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P36915 (GNL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein-like 1
Alternative name(s):
GTP-binding protein HSR1
Gene names
Name:GNL1
Synonyms:HSR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possible regulatory or functional link with the histocompatibility cluster.

Domain

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 similarities

Belongs to the MMR1/HSR1 GTP-binding protein family.

Contains 1 G (guanine nucleotide-binding) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36915-1)

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.
Isoform 2 (identifier: P36915-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Guanine nucleotide-binding protein-like 1
PRO_0000122441

Regions

Domain372 – 41948G
Nucleotide binding225 – 2284GTP Potential
Nucleotide binding367 – 3748GTP Potential
Nucleotide binding411 – 4155GTP Potential
Compositional bias551 – 60757Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue321Phosphoserine Ref.8
Modified residue331Phosphoserine Ref.8
Modified residue341Phosphoserine Ref.8
Modified residue481Phosphothreonine Ref.8 Ref.9
Modified residue501Phosphothreonine Ref.8 Ref.9
Modified residue511Phosphoserine Ref.8 Ref.9
Modified residue681Phosphoserine Ref.7
Modified residue3241Phosphoserine Ref.8 Ref.12

Natural variations

Alternative sequence1 – 177177Missing in isoform 2.
VSP_026992
Alternative sequence178 – 1836WRQLWR → MEAAVA in isoform 2.
VSP_026993

Experimental info

Sequence conflict232 – 2332PA → RR in AAA66492. Ref.1
Sequence conflict3151Missing in AAA66492. Ref.1
Sequence conflict3391E → EQ in AAA66492. Ref.1
Sequence conflict5141L → V in AAA66492. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: F8EBB4EDBB73D929

FASTA60768,661
        10         20         30         40         50         60 
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI 

        70         80         90        100        110        120 
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA ELLELDIREV 

       130        140        150        160        170        180 
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ 

       190        200        210        220        230        240 
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH 

       250        260        270        280        290        300 
YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG 

       310        320        330        340        350        360 
KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG PTQERYKDGV 

       370        380        390        400        410        420 
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL 

       430        440        450        460        470        480 
LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE 

       490        500        510        520        530        540 
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV 

       550        560        570        580        590        600 
VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA 


LLGEDEC 

« Hide

Isoform 2 [UniParc].

Checksum: DCCC3C4763631295
Show »

FASTA43047,306

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4680.1. [P36915-1]
PIRI57013.
RefSeqNP_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]
UniGeneHs.118354.
Hs.83147.

3D structure databases

ProteinModelPortalP36915.
SMRP36915. Positions 363-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109056. 9 interactions.
IntActP36915. 3 interactions.
STRING9606.ENSP00000394290.

Polymorphism databases

DMDM158939140.

Proteomic databases

MaxQBP36915.
PaxDbP36915.
PRIDEP36915.

Protocols and materials databases

DNASU2794.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376621; 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]
GeneID2794.
KEGGhsa:2794.
UCSCuc003nqh.3. human. [P36915-1]

Organism-specific databases

CTD2794.
GeneCardsGC06M030509.
GC06Mj30498.
GC06Mk30499.
GC06Ml30553.
GC06Mm30587.
GC06Mn30498.
GC06Mo30500.
HGNCHGNC:4413. GNL1.
HPACAB033575.
HPA043338.
HPA050455.
MIM143024. gene.
neXtProtNX_P36915.
PharmGKBPA28792.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1161.
HOGENOMHOG000007598.
HOVERGENHBG005865.
InParanoidP36915.
OMAPNRFRLH.
PhylomeDBP36915.
TreeFamTF324569.

Gene expression databases

ArrayExpressP36915.
BgeeP36915.
CleanExHS_GNL1.
GenevestigatorP36915.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSGNL1. human.
GenomeRNAi2794.
NextBio11009.
PMAP-CutDBP36915.
PROP36915.
SOURCESearch...

Entry information

Entry nameGNL1_HUMAN
AccessionPrimary (citable) accession number: P36915
Secondary accession number(s): B0S838, Q96CT5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM