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Protein

Aldo-keto reductase family 1 member B10

Gene

AKR1B10

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

Functioni

Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs.1 Publication

Enzyme regulationi

Inhibited by tolrestat.1 Publication

Kineticsi

  1. KM=600 µM for D,L-glyceraldehyde1 Publication
  2. KM=0.6 µM for all-trans-retinaldehyde1 Publication
  3. KM=0.7 µM for 9-cis-retinaldehyde1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441NADP1 Publication
Active sitei49 – 491Proton donor1 Publication
Sitei78 – 781Lowers pKa of active site TyrBy similarity
Binding sitei111 – 1111Substrate1 Publication
Binding sitei184 – 1841NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 223NADP1 Publication
Nucleotide bindingi160 – 1612NADP1 Publication
Nucleotide bindingi210 – 2178NADP1 Publication
Nucleotide bindingi261 – 27313NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  1. aldo-keto reductase (NADP) activity Source: UniProtKB
  2. geranylgeranyl reductase activity Source: UniProtKB
  3. indanol dehydrogenase activity Source: UniProtKB
  4. retinal dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. cellular aldehyde metabolic process Source: ProtInc
  2. daunorubicin metabolic process Source: UniProtKB
  3. digestion Source: ProtInc
  4. doxorubicin metabolic process Source: UniProtKB
  5. farnesol catabolic process Source: UniProtKB
  6. phototransduction, visible light Source: Reactome
  7. retinoid metabolic process Source: Reactome
  8. steroid metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.21. 2681.
ReactomeiREACT_24968. Retinoid metabolism and transport.
SABIO-RKO60218.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldo-keto reductase family 1 member B10 (EC:1.1.1.-)
Alternative name(s):
ARL-1
Aldose reductase-like
Aldose reductase-related protein
Short name:
ARP
Short name:
hARP
Small intestine reductase
Short name:
SI reductase
Gene namesi
Name:AKR1B10
Synonyms:AKR1B11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:382. AKR1B10.

Subcellular locationi

Lysosome 1 Publication. Secreted 1 Publication
Note: Secreted through a lysosome-mediated non-classical pathway.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251K → L: Increased affinity and reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication
Mutagenesisi301 – 3011V → L: Reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication

Organism-specific databases

PharmGKBiPA24676.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Aldo-keto reductase family 1 member B10PRO_0000124632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysine1 Publication
Modified residuei263 – 2631N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO60218.
PaxDbiO60218.
PRIDEiO60218.

2D gel databases

DOSAC-COBS-2DPAGEO60218.

PTM databases

PhosphoSiteiO60218.

Expressioni

Tissue specificityi

Found in many tissues. Highly expressed in small intestine, colon and adrenal gland.

Gene expression databases

BgeeiO60218.
CleanExiHS_AKR1B10.
GenevestigatoriO60218.

Organism-specific databases

HPAiCAB070163.
HPA020280.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACACAQ130854EBI-1572139,EBI-717681

Protein-protein interaction databases

BioGridi121325. 8 interactions.
IntActiO60218. 1 interaction.
STRINGi9606.ENSP00000352584.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi12 – 198Combined sources
Turni25 – 273Combined sources
Helixi28 – 3710Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 493Combined sources
Helixi52 – 6413Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 833Combined sources
Helixi86 – 10015Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi127 – 1315Combined sources
Helixi138 – 15013Combined sources
Beta strandi153 – 1619Combined sources
Helixi164 – 1718Combined sources
Beta strandi181 – 1866Combined sources
Helixi194 – 2029Combined sources
Beta strandi206 – 2116Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 2409Combined sources
Helixi245 – 25410Combined sources
Turni255 – 2573Combined sources
Helixi267 – 2748Combined sources
Helixi283 – 2908Combined sources
Helixi302 – 3043Combined sources
Beta strandi305 – 3073Combined sources
Helixi311 – 3133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUAX-ray1.25X1-316[»]
4GA8X-ray1.94A1-316[»]
4GABX-ray1.60A1-316[»]
4GQ0X-ray2.10A1-316[»]
4GQGX-ray1.92A1-316[»]
4I5XX-ray2.10A1-316[»]
4ICCX-ray1.75X1-316[»]
4JIHX-ray2.30A1-316[»]
4JIIX-ray2.20X1-316[»]
4WEVX-ray1.45X1-316[»]
ProteinModelPortaliO60218.
SMRiO60218. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60218.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiO60218.
KOiK00011.
OMAiVSNFSHF.
OrthoDBiEOG70KGQF.
PhylomeDBiO60218.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ
60 70 80 90 100
NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVR KAFEKTLKDL
110 120 130 140 150
KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD
160 170 180 190 200
EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC
210 220 230 240 250
HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI
260 270 280 290 300
RFHIQRNVIV IPKSVTPARI VENIQVFDFK LSDEEMATIL SFNRNWRACN
310
VLQSSHLEDY PFNAEY
Length:316
Mass (Da):36,020
Last modified:February 7, 2011 - v2
Checksum:i0C2FC0E798955A33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761V → A in AAO13380 (Ref. 3) Curated
Sequence conflicti100 – 1001L → P in AAO13380 (Ref. 3) Curated
Sequence conflicti288 – 2881T → I in AAO13380 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871P → S.
Corresponds to variant rs2303312 [ dbSNP | Ensembl ].
VAR_020077
Natural varianti286 – 2861M → T.
Corresponds to variant rs3735042 [ dbSNP | Ensembl ].
VAR_020078
Natural varianti313 – 3131N → D.7 Publications
Corresponds to variant rs4728329 [ dbSNP | Ensembl ].
VAR_013287

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37100 mRNA. Translation: AAC17469.1.
AF052577 mRNA. Translation: AAC36465.1.
AF524864 mRNA. Translation: AAO13380.1.
BT006794 mRNA. Translation: AAP35440.1.
CR541801 mRNA. Translation: CAG46600.1.
AC078847 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24069.1.
CH471070 Genomic DNA. Translation: EAW83816.1.
BC008837 mRNA. Translation: AAH08837.1.
AF044961 mRNA. Translation: AAC15671.1.
CCDSiCCDS5832.1.
RefSeqiNP_064695.3. NM_020299.4.
UniGeneiHs.116724.

Genome annotation databases

EnsembliENST00000359579; ENSP00000352584; ENSG00000198074.
GeneIDi57016.
KEGGihsa:57016.
UCSCiuc003vrr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37100 mRNA. Translation: AAC17469.1.
AF052577 mRNA. Translation: AAC36465.1.
AF524864 mRNA. Translation: AAO13380.1.
BT006794 mRNA. Translation: AAP35440.1.
CR541801 mRNA. Translation: CAG46600.1.
AC078847 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24069.1.
CH471070 Genomic DNA. Translation: EAW83816.1.
BC008837 mRNA. Translation: AAH08837.1.
AF044961 mRNA. Translation: AAC15671.1.
CCDSiCCDS5832.1.
RefSeqiNP_064695.3. NM_020299.4.
UniGeneiHs.116724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUAX-ray1.25X1-316[»]
4GA8X-ray1.94A1-316[»]
4GABX-ray1.60A1-316[»]
4GQ0X-ray2.10A1-316[»]
4GQGX-ray1.92A1-316[»]
4I5XX-ray2.10A1-316[»]
4ICCX-ray1.75X1-316[»]
4JIHX-ray2.30A1-316[»]
4JIIX-ray2.20X1-316[»]
4WEVX-ray1.45X1-316[»]
ProteinModelPortaliO60218.
SMRiO60218. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121325. 8 interactions.
IntActiO60218. 1 interaction.
STRINGi9606.ENSP00000352584.

Chemistry

BindingDBiO60218.
ChEMBLiCHEMBL5983.

PTM databases

PhosphoSiteiO60218.

2D gel databases

DOSAC-COBS-2DPAGEO60218.

Proteomic databases

MaxQBiO60218.
PaxDbiO60218.
PRIDEiO60218.

Protocols and materials databases

DNASUi57016.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359579; ENSP00000352584; ENSG00000198074.
GeneIDi57016.
KEGGihsa:57016.
UCSCiuc003vrr.3. human.

Organism-specific databases

CTDi57016.
GeneCardsiGC07P134212.
H-InvDBHIX0007102.
HIX0033661.
HGNCiHGNC:382. AKR1B10.
HPAiCAB070163.
HPA020280.
MIMi604707. gene.
neXtProtiNX_O60218.
PharmGKBiPA24676.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiO60218.
KOiK00011.
OMAiVSNFSHF.
OrthoDBiEOG70KGQF.
PhylomeDBiO60218.
TreeFamiTF106492.

Enzyme and pathway databases

BRENDAi1.1.1.21. 2681.
ReactomeiREACT_24968. Retinoid metabolism and transport.
SABIO-RKO60218.

Miscellaneous databases

EvolutionaryTraceiO60218.
GeneWikiiAKR1B10.
GenomeRNAii57016.
NextBioi62758.
PROiO60218.
SOURCEiSearch...

Gene expression databases

BgeeiO60218.
CleanExiHS_AKR1B10.
GenevestigatoriO60218.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel human aldose reductase-like gene."
    Cao D., Fan S.T., Chung S.S.M.
    J. Biol. Chem. 273:11429-11435(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-313.
    Tissue: Liver tumor.
  2. "Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family."
    Hyndman D.J., Flynn T.G.
    Biochim. Biophys. Acta 1399:198-202(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Small intestine.
  3. "Representational difference analysis based identification and full-length sequencing of a gene of the aldo-ketoreductase family strongly overexpressed in hepatocellular carcinoma."
    Heringlake S.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-313.
  4. "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 (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-313.
  5. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-313.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-313.
    Tissue: Pancreas.
  10. "New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma."
    Scuric Z., Stain S.C., Anderson W.F., Hwang J.-J.
    Hepatology 27:943-950(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 232-316, VARIANT ASP-313.
  11. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway."
    Luo D.X., Huang M.C., Ma J., Gao Z., Liao D.F., Cao D.
    Biochem. J. 438:71-80(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10."
    Gallego O., Ruiz F.X., Ardevol A., Dominguez M., Alvarez R., de Lera A.R., Rovira C., Farres J., Fita I., Pares X.
    Proc. Natl. Acad. Sci. U.S.A. 104:20764-20769(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH TOLRESTAT AND NADP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF LYS-125 AND VAL-301.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAK1BA_HUMAN
AccessioniPrimary (citable) accession number: O60218
Secondary accession number(s): A4D1P1
, O75890, Q6FHF3, Q8IWZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2002
Last sequence update: February 7, 2011
Last modified: March 31, 2015
This is version 136 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 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.