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Q92616

- GCN1L_HUMAN

UniProt

Q92616 - GCN1L_HUMAN

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Protein

Translational activator GCN1

Gene

GCN1L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a translation activator that mediates translational control and perform an EF3-related function on the ribosome by regulating GCN2 protein kinase (EIF2AK1-4) activity.By similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. translation factor activity, nucleic acid binding Source: UniProtKB

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. translation Source: GOC
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Translational activator GCN1
Short name:
HsGCN1
Alternative name(s):
GCN1-like protein 1
Gene namesi
Name:GCN1L1
Synonyms:KIAA0219
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4199. GCN1L1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
  3. ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 26712670Translational activator GCN1PRO_0000087443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei786 – 7861Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92616.
PaxDbiQ92616.
PRIDEiQ92616.

PTM databases

PhosphoSiteiQ92616.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ92616.
ExpressionAtlasiQ92616. baseline and differential.
GenevestigatoriQ92616.

Organism-specific databases

HPAiHPA018799.
HPA019648.
HPA024367.

Interactioni

Subunit structurei

Interacts with IMPACT; prevents the interaction with GCN2 protein kinase (EIF2AK1-4).By similarity

Protein-protein interaction databases

BioGridi116181. 69 interactions.
IntActiQ92616. 28 interactions.
MINTiMINT-1144027.

Structurei

3D structure databases

ProteinModelPortaliQ92616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati257 – 29438HEAT 1Add
BLAST
Repeati295 – 33137HEAT 2Add
BLAST
Repeati460 – 50344HEAT 3Add
BLAST
Repeati1078 – 111538HEAT 4Add
BLAST
Repeati1290 – 133243HEAT 5Add
BLAST
Repeati1335 – 137238HEAT 6Add
BLAST
Repeati1455 – 149238HEAT 7Add
BLAST
Repeati1493 – 153038HEAT 8Add
BLAST
Repeati1534 – 157138HEAT 9Add
BLAST
Repeati1573 – 160937HEAT 10Add
BLAST
Repeati1611 – 164838HEAT 11Add
BLAST
Repeati1653 – 169038HEAT 12Add
BLAST
Repeati1773 – 181038HEAT 13Add
BLAST
Repeati1812 – 184837HEAT 14Add
BLAST
Repeati1921 – 195838HEAT 15Add
BLAST
Repeati1959 – 199638HEAT 16Add
BLAST
Repeati2001 – 203838HEAT 17Add
BLAST
Repeati2039 – 207638HEAT 18Add
BLAST
Repeati2188 – 222538HEAT 19Add
BLAST
Repeati2259 – 229638HEAT 20Add
BLAST
Repeati2339 – 238042HEAT 21Add
BLAST
Repeati2422 – 245938HEAT 22Add
BLAST
Repeati2560 – 258324HEAT 23Add
BLAST
Repeati2588 – 262538HEAT 24Add
BLAST

Sequence similaritiesi

Belongs to the GCN1 family.Curated
Contains 24 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG325174.
HOVERGENiHBG081550.
InParanoidiQ92616.
OMAiGLMELHM.
OrthoDBiEOG7H4DSM.
PhylomeDBiQ92616.
TreeFamiTF105398.

Family and domain databases

Gene3Di1.25.10.10. 8 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR022716. DUF3554.
IPR026827. ECM29/GCN1.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERiPTHR23346. PTHR23346. 1 hit.
PfamiPF12074. DUF3554. 1 hit.
[Graphical view]
SMARTiSM00185. ARM. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 7 hits.
PROSITEiPS50077. HEAT_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92616-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAADTQVSET LKRFAGKVTT ASVKERREIL SELGKCVAGK DLPEGAVKGL
60 70 80 90 100
CKLFCLTLHR YRDAASRRAL QAAIQQLAEA QPEATAKNLL HSLQSSGIGS
110 120 130 140 150
KAGVPSKSSG SAALLALTWT CLLVRIVFPS RAKRQGDIWN KLVEVQCLLL
160 170 180 190 200
LEVLGGSHKH AVDGAVKKLT KLWKENPGLV EQYLSAILSL EPNQNYAGML
210 220 230 240 250
GLLVQFCTSH KEMDVVSQHK SALLDFYMKN ILMSKVKPPK YLLDSCAPLL
260 270 280 290 300
RYLSHSEFKD LILPTIQKSL LRSPENVIET ISSLLASVTL DLSQYAMDIV
310 320 330 340 350
KGLAGHLKSN SPRLMDEAVL ALRNLARQCS DSSAMESLTK HLFAILGGSE
360 370 380 390 400
GKLTVVAQKM SVLSGIGSVS HHVVSGPSSQ VLNGIVAELF IPFLQQEVHE
410 420 430 440 450
GTLVHAVSVL ALWCNRFTME VPKKLTEWFK KAFSLKTSTS AVRHAYLQCM
460 470 480 490 500
LASYRGDTLL QALDLLPLLI QTVEKAASQS TQVPTITEGV AAALLLLKLS
510 520 530 540 550
VADSQAEAKL SSFWQLIVDE KKQVFTSEKF LVMASEDALC TVLHLTERLF
560 570 580 590 600
LDHPHRLTGN KVQQYHRALV AVLLSRTWHV RRQAQQTVRK LLSSLGGFKL
610 620 630 640 650
AHGLLEELKT VLSSHKVLPL EALVTDAGEV TEAGKAYVPP RVLQEALCVI
660 670 680 690 700
SGVPGLKGDV TDTEQLAQEM LIISHHPSLV AVQSGLWPAL LARMKIDPEA
710 720 730 740 750
FITRHLDQII PRMTTQSPLN QSSMNAMGSL SVLSPDRVLP QLISTITASV
760 770 780 790 800
QNPALRLVTR EEFAIMQTPA GELYDKSIIQ SAQQDSIKKA NMKRENKAYS
810 820 830 840 850
FKEQIIELEL KEEIKKKKGI KEEVQLTSKQ KEMLQAQLDR EAQVRRRLQE
860 870 880 890 900
LDGELEAALG LLDIILAKNP SGLTQYIPVL VDSFLPLLKS PLAAPRIKNP
910 920 930 940 950
FLSLAACVMP SRLKALGTLV SHVTLRLLKP ECVLDKSWCQ EELSVAVKRA
960 970 980 990 1000
VMLLHTHTIT SRVGKGEPGA APLSAPAFSL VFPFLKMVLT EMPHHSEEEE
1010 1020 1030 1040 1050
EWMAQILQIL TVQAQLRASP NTPPGRVDEN GPELLPRVAM LRLLTWVIGT
1060 1070 1080 1090 1100
GSPRLQVLAS DTLTTLCASS SGDDGCAFAE QEEVDVLLCA LQSPCASVRE
1110 1120 1130 1140 1150
TVLRGLMELH MVLPAPDTDE KNGLNLLRRL WVVKFDKEEE IRKLAERLWS
1160 1170 1180 1190 1200
MMGLDLQPDL CSLLIDDVIY HEAAVRQAGA EALSQAVARY QRQAAEVMGR
1210 1220 1230 1240 1250
LMEIYQEKLY RPPPVLDALG RVISESPPDQ WEARCGLALA LNKLSQYLDS
1260 1270 1280 1290 1300
SQVKPLFQFF VPDALNDRHP DVRKCMLDAA LATLNTHGKE NVNSLLPVFE
1310 1320 1330 1340 1350
EFLKNAPNDA SYDAVRQSVV VLMGSLAKHL DKSDPKVKPI VAKLIAALST
1360 1370 1380 1390 1400
PSQQVQESVA SCLPPLVPAI KEDAGGMIQR LMQQLLESDK YAERKGAAYG
1410 1420 1430 1440 1450
LAGLVKGLGI LSLKQQEMMA ALTDAIQDKK NFRRREGALF AFEMLCTMLG
1460 1470 1480 1490 1500
KLFEPYVVHV LPHLLLCFGD GNQYVREAAD DCAKAVMSNL SAHGVKLVLP
1510 1520 1530 1540 1550
SLLAALEEES WRTKAGSVEL LGAMAYCAPK QLSSCLPNIV PKLTEVLTDS
1560 1570 1580 1590 1600
HVKVQKAGQQ ALRQIGSVIR NPEILAIAPV LLDALTDPSR KTQKCLQTLL
1610 1620 1630 1640 1650
DTKFVHFIDA PSLALIMPIV QRAFQDRSTD TRKMAAQIIG NMYSLTDQKD
1660 1670 1680 1690 1700
LAPYLPSVTP GLKASLLDPV PEVRTVSAKA LGAMVKGMGE SCFEDLLPWL
1710 1720 1730 1740 1750
METLTYEQSS VDRSGAAQGL AEVMAGLGVE KLEKLMPEIV ATASKVDIAP
1760 1770 1780 1790 1800
HVRDGYIMMF NYLPITFGDK FTPYVGPIIP CILKALADEN EFVRDTALRA
1810 1820 1830 1840 1850
GQRVISMYAE TAIALLLPQL EQGLFDDLWR IRFSSVQLLG DLLFHISGVT
1860 1870 1880 1890 1900
GKMTTETASE DDNFGTAQSN KAIITALGVE RRNRVLAGLY MGRSDTQLVV
1910 1920 1930 1940 1950
RQASLHVWKI VVSNTPRTLR EILPTLFGLL LGFLASTCAD KRTIAARTLG
1960 1970 1980 1990 2000
DLVRKLGEKI LPEIIPILEE GLRSQKSDER QGVCIGLSEI MKSTSRDAVL
2010 2020 2030 2040 2050
YFSESLVPTA RKALCDPLEE VREAAAKTFE QLHSTIGHQA LEDILPFLLK
2060 2070 2080 2090 2100
QLDDEEVSEF ALDGLKQVMA IKSRVVLPYL VPKLTTPPVN TRVLAFLSSV
2110 2120 2130 2140 2150
AGDALTRHLG VILPAVMLAL KEKLGTPDEQ LEMANCQAVI LSVEDDTGHR
2160 2170 2180 2190 2200
IIIEYLLEAT RSPEVGMRQA AAIILNIYCS RSKADYTSHL RSLVSGLIRL
2210 2220 2230 2240 2250
FNDSSPVVLE ESWDALNAIT KKLDAGNQLA LIEELHKEIR LIGNESKGEH
2260 2270 2280 2290 2300
VPGFCLPKKG VTSILPVLRE GVLTGSPEQK EEAAKALGLV IRLTSADALR
2310 2320 2330 2340 2350
PSVVSITGPL IRILGDRFSW NVKAALLETL SLLLAKVGIA LKPFLPQLQT
2360 2370 2380 2390 2400
TFTKALQDSN RGVRLKAADA LGKLISIHIK VDPLFTELLN GIRAMEDPGV
2410 2420 2430 2440 2450
RDTMLQALRF VIQGAGAKVD AVIRKNIVSL LLSMLGHDED NTRISSAGCL
2460 2470 2480 2490 2500
GELCAFLTEE ELSAVLQQCL LADVSGIDWM VRHGRSLALS VAVNVAPGRL
2510 2520 2530 2540 2550
CAGRYSSDVQ EMILSSATAD RIPIAVSGVR GMGFLMRHHI ETGGGQLPAK
2560 2570 2580 2590 2600
LSSLFVKCLQ NPSSDIRLVA EKMIWWANKD PLPPLDPQAI KPILKALLDN
2610 2620 2630 2640 2650
TKDKNTVVRA YSDQAIVNLL KMRQGEEVFQ SLSKILDVAS LEVLNEVNRR
2660 2670
SLKKLASQAD STEQVDDTIL T
Length:2,671
Mass (Da):292,758
Last modified:May 18, 2010 - v6
Checksum:iFC34F50517DCC2A8
GO

Sequence cautioni

The sequence AAC51648.1 differs from that shown. Reason: Frameshift at position 2657.
The sequence BAA13209.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAC83183.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921L → F in BAA13209. (PubMed:9039502)Curated
Sequence conflicti292 – 2921L → F in AAI53882. (PubMed:15489334)Curated
Sequence conflicti842 – 8421A → G in AAC51648. (PubMed:9234705)Curated
Sequence conflicti1584 – 15841A → V in AAC51648. (PubMed:9234705)Curated
Sequence conflicti1683 – 16831A → V in AAC51648. (PubMed:9234705)Curated
Sequence conflicti1760 – 17601F → S in AAD00655. 1 PublicationCurated
Sequence conflicti2298 – 22981A → V in AAC51648. (PubMed:9234705)Curated
Sequence conflicti2486 – 24861S → T in AAD00655. 1 PublicationCurated
Sequence conflicti2549 – 25491A → R in AAC51648. (PubMed:9234705)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2155 – 21551Y → D.5 Publications
Corresponds to variant rs3864938 [ dbSNP | Ensembl ].
VAR_062228

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D86973 mRNA. Translation: BAA13209.2. Different initiation.
AC004812 Genomic DNA. Translation: AAC83183.1. Sequence problems.
BC021129 mRNA. Translation: AAH21129.1.
BC032335 mRNA. Translation: AAH32335.1.
BC046177 mRNA. Translation: AAH46177.1.
BC064346 mRNA. Translation: AAH64346.1.
BC153881 mRNA. Translation: AAI53882.1.
U88836 mRNA. Translation: AAD00655.1.
U88837 mRNA. Translation: AAD00656.1.
U77700 mRNA. Translation: AAC51648.1. Frameshift.
CCDSiCCDS41847.1.
RefSeqiNP_006827.1. NM_006836.1.
UniGeneiHs.298716.

Genome annotation databases

EnsembliENST00000300648; ENSP00000300648; ENSG00000089154.
GeneIDi10985.
KEGGihsa:10985.
UCSCiuc001txo.3. human.

Polymorphism databases

DMDMi296439506.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D86973 mRNA. Translation: BAA13209.2 . Different initiation.
AC004812 Genomic DNA. Translation: AAC83183.1 . Sequence problems.
BC021129 mRNA. Translation: AAH21129.1 .
BC032335 mRNA. Translation: AAH32335.1 .
BC046177 mRNA. Translation: AAH46177.1 .
BC064346 mRNA. Translation: AAH64346.1 .
BC153881 mRNA. Translation: AAI53882.1 .
U88836 mRNA. Translation: AAD00655.1 .
U88837 mRNA. Translation: AAD00656.1 .
U77700 mRNA. Translation: AAC51648.1 . Frameshift.
CCDSi CCDS41847.1.
RefSeqi NP_006827.1. NM_006836.1.
UniGenei Hs.298716.

3D structure databases

ProteinModelPortali Q92616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116181. 69 interactions.
IntActi Q92616. 28 interactions.
MINTi MINT-1144027.

PTM databases

PhosphoSitei Q92616.

Polymorphism databases

DMDMi 296439506.

Proteomic databases

MaxQBi Q92616.
PaxDbi Q92616.
PRIDEi Q92616.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300648 ; ENSP00000300648 ; ENSG00000089154 .
GeneIDi 10985.
KEGGi hsa:10985.
UCSCi uc001txo.3. human.

Organism-specific databases

CTDi 10985.
GeneCardsi GC12M120565.
HGNCi HGNC:4199. GCN1L1.
HPAi HPA018799.
HPA019648.
HPA024367.
MIMi 605614. gene.
neXtProti NX_Q92616.
PharmGKBi PA28616.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG325174.
HOVERGENi HBG081550.
InParanoidi Q92616.
OMAi GLMELHM.
OrthoDBi EOG7H4DSM.
PhylomeDBi Q92616.
TreeFami TF105398.

Miscellaneous databases

ChiTaRSi GCN1L1. human.
GeneWikii GCN1L1.
GenomeRNAii 10985.
NextBioi 41737.
PROi Q92616.
SOURCEi Search...

Gene expression databases

Bgeei Q92616.
ExpressionAtlasi Q92616. baseline and differential.
Genevestigatori Q92616.

Family and domain databases

Gene3Di 1.25.10.10. 8 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR022716. DUF3554.
IPR026827. ECM29/GCN1.
IPR021133. HEAT_type_2.
[Graphical view ]
PANTHERi PTHR23346. PTHR23346. 1 hit.
Pfami PF12074. DUF3554. 1 hit.
[Graphical view ]
SMARTi SM00185. ARM. 3 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 7 hits.
PROSITEi PS50077. HEAT_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY, VARIANT ASP-2155.
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ASP-2155.
    Tissue: Brain, Liver and Skin.
  5. Bienvenut W.V.
    Submitted (MAR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 69-87; 221-229; 241-251; 314-323; 568-576; 617-635; 822-829; 1201-1208; 1485-1496; 1604-1622; 1735-1745; 1960-1973; 2093-2107; 2151-2161; 2192-2199; 2402-2418 AND 2522-2530, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  6. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
    Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-359 AND 1678-2671, VARIANT ASP-2155.
  7. "Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2."
    Marton M.J., Vazquez de Aldana C.R., Qiu H., Chakraburtty K., Hinnebusch A.G.
    Mol. Cell. Biol. 17:4474-4489(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 842-2671, VARIANT ASP-2155.
    Tissue: Skeletal muscle.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGCN1L_HUMAN
AccessioniPrimary (citable) accession number: Q92616
Secondary accession number(s): A8KAY1
, O95001, O95651, Q6P2S3, Q86X65, Q8N5I5, Q8WU80, Q99736, Q9UE60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 129 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3