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Protein

Uridine-cytidine kinase 2

Gene

UCK2

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

Functioni

Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.

Catalytic activityi

ATP + uridine = ADP + UMP.
ATP + cytidine = ADP + CMP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate
Binding sitei112 – 1121Substrate
Binding sitei117 – 1171Substrate
Binding sitei166 – 1661Substrate
Binding sitei176 – 1761Substrate
Binding sitei184 – 1841Substrate
Binding sitei213 – 2131ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside kinase activity Source: Reactome
  3. uridine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to oxygen levels Source: Ensembl
  2. CMP salvage Source: InterPro
  3. CTP salvage Source: UniProtKB-UniPathway
  4. feeding behavior Source: Ensembl
  5. nucleobase-containing small molecule metabolic process Source: Reactome
  6. pyrimidine nucleobase metabolic process Source: Reactome
  7. pyrimidine nucleoside salvage Source: Reactome
  8. response to axon injury Source: Ensembl
  9. small molecule metabolic process Source: Reactome
  10. UMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07003-MONOMER.
BRENDAi2.7.1.48. 2681.
ReactomeiREACT_655. Pyrimidine salvage reactions.
SABIO-RKQ9BZX2.
UniPathwayiUPA00574; UER00637.
UPA00579; UER00640.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridine-cytidine kinase 2 (EC:2.7.1.48)
Short name:
UCK 2
Alternative name(s):
Cytidine monophosphokinase 2
Testis-specific protein TSA903
Uridine monophosphokinase 2
Gene namesi
Name:UCK2
Synonyms:UMPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12562. UCK2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. intracellular membrane-bounded organelle Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA362.

Polymorphism and mutation databases

BioMutaiUCK2.
DMDMi20455356.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 261260Uridine-cytidine kinase 2PRO_0000164455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei254 – 2541Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BZX2.
PaxDbiQ9BZX2.
PeptideAtlasiQ9BZX2.
PRIDEiQ9BZX2.

PTM databases

PhosphoSiteiQ9BZX2.

Expressioni

Tissue specificityi

According to PubMed:8812458; testis-specific. According to PubMed:11306702, placenta-specific.1 Publication

Gene expression databases

BgeeiQ9BZX2.
CleanExiHS_UCK2.
ExpressionAtlasiQ9BZX2. baseline and differential.
GenevestigatoriQ9BZX2.

Organism-specific databases

HPAiHPA051286.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi113217. 12 interactions.
IntActiQ9BZX2. 1 interaction.
STRINGi9606.ENSP00000356853.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 266Combined sources
Helixi33 – 4311Combined sources
Helixi46 – 483Combined sources
Helixi51 – 533Combined sources
Beta strandi55 – 606Combined sources
Helixi61 – 644Combined sources
Helixi70 – 778Combined sources
Helixi86 – 883Combined sources
Helixi91 – 10212Combined sources
Beta strandi107 – 1137Combined sources
Turni114 – 1174Combined sources
Beta strandi118 – 1269Combined sources
Beta strandi130 – 1356Combined sources
Turni137 – 1404Combined sources
Helixi143 – 1486Combined sources
Beta strandi150 – 1567Combined sources
Helixi159 – 17315Combined sources
Helixi178 – 18710Combined sources
Helixi189 – 1968Combined sources
Helixi198 – 2036Combined sources
Beta strandi205 – 2095Combined sources
Helixi211 – 2133Combined sources
Helixi215 – 23016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UDWX-ray2.60A/B1-250[»]
1UEIX-ray2.60A/B1-250[»]
1UEJX-ray2.61A/B1-250[»]
1UFQX-ray2.50A/B/C/D1-250[»]
1UJ2X-ray1.80A/B1-250[»]
1XRJX-ray2.00A/B1-261[»]
ProteinModelPortaliQ9BZX2.
SMRiQ9BZX2. Positions 19-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZX2.

Family & Domainsi

Sequence similaritiesi

Belongs to the uridine kinase family.Curated

Phylogenomic databases

eggNOGiCOG0572.
GeneTreeiENSGT00390000015696.
HOGENOMiHOG000262756.
HOVERGENiHBG023339.
InParanoidiQ9BZX2.
KOiK00876.
OMAiDICFMRR.
OrthoDBiEOG7Q8CP2.
PhylomeDBiQ9BZX2.
TreeFamiTF316686.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR029925. UCK-2.
IPR000764. Uridine_kinase_like.
[Graphical view]
PANTHERiPTHR10285:SF28. PTHR10285:SF28. 1 hit.
PfamiPF00485. PRK. 1 hit.
[Graphical view]
PRINTSiPR00988. URIDINKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00235. udk. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZX2-1) [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
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD
60 70 80 90 100
YRQKQVVILS QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE
110 120 130 140 150
ITEGKTVQIP VYDFVSHSRK EETVTVYPAD VVLFEGILAF YSQEVRDLFQ
160 170 180 190 200
MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ ILSQYITFVK PAFEEFCLPT
210 220 230 240 250
KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG CLNGYTPSRK
260
RQASESSSRP H
Length:261
Mass (Da):29,299
Last modified:June 1, 2001 - v1
Checksum:i71791346F091EBFD
GO
Isoform 2 (identifier: Q9BZX2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.

Show »
Length:111
Mass (Da):12,587
Checksum:iE6688B1B86F432A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021K → Q in BAA11349 (PubMed:8812458).Curated
Sequence conflicti222 – 2221V → E in BAA11349 (PubMed:8812458).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 150150Missing in isoform 2. 3 PublicationsVSP_014262Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78335 mRNA. Translation: BAA11349.1.
AF236637 mRNA. Translation: AAK14053.1.
BT006860 mRNA. Translation: AAP35506.1.
CR456857 mRNA. Translation: CAG33138.1.
AL451074, AL358115 Genomic DNA. Translation: CAH74066.1.
AL358115, AL451074 Genomic DNA. Translation: CAI15121.1.
BC002906 mRNA. Translation: AAH02906.2.
AB062451 mRNA. Translation: BAB56162.1.
CCDSiCCDS1252.1. [Q9BZX2-1]
RefSeqiNP_036606.2. NM_012474.4. [Q9BZX2-1]
UniGeneiHs.458360.

Genome annotation databases

EnsembliENST00000367879; ENSP00000356853; ENSG00000143179. [Q9BZX2-1]
ENST00000469256; ENSP00000476692; ENSG00000143179. [Q9BZX2-2]
ENST00000470820; ENSP00000476327; ENSG00000143179. [Q9BZX2-2]
GeneIDi7371.
KEGGihsa:7371.
UCSCiuc001gdp.3. human. [Q9BZX2-1]
uc010plb.2. human. [Q9BZX2-2]

Polymorphism and mutation databases

BioMutaiUCK2.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78335 mRNA. Translation: BAA11349.1.
AF236637 mRNA. Translation: AAK14053.1.
BT006860 mRNA. Translation: AAP35506.1.
CR456857 mRNA. Translation: CAG33138.1.
AL451074, AL358115 Genomic DNA. Translation: CAH74066.1.
AL358115, AL451074 Genomic DNA. Translation: CAI15121.1.
BC002906 mRNA. Translation: AAH02906.2.
AB062451 mRNA. Translation: BAB56162.1.
CCDSiCCDS1252.1. [Q9BZX2-1]
RefSeqiNP_036606.2. NM_012474.4. [Q9BZX2-1]
UniGeneiHs.458360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UDWX-ray2.60A/B1-250[»]
1UEIX-ray2.60A/B1-250[»]
1UEJX-ray2.61A/B1-250[»]
1UFQX-ray2.50A/B/C/D1-250[»]
1UJ2X-ray1.80A/B1-250[»]
1XRJX-ray2.00A/B1-261[»]
ProteinModelPortaliQ9BZX2.
SMRiQ9BZX2. Positions 19-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113217. 12 interactions.
IntActiQ9BZX2. 1 interaction.
STRINGi9606.ENSP00000356853.

Chemistry

ChEMBLiCHEMBL2469.

PTM databases

PhosphoSiteiQ9BZX2.

Polymorphism and mutation databases

BioMutaiUCK2.
DMDMi20455356.

Proteomic databases

MaxQBiQ9BZX2.
PaxDbiQ9BZX2.
PeptideAtlasiQ9BZX2.
PRIDEiQ9BZX2.

Protocols and materials databases

DNASUi7371.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367879; ENSP00000356853; ENSG00000143179. [Q9BZX2-1]
ENST00000469256; ENSP00000476692; ENSG00000143179. [Q9BZX2-2]
ENST00000470820; ENSP00000476327; ENSG00000143179. [Q9BZX2-2]
GeneIDi7371.
KEGGihsa:7371.
UCSCiuc001gdp.3. human. [Q9BZX2-1]
uc010plb.2. human. [Q9BZX2-2]

Organism-specific databases

CTDi7371.
GeneCardsiGC01P165796.
HGNCiHGNC:12562. UCK2.
HPAiHPA051286.
MIMi609329. gene.
neXtProtiNX_Q9BZX2.
PharmGKBiPA362.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0572.
GeneTreeiENSGT00390000015696.
HOGENOMiHOG000262756.
HOVERGENiHBG023339.
InParanoidiQ9BZX2.
KOiK00876.
OMAiDICFMRR.
OrthoDBiEOG7Q8CP2.
PhylomeDBiQ9BZX2.
TreeFamiTF316686.

Enzyme and pathway databases

UniPathwayiUPA00574; UER00637.
UPA00579; UER00640.
BioCyciMetaCyc:HS07003-MONOMER.
BRENDAi2.7.1.48. 2681.
ReactomeiREACT_655. Pyrimidine salvage reactions.
SABIO-RKQ9BZX2.

Miscellaneous databases

ChiTaRSiUCK2. human.
EvolutionaryTraceiQ9BZX2.
GeneWikiiUCK2.
GenomeRNAii7371.
NextBioi28862.
PROiQ9BZX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZX2.
CleanExiHS_UCK2.
ExpressionAtlasiQ9BZX2. baseline and differential.
GenevestigatoriQ9BZX2.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006083. PRK/URK.
IPR029925. UCK-2.
IPR000764. Uridine_kinase_like.
[Graphical view]
PANTHERiPTHR10285:SF28. PTHR10285:SF28. 1 hit.
PfamiPF00485. PRK. 1 hit.
[Graphical view]
PRINTSiPR00988. URIDINKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00235. udk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method."
    Ozaki K., Kuroki T., Hayashi S., Nakamura Y.
    Genomics 36:316-319(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  2. "Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases."
    Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.
    Mol. Pharmacol. 59:1181-1186(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
  3. "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] (ISOFORM 2).
  4. "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 2).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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).
    Tissue: Lung.
  7. "Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells."
    Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T., Fukushima M.
    Int. J. Mol. Med. 8:273-278(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-261 (ISOFORM 1).
    Tissue: Fibrosarcoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase."
    Suzuki N.N., Koizumi K., Fukushima M., Matsuda A., Inagaki F.
    Structure 12:751-764(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-250 IN COMPLEXES WITH ADP; CYTIDINE; CMP; CTP AND UTP, SUBUNIT.
  13. "Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative."
    Appleby T.C., Larson G., Cheney I.W., Walker H., Wu J.Z., Zhong W., Hong Z., Yao N.
    Acta Crystallogr. D 61:278-284(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CMP, SUBUNIT.

Entry informationi

Entry nameiUCK2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZX2
Secondary accession number(s): Q5VV91
, Q7KZV3, Q92528, Q96KG5, Q9BU42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 128 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 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.