1; AAA66492).
FT CONFLICT 514 514 L -> V (in Ref. 1; AAA66492).
SQ SEQUENCE 607 AA; 68661 MW; F8EBB4EDBB73D929 CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA ELLELDIREV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG PTQERYKDGV
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV
VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA
LLGEDEC
//
ID GNL1_HUMAN Reviewed; 607 AA.
AC P36915; B0S838; Q96CT5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JUL-2007, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
DE AltName: Full=GTP-binding protein HSR1;
GN Name=GNL1; Synonyms=HSR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=8180467; DOI=10.1007/BF00292335;
RA Vernet C., Ribouchon M.-T., Chimini G., Pontarotti P.;
RT "Structure and evolution of a member of a new subfamily of GTP-binding
RT proteins mapping to the human MHC class I region.";
RL Mamm. Genome 5:100-105(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-34;
RP THR-48; THR-50; SER-51 AND SER-324, AND MASS SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51,
RP AND MASS SPECTROMETRY.
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 [10]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36915-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36915-2; Sequence=VSP_026992, VSP_026993;
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs
CC described by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the MMR1/HSR1 GTP-binding protein family.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L25665; AAA66492.1; -; mRNA.
DR EMBL; BT006648; AAP35294.1; -; mRNA.
DR EMBL; AL662825; CAI17831.1; -; Genomic_DNA.
DR EMBL; AL662800; CAI18152.1; -; Genomic_DNA.
DR EMBL; BX000357; CAI18558.1; -; Genomic_DNA.
DR EMBL; BX248518; CAM26012.1; -; Genomic_DNA.
DR EMBL; CR388372; CAQ07868.1; -; Genomic_DNA.
DR EMBL; CR936927; CAQ08501.1; -; Genomic_DNA.
DR EMBL; BX927220; CAQ09053.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03294.1; -; Genomic_DNA.
DR EMBL; BC013959; AAH13959.1; -; mRNA.
DR EMBL; BC018366; AAH18366.1; -; mRNA.
DR PIR; I57013; I57013.
DR RefSeq; NP_005266.2; NM_005275.3.
DR RefSeq; XP_005249072.1; XM_005249015.1.
DR RefSeq; XP_005272850.1; XM_005272793.1.
DR RefSeq; XP_005274996.1; XM_005274939.1.
DR RefSeq; XP_005275150.1; XM_005275093.1.
DR RefSeq; XP_005275292.1; XM_005275235.1.
DR RefSeq; XP_005275426.1; XM_005275369.1.
DR RefSeq; XP_005275586.1; XM_005275529.1.
DR UniGene; Hs.118354; -.
DR UniGene; Hs.83147; -.
DR ProteinModelPortal; P36915; -.
DR SMR; P36915; 363-414.
DR IntAct; P36915; 3.
DR STRING; 9606.ENSP00000394290; -.
DR DMDM; 158939140; -.
DR PaxDb; P36915; -.
DR PRIDE; P36915; -.
DR DNASU; 2794; -.
DR Ensembl; ENST00000376621; ENSP00000365806; ENSG00000204590.
DR Ensembl; ENST00000383596; ENSP00000373090; ENSG00000206492.
DR Ensembl; ENST00000417834; ENSP00000403576; ENSG00000226882.
DR Ensembl; ENST00000428189; ENSP00000409074; ENSG00000229470.
DR Ensembl; ENST00000437917; ENSP00000411162; ENSG00000228581.
DR Ensembl; ENST00000441604; ENSP00000394290; ENSG00000235986.
DR Ensembl; ENST00000454829; ENSP00000409367; ENSG00000232143.
DR GeneID; 2794; -.
DR KEGG; hsa:2794; -.
DR UCSC; uc003nqh.3; human.
DR CTD; 2794; -.
DR GeneCards; GC06M030509; -.
DR GeneCards; GC06Mj30498; -.
DR GeneCards; GC06Mk30499; -.
DR GeneCards; GC06Ml30553; -.
DR GeneCards; GC06Mm30587; -.
DR GeneCards; GC06Mn30498; -.
DR GeneCards; GC06Mo30500; -.
DR HGNC; HGNC:4413; GNL1.
DR HPA; CAB033575; -.
DR HPA; HPA043338; -.
DR MIM; 143024; gene.
DR neXtProt; NX_P36915; -.
DR PharmGKB; PA28792; -.
DR eggNOG; COG1161; -.
DR HOGENOM; HOG000007598; -.
DR HOVERGEN; HBG005865; -.
DR InParanoid; P36915; -.
DR OMA; CIGFPNV; -.
DR PhylomeDB; P36915; -.
DR ChiTaRS; GNL1; human.
DR GenomeRNAi; 2794; -.
DR NextBio; 11009; -.
DR PMAP-CutDB; P36915; -.
DR PRO; PR:P36915; -.
DR ArrayExpress; P36915; -.
DR Bgee; P36915; -.
DR CleanEx; HS_GNL1; -.
DR Genevestigator; P36915; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:RefGenome.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:RefGenome.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0002456; P:T cell mediated immunity; NAS:UniProtKB.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 607 Guanine nucleotide-binding protein-like
FT 1.
FT /FTId=PRO_0000122441.
FT DOMAIN 372 419 G.
FT NP_BIND 225 228 GTP (Potential).
FT NP_BIND 367 374 GTP (Potential).
FT NP_BIND 411 415 GTP (Potential).
FT COMPBIAS 551 607 Asp/Glu-rich (highly acidic).
FT MOD_RES 32 32 Phosphoserine.
FT MOD_RES 33 33 Phosphoserine.
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 48 48 Phosphothreonine.
FT MOD_RES 50 50 Phosphothreonine.
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 324 324 Phosphoserine.
FT VAR_SEQ 1 177 Missing (in isoform 2).
FT /FTId=VSP_026992.
FT VAR_SEQ 178 183 WRQLWR -> MEAAVA (in isoform 2).
FT /FTId=VSP_026993.
FT CONFLICT 232 233 PA -> RR (in Ref. 1; AAA66492).
FT CONFLICT 315 315 Missing (in Ref. 1; AAA66492).
FT CONFLICT 339 339 E -> EQ (in Ref. 1; AAA66492).
FT CONFLICT 514 514 L -> V (in Ref. 1; AAA66492).
SQ SEQUENCE 607 AA; 68661 MW; F8EBB4EDBB73D929 CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA ELLELDIREV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG PTQERYKDGV
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV
VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA
LLGEDEC
//
MIM
143024
*RECORD*
*FIELD* NO
143024
*FIELD* TI
*143024 GUANINE NUCLEOTIDE-BINDING PROTEIN-LIKE 1; GNL1
;;HSR1 GTP-BINDING PROTEIN
read more*FIELD* TX
The GNL1 gene (also referred to as the HSR1 gene), identified in the
human major histocompatibility complex class I region, shows a high
degree of homology with its mouse counterpart. Vernet et al. (1994)
found that the HSR1 gene is located less than 2 kb centromeric to HLA-E
(143010), in the same transcriptional orientation. HSR1 is telomeric to
HLA-B (142830) and HLA-C (142840).
*FIELD* RF
1. Vernet, C.; Ribouchon, M.-T.; Chimini, G.; Pontarotti, P.: Structure
and evolution of a member of a new subfamily of GTP-binding proteins
mapping to the human MHC class I region. Mammalian Genome 5: 100-105,
1994.
*FIELD* CD
Victor A. McKusick: 4/4/1994
*FIELD* ED
carol: 07/02/1998
mark: 10/10/1995
carol: 4/4/1994
*RECORD*
*FIELD* NO
143024
*FIELD* TI
*143024 GUANINE NUCLEOTIDE-BINDING PROTEIN-LIKE 1; GNL1
;;HSR1 GTP-BINDING PROTEIN
read more*FIELD* TX
The GNL1 gene (also referred to as the HSR1 gene), identified in the
human major histocompatibility complex class I region, shows a high
degree of homology with its mouse counterpart. Vernet et al. (1994)
found that the HSR1 gene is located less than 2 kb centromeric to HLA-E
(143010), in the same transcriptional orientation. HSR1 is telomeric to
HLA-B (142830) and HLA-C (142840).
*FIELD* RF
1. Vernet, C.; Ribouchon, M.-T.; Chimini, G.; Pontarotti, P.: Structure
and evolution of a member of a new subfamily of GTP-binding proteins
mapping to the human MHC class I region. Mammalian Genome 5: 100-105,
1994.
*FIELD* CD
Victor A. McKusick: 4/4/1994
*FIELD* ED
carol: 07/02/1998
mark: 10/10/1995
carol: 4/4/1994