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Q6P6C2

- ALKB5_HUMAN

UniProt

Q6P6C2 - ALKB5_HUMAN

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Protein

RNA demethylase ALKBH5

Gene

ALKBH5

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

Functioni

Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export and is required for spermatogenesis.2 Publications

Cofactori

Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041Iron; catalyticCurated
Metal bindingi206 – 2061Iron; catalyticBy similarity
Metal bindingi266 – 2661Iron; catalyticCurated

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. oxidative RNA demethylase activity Source: UniProtKB
  3. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. mRNA export from nucleus Source: UniProtKB
  3. mRNA processing Source: UniProtKB
  4. oxidative single-stranded RNA demethylation Source: UniProtKB
  5. response to hypoxia Source: UniProtKB
  6. spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA demethylase ALKBH5 (EC:1.14.11.-)
Alternative name(s):
Alkylated DNA repair protein alkB homolog 5
Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5
Gene namesi
Name:ALKBH5
Synonyms:ABH5, OFOXD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:25996. ALKBH5.

Subcellular locationi

Nucleus speckle 2 Publications

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041H → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi266 – 2661H → A: Impaired catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA142671230.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 394393RNA demethylase ALKBH5PRO_0000239283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei64 – 641Phosphoserine2 Publications
Modified residuei69 – 691Phosphoserine1 Publication
Modified residuei71 – 711Phosphotyrosine1 Publication
Modified residuei132 – 1321N6-acetyllysine1 Publication
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei371 – 3711PhosphoserineBy similarity
Modified residuei374 – 3741Phosphoserine1 Publication
Modified residuei384 – 3841PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6P6C2.
PaxDbiQ6P6C2.
PRIDEiQ6P6C2.

PTM databases

PhosphoSiteiQ6P6C2.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in lung, followed by testis, pancreas, spleen and ovary.1 Publication

Inductioni

By hypoxia, directly activated by HIF1A. Expression is regulated by PRMT7.2 Publications

Gene expression databases

BgeeiQ6P6C2.
CleanExiHS_ALKBH5.
ExpressionAtlasiQ6P6C2. baseline and differential.
GenevestigatoriQ6P6C2.

Organism-specific databases

HPAiHPA007196.

Interactioni

Protein-protein interaction databases

BioGridi120237. 6 interactions.
IntActiQ6P6C2. 1 interaction.
STRINGi9606.ENSP00000382091.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 8612
Beta strandi89 – 935
Helixi97 – 11519
Helixi121 – 1233
Beta strandi124 – 1274
Beta strandi130 – 1378
Beta strandi139 – 1413
Beta strandi152 – 1554
Beta strandi160 – 1623
Helixi166 – 1716
Helixi173 – 1786
Beta strandi189 – 1957
Beta strandi201 – 2044
Turni208 – 2103
Beta strandi215 – 2195
Beta strandi224 – 2285
Helixi231 – 2333
Turni236 – 2383
Beta strandi243 – 2486
Beta strandi252 – 2565
Helixi258 – 2625
Beta strandi266 – 2683
Helixi270 – 2723
Beta strandi277 – 2837

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NJ4X-ray2.02A/B66-292[»]
4NRMX-ray2.17A66-292[»]
4NROX-ray2.30A66-292[»]
4NRPX-ray1.80A66-292[»]
4NRQX-ray2.50A66-292[»]
4O61X-ray1.90A/B74-294[»]
4O7XX-ray1.78A66-292[»]
4OCTX-ray2.28A/B74-294[»]
ProteinModelPortaliQ6P6C2.
SMRiQ6P6C2. Positions 70-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 11650Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 4819Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the alkB family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264303.
GeneTreeiENSGT00390000009298.
HOGENOMiHOG000007505.
HOVERGENiHBG080833.
InParanoidiQ6P6C2.
KOiK10767.
OMAiGAKRKYQ.
TreeFamiTF329212.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
[Graphical view]
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q6P6C2-2) [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
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP
60 70 80 90 100
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC
110 120 130 140 150
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP
160 170 180 190 200
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGGC
210 220 230 240 250
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR
260 270 280 290 300
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS
310 320 330 340 350
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS
360 370 380 390
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH
Length:394
Mass (Da):44,256
Last modified:October 3, 2012 - v2
Checksum:iDEB7BF8770BDB3A0
GO
Isoform 1 (identifier: Q6P6C2-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     386-394: ARKVKMRRH → GNSGSSLRSG...PPGWKGCWHQ

Note: No experimental confirmation available.

Show »
Length:467
Mass (Da):52,255
Checksum:iCAB456568C428C85
GO
Isoform 3 (identifier: Q6P6C2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MAAASGYTDLREKLKSMTSRDNYKAGSREAAA → MRRCWRPCPAGRGEGGGGRSP

Show »
Length:383
Mass (Da):43,049
Checksum:i45D8A30C0297A361
GO

Sequence cautioni

The sequence BAA91078.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → L in BAA91078. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232MAAAS…REAAA → MRRCWRPCPAGRGEGGGGRS P in isoform 3. 1 PublicationVSP_044226Add
BLAST
Alternative sequencei386 – 3949ARKVKMRRH → GNSGSSLRSGNSGSSLRSCP SFCFEGFVFVHWGVFVFCFL FFLILYIFPWFCCLLGLKNR IGQDLGSHILGIPPGWKGCW HQ in isoform 1. 1 PublicationVSP_019130

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK000315 mRNA. Translation: BAA91078.1. Different initiation.
AK301107 mRNA. Translation: BAG62706.1.
AC087164 Genomic DNA. No translation available.
AC109515 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55661.1.
CH471196 Genomic DNA. Translation: EAW55662.1.
BC062339 mRNA. Translation: AAH62339.1.
CCDSiCCDS42272.1. [Q6P6C2-2]
RefSeqiNP_060228.3. NM_017758.3. [Q6P6C2-2]
UniGeneiHs.744130.

Genome annotation databases

EnsembliENST00000399138; ENSP00000382091; ENSG00000091542. [Q6P6C2-2]
GeneIDi54890.
KEGGihsa:54890.
UCSCiuc010cpw.3. human. [Q6P6C2-2]

Polymorphism databases

DMDMi408359959.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK000315 mRNA. Translation: BAA91078.1 . Different initiation.
AK301107 mRNA. Translation: BAG62706.1 .
AC087164 Genomic DNA. No translation available.
AC109515 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55661.1 .
CH471196 Genomic DNA. Translation: EAW55662.1 .
BC062339 mRNA. Translation: AAH62339.1 .
CCDSi CCDS42272.1. [Q6P6C2-2 ]
RefSeqi NP_060228.3. NM_017758.3. [Q6P6C2-2 ]
UniGenei Hs.744130.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NJ4 X-ray 2.02 A/B 66-292 [» ]
4NRM X-ray 2.17 A 66-292 [» ]
4NRO X-ray 2.30 A 66-292 [» ]
4NRP X-ray 1.80 A 66-292 [» ]
4NRQ X-ray 2.50 A 66-292 [» ]
4O61 X-ray 1.90 A/B 74-294 [» ]
4O7X X-ray 1.78 A 66-292 [» ]
4OCT X-ray 2.28 A/B 74-294 [» ]
ProteinModelPortali Q6P6C2.
SMRi Q6P6C2. Positions 70-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120237. 6 interactions.
IntActi Q6P6C2. 1 interaction.
STRINGi 9606.ENSP00000382091.

PTM databases

PhosphoSitei Q6P6C2.

Polymorphism databases

DMDMi 408359959.

Proteomic databases

MaxQBi Q6P6C2.
PaxDbi Q6P6C2.
PRIDEi Q6P6C2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399138 ; ENSP00000382091 ; ENSG00000091542 . [Q6P6C2-2 ]
GeneIDi 54890.
KEGGi hsa:54890.
UCSCi uc010cpw.3. human. [Q6P6C2-2 ]

Organism-specific databases

CTDi 54890.
GeneCardsi GC17P018086.
HGNCi HGNC:25996. ALKBH5.
HPAi HPA007196.
MIMi 613303. gene.
neXtProti NX_Q6P6C2.
PharmGKBi PA142671230.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264303.
GeneTreei ENSGT00390000009298.
HOGENOMi HOG000007505.
HOVERGENi HBG080833.
InParanoidi Q6P6C2.
KOi K10767.
OMAi GAKRKYQ.
TreeFami TF329212.

Miscellaneous databases

GenomeRNAii 54890.
NextBioi 57883.
PROi Q6P6C2.
SOURCEi Search...

Gene expression databases

Bgeei Q6P6C2.
CleanExi HS_ALKBH5.
ExpressionAtlasi Q6P6C2. baseline and differential.
Genevestigatori Q6P6C2.

Family and domain databases

Gene3Di 2.60.120.590. 1 hit.
InterProi IPR027450. AlkB-like.
[Graphical view ]
Pfami PF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 2 AND 3).
    Tissue: Hepatoma and Spleen.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (ISOFORM 1).
    Tissue: Brain.
  5. "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.
  6. Cited for: TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-69 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  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 SER-64; TYR-71 AND SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1alpha (HIF-1alpha)."
    Thalhammer A., Bencokova Z., Poole R., Loenarz C., Adam J., O'Flaherty L., Schodel J., Mole D., Giaslakiotis K., Schofield C.J., Hammond E.M., Ratcliffe P.J., Pollard P.J.
    PLoS ONE 6:E16210-E16210(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  13. "Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1."
    Karkhanis V., Wang L., Tae S., Hu Y.J., Imbalzano A.N., Sif S.
    J. Biol. Chem. 287:29801-29814(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-204 AND HIS-266.

Entry informationi

Entry nameiALKB5_HUMAN
AccessioniPrimary (citable) accession number: Q6P6C2
Secondary accession number(s): B4DVJ4, D3DXC6, Q9NXD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 3, 2012
Last modified: October 29, 2014
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3