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P15104

- GLNA_HUMAN

UniProt

P15104 - GLNA_HUMAN

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Protein
Glutamine synthetase
Gene
GLUL, GLNS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner By similarity. Essential for proliferation of fetal skin fibroblasts.1 Publication

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Biotin By similarity.
Magnesium or manganese By similarity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate binding Source: Ensembl
  3. glutamate decarboxylase activity Source: UniProtKB-EC
  4. glutamate-ammonia ligase activity Source: Reactome
  5. identical protein binding Source: IntAct
  6. magnesium ion binding Source: Ensembl
  7. manganese ion binding Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular amino acid biosynthetic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. glutamate catabolic process Source: BHF-UCL
  5. glutamine biosynthetic process Source: BHF-UCL
  6. neurotransmitter uptake Source: Reactome
  7. positive regulation of epithelial cell proliferation Source: Ensembl
  8. positive regulation of insulin secretion Source: Ensembl
  9. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  10. protein homooligomerization Source: Ensembl
  11. response to glucose Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06066-MONOMER.
ReactomeiREACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RKP15104.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
Gene namesi
Name:GLUL
Synonyms:GLNS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4341. GLUL.

Subcellular locationi

Cytoplasm. Mitochondrion By similarity

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: UniProtKB-SubCell
  6. nucleus Source: UniProt
  7. perikaryon Source: Ensembl
  8. protein complex Source: Ensembl
  9. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Congenital systemic glutamine deficiency (CSGD) [MIM:610015]: Rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
VAR_026560
Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
VAR_026561

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610015. phenotype.
Orphaneti71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
PharmGKBiPA28743.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 373372Glutamine synthetase
PRO_0000153139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei104 – 1041Phosphotyrosine By similarity

Post-translational modificationi

Ubiquitinated by ZNRF1 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15104.
PaxDbiP15104.
PeptideAtlasiP15104.
PRIDEiP15104.

2D gel databases

REPRODUCTION-2DPAGEIPI00010130.
UCD-2DPAGEP15104.

PTM databases

PhosphoSiteiP15104.

Expressioni

Developmental stagei

Expressed during early fetal stages.1 Publication

Inductioni

By glucocorticoids. Vitamin D and the Wnt signaling pathway inhibit its expression and activity.1 Publication

Gene expression databases

ArrayExpressiP15104.
BgeeiP15104.
CleanExiHS_GLUL.
GenevestigatoriP15104.

Organism-specific databases

HPAiCAB008636.
HPA007316.
HPA007571.

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-746653,EBI-746653

Protein-protein interaction databases

BioGridi109014. 20 interactions.
DIPiDIP-308N.
IntActiP15104. 18 interactions.
MINTiMINT-1183856.
STRINGi9606.ENSP00000307900.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84
Helixi11 – 188
Beta strandi26 – 338
Beta strandi40 – 4910
Helixi54 – 563
Beta strandi60 – 634
Turni64 – 685
Beta strandi69 – 713
Helixi72 – 743
Beta strandi76 – 8611
Turni88 – 903
Beta strandi95 – 1028
Beta strandi106 – 1083
Helixi114 – 12310
Helixi124 – 1274
Beta strandi130 – 14011
Beta strandi144 – 1463
Beta strandi158 – 1603
Turni167 – 1693
Helixi173 – 18614
Beta strandi190 – 1956
Beta strandi201 – 21010
Helixi213 – 23220
Beta strandi235 – 2373
Beta strandi245 – 2473
Beta strandi251 – 2577
Helixi259 – 2624
Turni264 – 2663
Helixi267 – 27812
Helixi281 – 2877
Turni290 – 2956
Helixi296 – 2983
Beta strandi314 – 3163
Beta strandi321 – 3255
Helixi327 – 3326
Beta strandi337 – 3393
Helixi348 – 35912

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OJWX-ray2.05A/B/C/D/E5-365[»]
2QC8X-ray2.60A/B/C/D/E/F/G/H/I/J5-365[»]
ProteinModelPortaliP15104.
SMRiP15104. Positions 10-365.

Miscellaneous databases

EvolutionaryTraceiP15104.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiP15104.
KOiK01915.
OMAiRIPRNVG.
OrthoDBiEOG7CZK5G.
PhylomeDBiP15104.
TreeFamiTF300491.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15104-1 [UniParc]FASTAAdd to Basket

« Hide

MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE    50
PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE 100
VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP 150
SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA 200
QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA 250
GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL 300
TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS 350
VTEALIRTCL LNETGDEPFQ YKN 373
Length:373
Mass (Da):42,064
Last modified:January 23, 2007 - v4
Checksum:i45390C100924FAF3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
VAR_026560
Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
VAR_026561

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → Y in AAH31964. 1 Publication
Sequence conflicti154 – 1541F → L in CAD97626. 1 Publication
Sequence conflicti155 – 1551P → T in AAH31964. 1 Publication
Sequence conflicti314 – 3141A → G in CAA68457. 1 Publication
Sequence conflicti322 – 3232SI → RL in CAA42495. 1 Publication
Sequence conflicti347 – 3471D → E in CAA42495. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00387 mRNA. Translation: CAA68457.1.
X59834 mRNA. Translation: CAA42495.1.
S70290 mRNA. Translation: AAB30693.1.
AY486122 mRNA. Translation: AAS57904.1.
AY486123 Genomic DNA. Translation: AAS57905.1.
BX537384 mRNA. Translation: CAD97626.1.
AL139344 Genomic DNA. Translation: CAI19842.1.
BC010037 mRNA. Translation: AAH10037.1.
BC011700 mRNA. Translation: AAH11700.1.
BC011852 mRNA. Translation: AAH11852.1.
BC018992 mRNA. Translation: AAH18992.1.
BC031964 mRNA. Translation: AAH31964.1.
BC051726 mRNA. Translation: AAH51726.1.
CCDSiCCDS1344.1.
PIRiS18455. AJHUQ.
RefSeqiNP_001028216.1. NM_001033044.2.
NP_001028228.1. NM_001033056.2.
NP_002056.2. NM_002065.5.
XP_006711341.1. XM_006711278.1.
UniGeneiHs.518525.

Genome annotation databases

EnsembliENST00000311223; ENSP00000307900; ENSG00000135821.
ENST00000331872; ENSP00000356537; ENSG00000135821.
ENST00000339526; ENSP00000344958; ENSG00000135821.
ENST00000417584; ENSP00000398320; ENSG00000135821.
GeneIDi2752.
KEGGihsa:2752.
UCSCiuc001gpa.2. human.

Cross-referencesi

Web resourcesi

Wikipedia

Glutamine synthetase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00387 mRNA. Translation: CAA68457.1 .
X59834 mRNA. Translation: CAA42495.1 .
S70290 mRNA. Translation: AAB30693.1 .
AY486122 mRNA. Translation: AAS57904.1 .
AY486123 Genomic DNA. Translation: AAS57905.1 .
BX537384 mRNA. Translation: CAD97626.1 .
AL139344 Genomic DNA. Translation: CAI19842.1 .
BC010037 mRNA. Translation: AAH10037.1 .
BC011700 mRNA. Translation: AAH11700.1 .
BC011852 mRNA. Translation: AAH11852.1 .
BC018992 mRNA. Translation: AAH18992.1 .
BC031964 mRNA. Translation: AAH31964.1 .
BC051726 mRNA. Translation: AAH51726.1 .
CCDSi CCDS1344.1.
PIRi S18455. AJHUQ.
RefSeqi NP_001028216.1. NM_001033044.2.
NP_001028228.1. NM_001033056.2.
NP_002056.2. NM_002065.5.
XP_006711341.1. XM_006711278.1.
UniGenei Hs.518525.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OJW X-ray 2.05 A/B/C/D/E 5-365 [» ]
2QC8 X-ray 2.60 A/B/C/D/E/F/G/H/I/J 5-365 [» ]
ProteinModelPortali P15104.
SMRi P15104. Positions 10-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109014. 20 interactions.
DIPi DIP-308N.
IntActi P15104. 18 interactions.
MINTi MINT-1183856.
STRINGi 9606.ENSP00000307900.

Chemistry

BindingDBi P15104.
ChEMBLi CHEMBL4612.
DrugBanki DB00023. Asparaginase.
DB00142. L-Glutamic Acid.
DB00130. L-Glutamine.
DB00134. L-Methionine.

PTM databases

PhosphoSitei P15104.

2D gel databases

REPRODUCTION-2DPAGE IPI00010130.
UCD-2DPAGE P15104.

Proteomic databases

MaxQBi P15104.
PaxDbi P15104.
PeptideAtlasi P15104.
PRIDEi P15104.

Protocols and materials databases

DNASUi 2752.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311223 ; ENSP00000307900 ; ENSG00000135821 .
ENST00000331872 ; ENSP00000356537 ; ENSG00000135821 .
ENST00000339526 ; ENSP00000344958 ; ENSG00000135821 .
ENST00000417584 ; ENSP00000398320 ; ENSG00000135821 .
GeneIDi 2752.
KEGGi hsa:2752.
UCSCi uc001gpa.2. human.

Organism-specific databases

CTDi 2752.
GeneCardsi GC01M182350.
HGNCi HGNC:4341. GLUL.
HPAi CAB008636.
HPA007316.
HPA007571.
MIMi 138290. gene.
610015. phenotype.
neXtProti NX_P15104.
Orphaneti 71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
PharmGKBi PA28743.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0174.
HOGENOMi HOG000061500.
HOVERGENi HBG005847.
InParanoidi P15104.
KOi K01915.
OMAi RIPRNVG.
OrthoDBi EOG7CZK5G.
PhylomeDBi P15104.
TreeFami TF300491.

Enzyme and pathway databases

BioCyci MetaCyc:HS06066-MONOMER.
Reactomei REACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RK P15104.

Miscellaneous databases

ChiTaRSi GLUL. human.
EvolutionaryTracei P15104.
GenomeRNAii 2752.
NextBioi 10840.
PROi P15104.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15104.
Bgeei P15104.
CleanExi HS_GLUL.
Genevestigatori P15104.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi IPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Overexpression of glutamine synthetase in human primary liver cancer."
    Christa L., Simon M.T., Flinois J.P., Gebhardt R., Brechot C., Lasserre C.
    Gastroenterology 106:1312-1320(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. Haberle J., Koch H.G.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain, Colon, Eye, Muscle and Testis.
  8. "Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase."
    Boksha I.S., Schonfeld H.J., Langen H., Muller F., Tereshkina E.B., Burbaeva G.S.H.
    Biochemistry (Mosc.) 67:1012-1020(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain.
  9. "Glutamine synthetase is essential for proliferation of fetal skin fibroblasts."
    Vermeulen T., Goerg B., Vogl T., Wolf M., Varga G., Toutain A., Paul R., Schliess F., Haeussinger D., Haeberle J.
    Arch. Biochem. Biophys. 478:96-102(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  10. "Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells."
    Olkku A., Mahonen A.
    Bone 43:483-493(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS CSGD CYS-324 AND CYS-341, CHARACTERIZATION OF VARIANTS CSGD CYS-324 AND CYS-341.

Entry informationi

Entry nameiGLNA_HUMAN
AccessioniPrimary (citable) accession number: P15104
Secondary accession number(s): Q499Y9
, Q5T9Z1, Q7Z3W4, Q8IZ17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 161 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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