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P09884 (DPOLA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase alpha catalytic subunit

EC=2.7.7.7
Alternative name(s):
DNA polymerase alpha catalytic subunit p180
Gene names
Name:POLA1
Synonyms:POLA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. Ref.8

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Interacts with PARP1; this interaction functions as part of the control of replication fork progression. Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA. Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with SV40 Large T antigen; this interaction allows viral DNA replication. Interacts with herpes simplex virus 1 (HHV-1) replication origin-binding protein UL9. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus.

Domain

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity.

Post-translational modification

A 165 kDa form is probably produced by proteolytic cleavage at Lys-124.

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Contains 1 CysA-type zinc finger.

Ontologies

Keywords
   Biological processDNA replication
Host-virus interaction
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   Ligand4Fe-4S
DNA-binding
Iron
Iron-sulfur
Metal-binding
Zinc
   Molecular functionDNA-directed DNA polymerase
Nucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from mutant phenotype PubMed 16762037PubMed 3917431PubMed 4084590. Source: UniProtKB

DNA replication initiation

Inferred from direct assay PubMed 2175912. Source: UniProtKB

DNA replication, synthesis of RNA primer

Inferred from direct assay PubMed 2175912. Source: GOC

DNA strand elongation involved in DNA replication

Inferred from mutant phenotype PubMed 4084590. Source: UniProtKB

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell proliferation

Inferred from direct assay Ref.1. Source: UniProtKB

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 11470886. Source: UniProtKB

lagging strand elongation

Inferred from direct assay PubMed 2175912PubMed 7910375. Source: UniProtKB

leading strand elongation

Inferred from direct assay PubMed 2175912PubMed 7910375. Source: UniProtKB

mitotic S phase

Inferred from direct assay PubMed 16762037. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of transcription involved in G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

translesion synthesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentalpha DNA polymerase:primase complex

Inferred from direct assay PubMed 2175912. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nuclear envelope

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear matrix

Inferred from direct assay PubMed 1903085. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.8. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 7045121. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 16762037PubMed 4084590. Source: UniProtKB

   Molecular_function3'-5' exonuclease activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay PubMed 16762037. Source: UniProtKB

DNA-directed DNA polymerase activity

Inferred from direct assay Ref.1PubMed 893425. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 16762037. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside binding

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from direct assay PubMed 3139084. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10518787PubMed 10869558PubMed 1311258PubMed 16438930Ref.4PubMed 9395244Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P030706EBI-850026,EBI-617698From a different organism.
E1P040142EBI-850026,EBI-7014446From a different organism.
RPA1P276942EBI-850026,EBI-621389
UL9P101934EBI-850026,EBI-8596799From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14621462DNA polymerase alpha catalytic subunit
PRO_0000046428

Regions

Zinc finger1283 – 131533CysA-type
Region650 – 71566DNA-binding region Potential
Region1245 – 1376132DNA-binding region Potential
Motif1348 – 137427CysB motif
Compositional bias75 – 11238Asp-rich
Compositional bias1047 – 10504Poly-Leu
Compositional bias1051 – 10544Poly-Lys

Sites

Metal binding12831Zinc By similarity
Metal binding12861Zinc By similarity
Metal binding13101Zinc By similarity
Metal binding13151Zinc By similarity
Metal binding13481Iron-sulfur (4Fe-4S) By similarity
Metal binding13531Iron-sulfur (4Fe-4S) By similarity
Metal binding13711Iron-sulfur (4Fe-4S) By similarity
Metal binding13741Iron-sulfur (4Fe-4S) By similarity
Site124 – 1252Cleavage

Amino acid modifications

Modified residue1741Phosphothreonine Ref.11 Ref.12
Modified residue1861Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14
Modified residue1901Phosphoserine Ref.9 Ref.12
Modified residue2091Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue2241N6-acetyllysine By similarity
Modified residue9701N6-succinyllysine By similarity

Natural variations

Natural variant7401Y → H.
Corresponds to variant rs2230927 [ dbSNP | Ensembl ].
VAR_048877

Experimental info

Sequence conflict503 – 5064SPQL → KSTA in CAA29920. Ref.1
Sequence conflict8371A → G in CAA29920. Ref.1
Sequence conflict14051L → C AA sequence Ref.4
Sequence conflict14261V → C AA sequence Ref.4

Secondary structure

.......... 1462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09884 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: DC40C3EDD6F4B495

FASTA1,462165,913
        10         20         30         40         50         60 
MAPVHGDDSL SDSGSFVSSR ARREKKSKKG RQEALERLKK AKAGEKYKYE VEDFTGVYEE 

        70         80         90        100        110        120 
VDEEQYSKLV QARQDDDWIV DDDGIGYVED GREIFDDDLE DDALDADEKG KDGKARNKDK 

       130        140        150        160        170        180 
RNVKKLAVTK PNNIKSMFIA CAGKKTADKA VDLSKDGLLG DILQDLNTET PQITPPPVMI 

       190        200        210        220        230        240 
LKKKRSIGAS PNPFSVHTAT AVPSGKIASP VSRKEPPLTP VPLKRAEFAG DDVQVESTEE 

       250        260        270        280        290        300 
EQESGAMEFE DGDFDEPMEV EEVDLEPMAA KAWDKESEPA EEVKQEADSG KGTVSYLGSF 

       310        320        330        340        350        360 
LPDVSCWDID QEGDSSFSVQ EVQVDSSHLP LVKGADEEQV FHFYWLDAYE DQYNQPGVVF 

       370        380        390        400        410        420 
LFGKVWIESA ETHVSCCVMV KNIERTLYFL PREMKIDLNT GKETGTPISM KDVYEEFDEK 

       430        440        450        460        470        480 
IATKYKIMKF KSKPVEKNYA FEIPDVPEKS EYLEVKYSAE MPQLPQDLKG ETFSHVFGTN 

       490        500        510        520        530        540 
TSSLELFLMN RKIKGPCWLE VKSPQLLNQP VSWCKVEAMA LKPDLVNVIK DVSPPPLVVM 

       550        560        570        580        590        600 
AFSMKTMQNA KNHQNEIIAM AALVHHSFAL DKAAPKPPFQ SHFCVVSKPK DCIFPYAFKE 

       610        620        630        640        650        660 
VIEKKNVKVE VAATERTLLG FFLAKVHKID PDIIVGHNIY GFELEVLLQR INVCKAPHWS 

       670        680        690        700        710        720 
KIGRLKRSNM PKLGGRSGFG ERNATCGRMI CDVEISAKEL IRCKSYHLSE LVQQILKTER 

       730        740        750        760        770        780 
VVIPMENIQN MYSESSQLLY LLEHTWKDAK FILQIMCELN VLPLALQITN IAGNIMSRTL 

       790        800        810        820        830        840 
MGGRSERNEF LLLHAFYENN YIVPDKQIFR KPQQKLGDED EEIDGDTNKY KKGRKKAAYA 

       850        860        870        880        890        900 
GGLVLDPKVG FYDKFILLLD FNSLYPSIIQ EFNICFTTVQ RVASEAQKVT EDGEQEQIPE 

       910        920        930        940        950        960 
LPDPSLEMGI LPREIRKLVE RRKQVKQLMK QQDLNPDLIL QYDIRQKALK LTANSMYGCL 

       970        980        990       1000       1010       1020 
GFSYSRFYAK PLAALVTYKG REILMHTKEM VQKMNLEVIY GDTDSIMINT NSTNLEEVFK 

      1030       1040       1050       1060       1070       1080 
LGNKVKSEVN KLYKLLEIDI DGVFKSLLLL KKKKYAALVV EPTSDGNYVT KQELKGLDIV 

      1090       1100       1110       1120       1130       1140 
RRDWCDLAKD TGNFVIGQIL SDQSRDTIVE NIQKRLIEIG ENVLNGSVPV SQFEINKALT 

      1150       1160       1170       1180       1190       1200 
KDPQDYPDKK SLPHVHVALW INSQGGRKVK AGDTVSYVIC QDGSNLTASQ RAYAPEQLQK 

      1210       1220       1230       1240       1250       1260 
QDNLTIDTQY YLAQQIHPVV ARICEPIDGI DAVLIATWLG LDPTQFRVHH YHKDEENDAL 

      1270       1280       1290       1300       1310       1320 
LGGPAQLTDE EKYRDCERFK CPCPTCGTEN IYDNVFDGSG TDMEPSLYRC SNIDCKASPL 

      1330       1340       1350       1360       1370       1380 
TFTVQLSNKL IMDIRRFIKK YYDGWLICEE PTCRNRTRHL PLQFSRTGPL CPACMKATLQ 

      1390       1400       1410       1420       1430       1440 
PEYSDKSLYT QLCFYRYIFD AECALEKLTT DHEKDKLKKQ FFTPKVLQDY RKLKNTAEQF 

      1450       1460 
LSRSGYSEVN LSKLFAGCAV KS 

« Hide

References

« Hide 'large scale' references
[1]"Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases."
Wong S.W., Wahl A.F., Yuan P.-M., Arai N., Pearson B.E., Arai K., Korn D., Hunkapiller M.W., Wang T.S.-F.
EMBO J. 7:37-47(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIEHS SNPs program
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells."
Pearson B.E., Nasheuer H.-P., Wang T.S.-F.
Mol. Cell. Biol. 11:2081-2095(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[4]"Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus."
Hsi K.-L., Copeland W.C., Wang T.S.-F.
Nucleic Acids Res. 18:6231-6237(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-37 AND 1405-1426, PROTEOLYTIC PROCESSING AT LYS-124.
[5]"T-antigen-DNA polymerase alpha complex implicated in simian virus 40 DNA replication."
Smale S.T., Tjian R.
Mol. Cell. Biol. 6:4077-4087(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[6]"Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha."
Lee S.S., Dong Q., Wang T.S., Lehman I.R.
Proc. Natl. Acad. Sci. U.S.A. 92:7882-7886(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-1 UL9 PROTEIN.
[7]"Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms."
Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S.
Biochemistry 36:8443-8454(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPA1.
[8]"Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Menissier-de Murcia J.
Nucleic Acids Res. 26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARP1.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-190 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Physical interactions between Mcm10, DNA, and DNA polymerase alpha."
Warren E.M., Huang H., Fanning E., Chazin W.J., Eichman B.F.
J. Biol. Chem. 284:24662-24672(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[11]"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 THR-174 AND SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; SER-186; SER-190 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-186 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha."
Evanics F., Maurmann L., Yang W.W., Bose R.N.
Biochim. Biophys. Acta 1651:163-171(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1345-1382.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06745 mRNA. Translation: CAA29920.1.
AY275833 Genomic DNA. Translation: AAP13534.1.
M64481 Genomic DNA. Translation: AAA52318.1.
CCDSCCDS14214.1.
PIRDJHUAC. S00257.
RefSeqNP_058633.2. NM_016937.3.
UniGeneHs.567319.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0PNMR-A1347-1377[»]
1K18NMR-A1347-1377[»]
1N5GNMR-A1345-1382[»]
ProteinModelPortalP09884.
SMRP09884. Positions 341-1240, 1269-1429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111418. 37 interactions.
IntActP09884. 10 interactions.
MINTMINT-1517478.
STRING9606.ENSP00000368349.

Chemistry

BindingDBP09884.
ChEMBLCHEMBL2363042.
DrugBankDB00631. Clofarabine.
DB01073. Fludarabine.

PTM databases

PhosphoSiteP09884.

Polymorphism databases

DMDM60392197.

Proteomic databases

MaxQBP09884.
PaxDbP09884.
PRIDEP09884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379059; ENSP00000368349; ENSG00000101868.
GeneID5422.
KEGGhsa:5422.
UCSCuc004dbl.3. human.

Organism-specific databases

CTD5422.
GeneCardsGC0XP024712.
H-InvDBHIX0028476.
HGNCHGNC:9173. POLA1.
HPACAB012274.
HPA002947.
MIM312040. gene.
neXtProtNX_P09884.
PharmGKBPA162399856.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0417.
HOGENOMHOG000163524.
HOVERGENHBG080008.
KOK02320.
PhylomeDBP09884.
TreeFamTF103001.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP09884.
BgeeP09884.
CleanExHS_POLA1.
GenevestigatorP09884.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR004578. DNA-dir_DNA_pol_B_pol2.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PfamPF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00592. pol2. 1 hit.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLA1. human.
EvolutionaryTraceP09884.
GeneWikiPolymerase_(DNA_directed),_alpha_1.
GenomeRNAi5422.
NextBio20977.
PROP09884.
SOURCESearch...

Entry information

Entry nameDPOLA_HUMAN
AccessionPrimary (citable) accession number: P09884
Secondary accession number(s): Q86UQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM