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Q14232

- EI2BA_HUMAN

UniProt

Q14232 - EI2BA_HUMAN

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Protein

Translation initiation factor eIF-2B subunit alpha

Gene

EIF2B1

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

Functioni

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.

GO - Molecular functioni

  1. enzyme regulator activity Source: Ensembl
  2. GDP binding Source: Ensembl
  3. GTP binding Source: Ensembl
  4. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to stimulus Source: UniProtKB
  3. gene expression Source: Reactome
  4. negative regulation of translational initiation in response to stress Source: Ensembl
  5. oligodendrocyte development Source: UniProtKB
  6. positive regulation of GTPase activity Source: GOC
  7. regulation of translational initiation Source: RefGenome
  8. response to glucose Source: UniProtKB
  9. response to heat Source: UniProtKB
  10. response to peptide hormone Source: UniProtKB
  11. translation Source: Reactome
  12. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1815. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit alpha
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit alpha
Gene namesi
Name:EIF2B1
Synonyms:EIF2BA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:3257. EIF2B1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic translation initiation factor 2B complex Source: UniProtKB
  4. membrane Source: MGI
  5. plasma membrane Source: MGI
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831V → F in VWM. 1 Publication
VAR_068450
Natural varianti208 – 2081N → Y in VWM. 1 Publication
VAR_015404

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi603896. phenotype.
Orphaneti157713. Congenital or early infantile CACH syndrome.
99854. Cree leukoencephalopathy.
157719. Juvenile or adult CACH syndrome.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBiPA27688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Translation initiation factor eIF-2B subunit alphaPRO_0000156055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14232.
PaxDbiQ14232.
PRIDEiQ14232.

PTM databases

PhosphoSiteiQ14232.

Expressioni

Gene expression databases

BgeeiQ14232.
CleanExiHS_EIF2B1.
ExpressionAtlasiQ14232. baseline and differential.
GenevestigatoriQ14232.

Organism-specific databases

HPAiCAB034258.
HPA049509.

Interactioni

Subunit structurei

Complex of five different subunits; alpha, beta, gamma, delta and epsilon.

Binary interactionsi

WithEntry#Exp.IntActNotes
Adra2aQ013382EBI-491065,EBI-491073From a different organism.
Adra2bP305452EBI-491065,EBI-491084From a different organism.

Protein-protein interaction databases

BioGridi108286. 27 interactions.
IntActiQ14232. 19 interactions.
MINTiMINT-1412710.
STRINGi9606.ENSP00000228958.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Helixi22 – 3413
Helixi44 – 5411
Turni55 – 595
Helixi63 – 7513
Helixi92 – 10413
Helixi107 – 1159
Helixi116 – 1183
Beta strandi123 – 1275
Helixi132 – 14211
Turni143 – 1453
Beta strandi148 – 1536
Turni156 – 1594
Helixi160 – 16910
Turni170 – 1723
Beta strandi175 – 1784
Helixi180 – 1823
Helixi183 – 1864
Helixi187 – 1893
Beta strandi191 – 1966
Beta strandi198 – 2003
Beta strandi206 – 2094
Helixi212 – 22110
Beta strandi226 – 2294
Helixi232 – 2343
Helixi243 – 2453
Helixi248 – 2503
Beta strandi272 – 2765
Helixi278 – 2803
Beta strandi282 – 2865
Beta strandi289 – 2913
Helixi293 – 2953
Helixi296 – 3049

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ECSX-ray2.65A/B/C/D/E/F/G/H1-305[»]
ProteinModelPortaliQ14232.
SMRiQ14232. Positions 1-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14232.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1184.
GeneTreeiENSGT00550000074853.
HOGENOMiHOG000175731.
HOVERGENiHBG051457.
InParanoidiQ14232.
KOiK03239.
OMAiTESHKFV.
OrthoDBiEOG7VHSZ3.
PhylomeDBiQ14232.
TreeFamiTF101505.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14232-1) [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
MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT
60 70 80 90 100
SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF
110 120 130 140 150
LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV
160 170 180 190 200
YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV
210 220 230 240 250
VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF
260 270 280 290 300
KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL

IKLYL
Length:305
Mass (Da):33,712
Last modified:November 1, 1997 - v1
Checksum:i91A915FF1B80B780
GO
Isoform 2 (identifier: Q14232-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-222: KKMAKALCHL...NQMAVCAKAQ → QVPFCSVMCP...ITEFAAGRSI
     223-305: Missing.

Note: No experimental confirmation available.

Show »
Length:222
Mass (Da):24,618
Checksum:i12DDBDF049B4D351
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831V → F in VWM. 1 Publication
VAR_068450
Natural varianti208 – 2081N → Y in VWM. 1 Publication
VAR_015404

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei162 – 22261KKMAK…CAKAQ → QVPFCSVMCPAIILQSKLRI TVQQDQNQNVPPACQQSALP FIVPFPAFGRKITEFAAGRS I in isoform 2. 1 PublicationVSP_055469Add
BLAST
Alternative sequencei223 – 30583Missing in isoform 2. 1 PublicationVSP_055470Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95648 mRNA. Translation: CAA64950.1.
AK294815 mRNA. Translation: BAG57931.1.
CR456831 mRNA. Translation: CAG33112.1.
AC117503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98424.1.
BC103763 mRNA. Translation: AAI03764.1.
BC104188 mRNA. Translation: AAI04189.1.
BC104189 mRNA. Translation: AAI04190.1.
CCDSiCCDS31924.1. [Q14232-1]
RefSeqiNP_001405.1. NM_001414.3. [Q14232-1]
UniGeneiHs.741273.

Genome annotation databases

EnsembliENST00000424014; ENSP00000416250; ENSG00000111361. [Q14232-1]
ENST00000537073; ENSP00000444183; ENSG00000111361. [Q14232-2]
GeneIDi1967.
KEGGihsa:1967.
UCSCiuc001ufm.3. human. [Q14232-1]

Polymorphism databases

DMDMi2494303.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Mendelian genes eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa (EIF2B1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95648 mRNA. Translation: CAA64950.1 .
AK294815 mRNA. Translation: BAG57931.1 .
CR456831 mRNA. Translation: CAG33112.1 .
AC117503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98424.1 .
BC103763 mRNA. Translation: AAI03764.1 .
BC104188 mRNA. Translation: AAI04189.1 .
BC104189 mRNA. Translation: AAI04190.1 .
CCDSi CCDS31924.1. [Q14232-1 ]
RefSeqi NP_001405.1. NM_001414.3. [Q14232-1 ]
UniGenei Hs.741273.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ECS X-ray 2.65 A/B/C/D/E/F/G/H 1-305 [» ]
ProteinModelPortali Q14232.
SMRi Q14232. Positions 1-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108286. 27 interactions.
IntActi Q14232. 19 interactions.
MINTi MINT-1412710.
STRINGi 9606.ENSP00000228958.

PTM databases

PhosphoSitei Q14232.

Polymorphism databases

DMDMi 2494303.

Proteomic databases

MaxQBi Q14232.
PaxDbi Q14232.
PRIDEi Q14232.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000424014 ; ENSP00000416250 ; ENSG00000111361 . [Q14232-1 ]
ENST00000537073 ; ENSP00000444183 ; ENSG00000111361 . [Q14232-2 ]
GeneIDi 1967.
KEGGi hsa:1967.
UCSCi uc001ufm.3. human. [Q14232-1 ]

Organism-specific databases

CTDi 1967.
GeneCardsi GC12M124105.
GeneReviewsi EIF2B1.
HGNCi HGNC:3257. EIF2B1.
HPAi CAB034258.
HPA049509.
MIMi 603896. phenotype.
606686. gene.
neXtProti NX_Q14232.
Orphaneti 157713. Congenital or early infantile CACH syndrome.
99854. Cree leukoencephalopathy.
157719. Juvenile or adult CACH syndrome.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBi PA27688.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1184.
GeneTreei ENSGT00550000074853.
HOGENOMi HOG000175731.
HOVERGENi HBG051457.
InParanoidi Q14232.
KOi K03239.
OMAi TESHKFV.
OrthoDBi EOG7VHSZ3.
PhylomeDBi Q14232.
TreeFami TF101505.

Enzyme and pathway databases

Reactomei REACT_1815. Recycling of eIF2:GDP.

Miscellaneous databases

EvolutionaryTracei Q14232.
GeneWikii EIF2B1.
GenomeRNAii 1967.
NextBioi 35471864.
PROi Q14232.
SOURCEi Search...

Gene expression databases

Bgeei Q14232.
CleanExi HS_EIF2B1.
ExpressionAtlasi Q14232. baseline and differential.
Genevestigatori Q14232.

Family and domain databases

InterProi IPR000649. IF-2B-related.
[Graphical view ]
Pfami PF01008. IF-2B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Torp A.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Brain.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter."
    van der Knaap M.S., Leegwater P.A.J., Koenst A.A.M., Visser A., Naidu S., Oudejans C.B.M., Schutgens R.B.H., Pronk J.C.
    Ann. Neurol. 51:264-270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VWM TYR-208.
  11. "Identification of ten novel mutations in patients with eIF2B-related disorders."
    Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F., Kohlschutter A., Gartner J.
    Hum. Mutat. 25:411-411(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VWM PHE-183.

Entry informationi

Entry nameiEI2BA_HUMAN
AccessioniPrimary (citable) accession number: Q14232
Secondary accession number(s): A6NLY9, B4DGX0, Q3SXP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 123 of the entry and version 1 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3