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O60218

- AK1BA_HUMAN

UniProt

O60218 - AK1BA_HUMAN

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Protein
Aldo-keto reductase family 1 member B10
Gene
AKR1B10, AKR1B11
Organism
Homo sapiens (Human)
Status
Reviewed - 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-retinaldehyde
  3. KM=0.7 µM for 9-cis-retinaldehyde

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441NADP
Active sitei49 – 491Proton donor
Sitei78 – 781Lowers pKa of active site Tyr By similarity
Binding sitei111 – 1111Substrate
Binding sitei184 – 1841NADP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 223NADP
Nucleotide bindingi160 – 1612NADP
Nucleotide bindingi210 – 2178NADP
Nucleotide bindingi261 – 27313NADP
Add
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. protein binding Source: IntAct
  5. 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

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: Chromosome 7

Organism-specific databases

HGNCiHGNC:382. AKR1B10.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  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 B10
PRO_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

HPAiHPA020280.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi121325. 3 interactions.
IntActiO60218. 1 interaction.
STRINGi9606.ENSP00000352584.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliO60218.
SMRiO60218. Positions 1-316.

Miscellaneous databases

EvolutionaryTraceiO60218.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiO60218.
KOiK00011.
OMAiTSKLWLQ.
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

MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ    50
NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVR KAFEKTLKDL 100
KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD 150
EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC 200
HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI 250
RFHIQRNVIV IPKSVTPARI VENIQVFDFK LSDEEMATIL SFNRNWRACN 300
VLQSSHLEDY PFNAEY 316
Length:316
Mass (Da):36,020
Last modified:February 8, 2011 - v2
Checksum:i0C2FC0E798955A33
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761V → A in AAO13380. 1 Publication
Sequence conflicti100 – 1001L → P in AAO13380. 1 Publication
Sequence conflicti288 – 2881T → I in AAO13380. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5832.1.
RefSeqi NP_064695.3. NM_020299.4.
UniGenei Hs.116724.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZUA X-ray 1.25 X 1-316 [» ]
4GA8 X-ray 1.94 A 1-316 [» ]
4GAB X-ray 1.60 A 1-316 [» ]
4GQ0 X-ray 2.10 A 1-316 [» ]
4GQG X-ray 1.92 A 1-316 [» ]
4I5X X-ray 2.10 A 1-316 [» ]
4ICC X-ray 1.75 X 1-316 [» ]
4JIH X-ray 2.30 A 1-316 [» ]
4JII X-ray 2.20 X 1-316 [» ]
ProteinModelPortali O60218.
SMRi O60218. Positions 1-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121325. 3 interactions.
IntActi O60218. 1 interaction.
STRINGi 9606.ENSP00000352584.

Chemistry

BindingDBi O60218.
ChEMBLi CHEMBL5983.

PTM databases

PhosphoSitei O60218.

2D gel databases

DOSAC-COBS-2DPAGE O60218.

Proteomic databases

MaxQBi O60218.
PaxDbi O60218.
PRIDEi O60218.

Protocols and materials databases

DNASUi 57016.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359579 ; ENSP00000352584 ; ENSG00000198074 .
GeneIDi 57016.
KEGGi hsa:57016.
UCSCi uc003vrr.3. human.

Organism-specific databases

CTDi 57016.
GeneCardsi GC07P134212.
H-InvDB HIX0007102.
HIX0033661.
HGNCi HGNC:382. AKR1B10.
HPAi HPA020280.
MIMi 604707. gene.
neXtProti NX_O60218.
PharmGKBi PA24676.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi O60218.
KOi K00011.
OMAi TSKLWLQ.
OrthoDBi EOG70KGQF.
PhylomeDBi O60218.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_24968. Retinoid metabolism and transport.
SABIO-RK O60218.

Miscellaneous databases

EvolutionaryTracei O60218.
GeneWikii AKR1B10.
GenomeRNAii 57016.
NextBioi 62758.
PROi O60218.
SOURCEi Search...

Gene expression databases

Bgeei O60218.
CleanExi HS_AKR1B10.
Genevestigatori O60218.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1998) [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(1998) [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 (JUN-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 (MAY-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 (JUN-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(2003) [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(2003) [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(2004) [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(1998) [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(2009) [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(2011) [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(2007) [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 10, 2002
Last sequence update: February 8, 2011
Last modified: September 3, 2014
This is version 130 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

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