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P49448

- DHE4_HUMAN

UniProt

P49448 - DHE4_HUMAN

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Protein

Glutamate dehydrogenase 2, mitochondrial

Gene
GLUD2, GLUDP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate By similarity
Active sitei183 – 1831 By similarity

GO - Molecular functioni

  1. ADP binding Source: BHF-UCL
  2. glutamate dehydrogenase (NAD+) activity Source: UniProtKB
  3. glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
  4. GTP binding Source: BHF-UCL
  5. leucine binding Source: BHF-UCL

GO - Biological processi

  1. glutamate biosynthetic process Source: BHF-UCL
  2. glutamate catabolic process Source: BHF-UCL
  3. glutamate metabolic process Source: UniProtKB
  4. oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS00018-MONOMER.
BRENDAi1.4.1.3. 2681.
SABIO-RKP49448.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
Short name:
GDH 2
Gene namesi
Name:GLUD2
Synonyms:GLUDP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:4336. GLUD2.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 2, mitochondrialPRO_0000007208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysine By similarity
Modified residuei79 – 791Phosphoserine By similarity
Modified residuei84 – 841N6-acetyllysine; alternate By similarity
Modified residuei84 – 841N6-succinyllysine; alternate By similarity
Modified residuei110 – 1101N6-acetyllysine; alternate By similarity
Modified residuei110 – 1101N6-succinyllysine; alternate By similarity
Modified residuei128 – 1281Phosphoserine By similarity
Modified residuei135 – 1351Phosphotyrosine By similarity
Modified residuei162 – 1621N6-acetyllysine; alternate By similarity
Modified residuei162 – 1621N6-succinyllysine; alternate By similarity
Modified residuei171 – 1711N6-acetyllysine By similarity
Modified residuei172 – 1721ADP-ribosylcysteine
Modified residuei183 – 1831N6-acetyllysine; alternate By similarity
Modified residuei183 – 1831N6-succinyllysine; alternate By similarity
Modified residuei187 – 1871N6-acetyllysine By similarity
Modified residuei191 – 1911N6-acetyllysine; alternate By similarity
Modified residuei191 – 1911N6-succinyllysine; alternate By similarity
Modified residuei200 – 2001N6-succinyllysine By similarity
Modified residuei211 – 2111N6-acetyllysine By similarity
Modified residuei326 – 3261N6-acetyllysine By similarity
Modified residuei346 – 3461N6-acetyllysine; alternate By similarity
Modified residuei346 – 3461N6-succinyllysine; alternate By similarity
Modified residuei352 – 3521N6-acetyllysine; alternate By similarity
Modified residuei352 – 3521N6-succinyllysine; alternate By similarity
Modified residuei363 – 3631N6-acetyllysine; alternate By similarity
Modified residuei363 – 3631N6-succinyllysine; alternate By similarity
Modified residuei365 – 3651N6-acetyllysine; alternate By similarity
Modified residuei365 – 3651N6-succinyllysine; alternate By similarity
Modified residuei386 – 3861N6-acetyllysine By similarity
Modified residuei390 – 3901N6-acetyllysine; alternate By similarity
Modified residuei390 – 3901N6-succinyllysine; alternate By similarity
Modified residuei399 – 3991N6-acetyllysine By similarity
Modified residuei415 – 4151N6-acetyllysine; alternate By similarity
Modified residuei415 – 4151N6-succinyllysine; alternate By similarity
Modified residuei457 – 4571N6-acetyllysine; alternate By similarity
Modified residuei457 – 4571N6-succinyllysine; alternate By similarity
Modified residuei477 – 4771N6-acetyllysine; alternate By similarity
Modified residuei477 – 4771N6-succinyllysine; alternate By similarity
Modified residuei480 – 4801N6-acetyllysine; alternate By similarity
Modified residuei480 – 4801N6-succinyllysine; alternate By similarity
Modified residuei503 – 5031N6-acetyllysine; alternate By similarity
Modified residuei503 – 5031N6-succinyllysine; alternate By similarity
Modified residuei527 – 5271N6-acetyllysine; alternate By similarity
Modified residuei527 – 5271N6-succinyllysine; alternate By similarity
Modified residuei545 – 5451N6-acetyllysine; alternate By similarity
Modified residuei545 – 5451N6-succinyllysine; alternate By similarity
Modified residuei548 – 5481N6-acetyllysine By similarity

Post-translational modificationi

Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiP49448.
PaxDbiP49448.
PeptideAtlasiP49448.
PRIDEiP49448.

2D gel databases

REPRODUCTION-2DPAGEIPI00027146.

PTM databases

PhosphoSiteiP49448.

Expressioni

Tissue specificityi

Expressed in retina, testis and, at a lower level, brain.

Gene expression databases

ArrayExpressiP49448.
BgeeiP49448.
GenevestigatoriP49448.

Organism-specific databases

HPAiHPA042492.
HPA044839.

Interactioni

Subunit structurei

Homohexamer By similarity.

Protein-protein interaction databases

BioGridi109009. 4 interactions.
IntActiP49448. 4 interactions.
MINTiMINT-1411373.
STRINGi9606.ENSP00000327589.

Structurei

3D structure databases

ProteinModelPortaliP49448.
SMRiP49448. Positions 63-558.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP49448.
KOiK00261.
OMAiTMELCQK.
OrthoDBiEOG73NG50.
PhylomeDBiP49448.
TreeFamiTF313945.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49448-1 [UniParc]FASTAAdd to Basket

« Hide

MYRYLAKALL PSRAGPAALG SAANHSAALL GRGRGQPAAA SQPGLALAAR    50
RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN 100
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK 200
ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN 250
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR 300
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 350
FKLQHGSILG FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI 400
IAEGANGPTT PEADKIFLER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
YGRLTFKYER DSNYHLLLSV QESLERKFGK HGGTIPIVPT AEFQDSISGA 500
SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
SEAGVTFT 558
Length:558
Mass (Da):61,434
Last modified:April 27, 2001 - v2
Checksum:iF222B1B2CB74A6EA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti498 – 4981S → A.
Corresponds to variant rs9697983 [ dbSNP | Ensembl ].
VAR_048867

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 2861E → Q in CAA46995. 1 Publication
Sequence conflicti286 – 2861E → Q in AAA20969. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66310 Genomic DNA. Translation: CAA46995.1.
U08997 Genomic DNA. Translation: AAA20969.1.
AK313356 mRNA. Translation: BAG36157.1.
AC006144 Genomic DNA. Translation: AAD05030.1.
BC050732 mRNA. Translation: AAH50732.1.
CCDSiCCDS14603.1.
PIRiA53719.
RefSeqiNP_036216.2. NM_012084.3.
UniGeneiHs.368538.

Genome annotation databases

EnsembliENST00000328078; ENSP00000327589; ENSG00000182890.
GeneIDi2747.
KEGGihsa:2747.
UCSCiuc004eto.3. human.

Polymorphism databases

DMDMi13432152.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66310 Genomic DNA. Translation: CAA46995.1 .
U08997 Genomic DNA. Translation: AAA20969.1 .
AK313356 mRNA. Translation: BAG36157.1 .
AC006144 Genomic DNA. Translation: AAD05030.1 .
BC050732 mRNA. Translation: AAH50732.1 .
CCDSi CCDS14603.1.
PIRi A53719.
RefSeqi NP_036216.2. NM_012084.3.
UniGenei Hs.368538.

3D structure databases

ProteinModelPortali P49448.
SMRi P49448. Positions 63-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109009. 4 interactions.
IntActi P49448. 4 interactions.
MINTi MINT-1411373.
STRINGi 9606.ENSP00000327589.

Chemistry

DrugBanki DB00142. L-Glutamic Acid.
DB00157. NADH.

PTM databases

PhosphoSitei P49448.

Polymorphism databases

DMDMi 13432152.

2D gel databases

REPRODUCTION-2DPAGE IPI00027146.

Proteomic databases

MaxQBi P49448.
PaxDbi P49448.
PeptideAtlasi P49448.
PRIDEi P49448.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328078 ; ENSP00000327589 ; ENSG00000182890 .
GeneIDi 2747.
KEGGi hsa:2747.
UCSCi uc004eto.3. human.

Organism-specific databases

CTDi 2747.
GeneCardsi GC0XP120181.
HGNCi HGNC:4336. GLUD2.
HPAi HPA042492.
HPA044839.
MIMi 300144. gene.
neXtProti NX_P49448.
PharmGKBi PA28738.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0334.
HOGENOMi HOG000243801.
HOVERGENi HBG005479.
InParanoidi P49448.
KOi K00261.
OMAi TMELCQK.
OrthoDBi EOG73NG50.
PhylomeDBi P49448.
TreeFami TF313945.

Enzyme and pathway databases

BioCyci MetaCyc:HS00018-MONOMER.
BRENDAi 1.4.1.3. 2681.
SABIO-RK P49448.

Miscellaneous databases

GeneWikii GLUD2.
GenomeRNAii 2747.
NextBioi 10828.
PROi P49448.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49448.
Bgeei P49448.
Genevestigatori P49448.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene."
    Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A., Papamatheakis J., Plaitakis A.
    J. Biol. Chem. 269:16971-16976(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Retina.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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].
    Tissue: Skin.
  5. "Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes."
    Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.
    FEBS Lett. 579:4125-4130(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION AT CYS-172.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import."
    Kotzamani D., Plaitakis A.
    Neurochem. Int. 61:463-469(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDHE4_HUMAN
AccessioniPrimary (citable) accession number: P49448
Secondary accession number(s): B2R8G0, Q9UDQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 128 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 X
    Human chromosome X: 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

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