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P36915

- GNL1_HUMAN

UniProt

P36915 - GNL1_HUMAN

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Protein

Guanine nucleotide-binding protein-like 1

Gene

GNL1

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

Functioni

Possible regulatory or functional link with the histocompatibility cluster.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi225 – 2284GTPSequence Analysis
Nucleotide bindingi367 – 3748GTPSequence Analysis
Nucleotide bindingi411 – 4155GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: RefGenome
  2. GTP binding Source: UniProtKB
  3. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. GTP catabolic process Source: GOC
  3. ribosome biogenesis Source: RefGenome
  4. signal transduction Source: UniProtKB
  5. T cell mediated immunity Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein-like 1
Alternative name(s):
GTP-binding protein HSR1
Gene namesi
Name:GNL1
Synonyms:HSR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:4413. GNL1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. extracellular space Source: UniProtKB
  3. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Guanine nucleotide-binding protein-like 1PRO_0000122441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei33 – 331Phosphoserine1 Publication
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei48 – 481Phosphothreonine2 Publications
Modified residuei50 – 501Phosphothreonine2 Publications
Modified residuei51 – 511Phosphoserine2 Publications
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei324 – 3241Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36915.
PaxDbiP36915.
PRIDEiP36915.

Miscellaneous databases

PMAP-CutDBP36915.

Expressioni

Gene expression databases

BgeeiP36915.
CleanExiHS_GNL1.
ExpressionAtlasiP36915. baseline and differential.
GenevestigatoriP36915.

Organism-specific databases

HPAiCAB033575.
HPA043338.
HPA050455.

Interactioni

Protein-protein interaction databases

BioGridi109056. 10 interactions.
IntActiP36915. 3 interactions.
STRINGi9606.ENSP00000394290.

Structurei

3D structure databases

ProteinModelPortaliP36915.
SMRiP36915. Positions 363-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 418241CP-type GPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi551 – 60757Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.

Sequence similaritiesi

Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1161.
GeneTreeiENSGT00530000063453.
HOGENOMiHOG000007598.
HOVERGENiHBG005865.
InParanoidiP36915.
OMAiPNRFRLH.
PhylomeDBiP36915.
TreeFamiTF324569.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36915-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT
60 70 80 90 100
SDGESVTHHI RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA
110 120 130 140 150
REQVLQPVSA ELLELDIREV YQPGSVLDFP RRPPWSYEMS KEQLMSQEER
160 170 180 190 200
SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ LWRVLEMSDI VLLITDIRHP
210 220 230 240 250
VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH YFHQHYPQLH
260 270 280 290 300
VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
310 320 330 340 350
KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG
360 370 380 390 400
PTQERYKDGV VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT
410 420 430 440 450
YFLTPSVKLC DCPGLIFPSL LPRQLQVLAG IYPIAQIQEP YTAVGYLASR
460 470 480 490 500
IPVQALLHLR HPEAEDPSAE HPWCAWDICE AWAEKRGYKT AKAARNDVYR
510 520 530 540 550
AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV VLQGRVGPAG
560 570 580 590 600
DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA

LLGEDEC
Length:607
Mass (Da):68,661
Last modified:July 24, 2007 - v2
Checksum:iF8EBB4EDBB73D929
GO
Isoform 2 (identifier: P36915-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-177: Missing.
     178-183: WRQLWR → MEAAVA

Show »
Length:430
Mass (Da):47,306
Checksum:iDCCC3C4763631295
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2332PA → RR in AAA66492. (PubMed:8180467)Curated
Sequence conflicti315 – 3151Missing in AAA66492. (PubMed:8180467)Curated
Sequence conflicti339 – 3391E → EQ in AAA66492. (PubMed:8180467)Curated
Sequence conflicti514 – 5141L → V in AAA66492. (PubMed:8180467)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 177177Missing in isoform 2. 1 PublicationVSP_026992Add
BLAST
Alternative sequencei178 – 1836WRQLWR → MEAAVA in isoform 2. 1 PublicationVSP_026993

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25665 mRNA. Translation: AAA66492.1.
BT006648 mRNA. Translation: AAP35294.1.
AL662825 Genomic DNA. Translation: CAI17831.1.
AL662800 Genomic DNA. Translation: CAI18152.1.
BX000357 Genomic DNA. Translation: CAI18558.1.
BX248518 Genomic DNA. Translation: CAM26012.1.
CR388372 Genomic DNA. Translation: CAQ07868.1.
CR936927 Genomic DNA. Translation: CAQ08501.1.
BX927220 Genomic DNA. Translation: CAQ09053.1.
CH471081 Genomic DNA. Translation: EAX03294.1.
BC013959 mRNA. Translation: AAH13959.1.
BC018366 mRNA. Translation: AAH18366.1.
CCDSiCCDS4680.1. [P36915-1]
PIRiI57013.
RefSeqiNP_005266.2. NM_005275.3. [P36915-1]
XP_005249072.1. XM_005249015.1. [P36915-1]
XP_005272850.1. XM_005272793.1. [P36915-1]
XP_005274996.1. XM_005274939.1. [P36915-1]
XP_005275150.1. XM_005275093.1. [P36915-1]
XP_005275292.1. XM_005275235.1. [P36915-1]
XP_005275426.1. XM_005275369.1. [P36915-1]
XP_005275586.1. XM_005275529.1. [P36915-1]
UniGeneiHs.118354.
Hs.83147.

Genome annotation databases

EnsembliENST00000376621; ENSP00000365806; ENSG00000204590. [P36915-1]
ENST00000383596; ENSP00000373090; ENSG00000206492. [P36915-1]
ENST00000417834; ENSP00000403576; ENSG00000226882. [P36915-1]
ENST00000428189; ENSP00000409074; ENSG00000229470. [P36915-1]
ENST00000437917; ENSP00000411162; ENSG00000228581. [P36915-1]
ENST00000441604; ENSP00000394290; ENSG00000235986. [P36915-1]
ENST00000454829; ENSP00000409367; ENSG00000232143. [P36915-1]
GeneIDi2794.
KEGGihsa:2794.
UCSCiuc003nqh.3. human. [P36915-1]

Polymorphism databases

DMDMi158939140.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25665 mRNA. Translation: AAA66492.1 .
BT006648 mRNA. Translation: AAP35294.1 .
AL662825 Genomic DNA. Translation: CAI17831.1 .
AL662800 Genomic DNA. Translation: CAI18152.1 .
BX000357 Genomic DNA. Translation: CAI18558.1 .
BX248518 Genomic DNA. Translation: CAM26012.1 .
CR388372 Genomic DNA. Translation: CAQ07868.1 .
CR936927 Genomic DNA. Translation: CAQ08501.1 .
BX927220 Genomic DNA. Translation: CAQ09053.1 .
CH471081 Genomic DNA. Translation: EAX03294.1 .
BC013959 mRNA. Translation: AAH13959.1 .
BC018366 mRNA. Translation: AAH18366.1 .
CCDSi CCDS4680.1. [P36915-1 ]
PIRi I57013.
RefSeqi NP_005266.2. NM_005275.3. [P36915-1 ]
XP_005249072.1. XM_005249015.1. [P36915-1 ]
XP_005272850.1. XM_005272793.1. [P36915-1 ]
XP_005274996.1. XM_005274939.1. [P36915-1 ]
XP_005275150.1. XM_005275093.1. [P36915-1 ]
XP_005275292.1. XM_005275235.1. [P36915-1 ]
XP_005275426.1. XM_005275369.1. [P36915-1 ]
XP_005275586.1. XM_005275529.1. [P36915-1 ]
UniGenei Hs.118354.
Hs.83147.

3D structure databases

ProteinModelPortali P36915.
SMRi P36915. Positions 363-414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109056. 10 interactions.
IntActi P36915. 3 interactions.
STRINGi 9606.ENSP00000394290.

Polymorphism databases

DMDMi 158939140.

Proteomic databases

MaxQBi P36915.
PaxDbi P36915.
PRIDEi P36915.

Protocols and materials databases

DNASUi 2794.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376621 ; ENSP00000365806 ; ENSG00000204590 . [P36915-1 ]
ENST00000383596 ; ENSP00000373090 ; ENSG00000206492 . [P36915-1 ]
ENST00000417834 ; ENSP00000403576 ; ENSG00000226882 . [P36915-1 ]
ENST00000428189 ; ENSP00000409074 ; ENSG00000229470 . [P36915-1 ]
ENST00000437917 ; ENSP00000411162 ; ENSG00000228581 . [P36915-1 ]
ENST00000441604 ; ENSP00000394290 ; ENSG00000235986 . [P36915-1 ]
ENST00000454829 ; ENSP00000409367 ; ENSG00000232143 . [P36915-1 ]
GeneIDi 2794.
KEGGi hsa:2794.
UCSCi uc003nqh.3. human. [P36915-1 ]

Organism-specific databases

CTDi 2794.
GeneCardsi GC06M030509.
GC06Mj30498.
GC06Mk30499.
GC06Ml30553.
GC06Mm30587.
GC06Mn30498.
GC06Mo30500.
HGNCi HGNC:4413. GNL1.
HPAi CAB033575.
HPA043338.
HPA050455.
MIMi 143024. gene.
neXtProti NX_P36915.
PharmGKBi PA28792.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1161.
GeneTreei ENSGT00530000063453.
HOGENOMi HOG000007598.
HOVERGENi HBG005865.
InParanoidi P36915.
OMAi PNRFRLH.
PhylomeDBi P36915.
TreeFami TF324569.

Miscellaneous databases

ChiTaRSi GNL1. human.
GenomeRNAii 2794.
NextBioi 11009.
PMAP-CutDB P36915.
PROi P36915.
SOURCEi Search...

Gene expression databases

Bgeei P36915.
CleanExi HS_GNL1.
ExpressionAtlasi P36915. baseline and differential.
Genevestigatori P36915.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF01926. MMR_HSR1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS51721. G_CP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region."
    Vernet C., Ribouchon M.-T., Chimini G., Pontarotti P.
    Mamm. Genome 5:100-105(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: T-cell.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Muscle and Skin.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-34; THR-48; THR-50; SER-51 AND SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-48; THR-50 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGNL1_HUMAN
AccessioniPrimary (citable) accession number: P36915
Secondary accession number(s): B0S838, Q96CT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 24, 2007
Last modified: October 29, 2014
This is version 123 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3