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Protein

Replication protein A 14 kDa subunit

Gene

RPA3

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

Functioni

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105).1 Publication6 Publications

GO - Molecular functioni

  1. damaged DNA binding Source: UniProtKB
  2. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. cellular response to heat Source: Reactome
  3. DNA recombinase assembly Source: Reactome
  4. DNA repair Source: Reactome
  5. DNA replication Source: UniProtKB
  6. DNA strand elongation involved in DNA replication Source: Reactome
  7. double-strand break repair Source: Reactome
  8. double-strand break repair via homologous recombination Source: UniProtKB
  9. G1/S transition of mitotic cell cycle Source: Reactome
  10. mismatch repair Source: UniProtKB
  11. mitotic cell cycle Source: Reactome
  12. nucleotide-excision repair Source: UniProtKB
  13. nucleotide-excision repair, DNA damage removal Source: Reactome
  14. nucleotide-excision repair, DNA gap filling Source: Reactome
  15. regulation of cell proliferation Source: Ensembl
  16. regulation of cellular response to heat Source: Reactome
  17. regulation of mitotic cell cycle Source: Ensembl
  18. telomere maintenance Source: Reactome
  19. telomere maintenance via recombination Source: Reactome
  20. telomere maintenance via semi-conservative replication Source: Reactome
  21. transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2055. Processing of DNA double-strand break ends.
REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_257. Formation of incision complex in GG-NER.
REACT_264071. HSF1 activation.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_27271. Meiotic recombination.
REACT_311. Dual incision reaction in GG-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_6769. Activation of ATR in response to replication stress.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein A 14 kDa subunit
Short name:
RP-A p14
Alternative name(s):
Replication factor A protein 3
Short name:
RF-A protein 3
Gene namesi
Name:RPA3
Synonyms:REPA3, RPA14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:10291. RPA3.

Subcellular locationi

GO - Cellular componenti

  1. DNA replication factor A complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34653.

Polymorphism and mutation databases

BioMutaiRPA3.
DMDMi464608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 121120Replication protein A 14 kDa subunitPRO_0000097276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvaline3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP35244.
PaxDbiP35244.
PeptideAtlasiP35244.
PRIDEiP35244.

PTM databases

PhosphoSiteiP35244.

Expressioni

Gene expression databases

BgeeiP35244.
CleanExiHS_RPA3.
ExpressionAtlasiP35244. baseline and differential.
GenevestigatoriP35244.

Organism-specific databases

HPAiHPA005708.

Interactioni

Subunit structurei

Component of the canonical replication protein A complex (RPA), an heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD52P433513EBI-621428,EBI-706448
RPA1P276946EBI-621428,EBI-621389
RPA2P159278EBI-621428,EBI-621404

Protein-protein interaction databases

BioGridi112039. 376 interactions.
DIPiDIP-24190N.
IntActiP35244. 21 interactions.
MINTiMINT-5002568.
STRINGi9606.ENSP00000223129.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi10 – 123Combined sources
Helixi14 – 207Combined sources
Beta strandi24 – 3411Combined sources
Beta strandi38 – 447Combined sources
Beta strandi50 – 545Combined sources
Beta strandi65 – 739Combined sources
Beta strandi79 – 868Combined sources
Beta strandi90 – 923Combined sources
Helixi96 – 10813Combined sources
Helixi110 – 1123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1OX-ray2.80A/D1-121[»]
1QUQX-ray2.50B/D1-121[»]
2PI2X-ray2.00E/F/G/H1-121[»]
2PQAX-ray2.50B/D1-121[»]
2Z6KX-ray3.00C/D1-121[»]
3KDFX-ray1.98A/C1-121[»]
SMRiP35244. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35244.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG42188.
GeneTreeiENSGT00390000008029.
HOGENOMiHOG000252930.
HOVERGENiHBG003004.
InParanoidiP35244.
KOiK10740.
OMAiMVDVMEL.
OrthoDBiEOG77WWFG.
PhylomeDBiP35244.
TreeFamiTF105243.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR013970. Rfa2.
[Graphical view]
PfamiPF08661. Rep_fac-A_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P35244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN
60 70 80 90 100
GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN
110 120
EAVKIIHDFP QFYPLGIVQH D
Length:121
Mass (Da):13,569
Last modified:February 1, 1994 - v1
Checksum:i3FD99851959FB498
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07493 mRNA. Translation: AAA58350.1.
BT007320 mRNA. Translation: AAP35984.1.
DQ003136 Genomic DNA. Translation: AAX84517.1.
AC004948 Genomic DNA. Translation: AAQ96878.1.
BC005264 mRNA. Translation: AAH05264.1.
BC009868 mRNA. Translation: AAH09868.1.
CCDSiCCDS5356.1.
PIRiA46008.
RefSeqiNP_002938.1. NM_002947.3.
UniGeneiHs.487540.

Genome annotation databases

EnsembliENST00000223129; ENSP00000223129; ENSG00000106399.
ENST00000396682; ENSP00000379914; ENSG00000106399.
GeneIDi6119.
KEGGihsa:6119.
UCSCiuc003sri.3. human.

Polymorphism and mutation databases

BioMutaiRPA3.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07493 mRNA. Translation: AAA58350.1.
BT007320 mRNA. Translation: AAP35984.1.
DQ003136 Genomic DNA. Translation: AAX84517.1.
AC004948 Genomic DNA. Translation: AAQ96878.1.
BC005264 mRNA. Translation: AAH05264.1.
BC009868 mRNA. Translation: AAH09868.1.
CCDSiCCDS5356.1.
PIRiA46008.
RefSeqiNP_002938.1. NM_002947.3.
UniGeneiHs.487540.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1OX-ray2.80A/D1-121[»]
1QUQX-ray2.50B/D1-121[»]
2PI2X-ray2.00E/F/G/H1-121[»]
2PQAX-ray2.50B/D1-121[»]
2Z6KX-ray3.00C/D1-121[»]
3KDFX-ray1.98A/C1-121[»]
SMRiP35244. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112039. 376 interactions.
DIPiDIP-24190N.
IntActiP35244. 21 interactions.
MINTiMINT-5002568.
STRINGi9606.ENSP00000223129.

PTM databases

PhosphoSiteiP35244.

Polymorphism and mutation databases

BioMutaiRPA3.
DMDMi464608.

Proteomic databases

MaxQBiP35244.
PaxDbiP35244.
PeptideAtlasiP35244.
PRIDEiP35244.

Protocols and materials databases

DNASUi6119.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223129; ENSP00000223129; ENSG00000106399.
ENST00000396682; ENSP00000379914; ENSG00000106399.
GeneIDi6119.
KEGGihsa:6119.
UCSCiuc003sri.3. human.

Organism-specific databases

CTDi6119.
GeneCardsiGC07M007643.
HGNCiHGNC:10291. RPA3.
HPAiHPA005708.
MIMi179837. gene.
neXtProtiNX_P35244.
PharmGKBiPA34653.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42188.
GeneTreeiENSGT00390000008029.
HOGENOMiHOG000252930.
HOVERGENiHBG003004.
InParanoidiP35244.
KOiK10740.
OMAiMVDVMEL.
OrthoDBiEOG77WWFG.
PhylomeDBiP35244.
TreeFamiTF105243.

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2055. Processing of DNA double-strand break ends.
REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_257. Formation of incision complex in GG-NER.
REACT_264071. HSF1 activation.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_27271. Meiotic recombination.
REACT_311. Dual incision reaction in GG-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_6769. Activation of ATR in response to replication stress.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.

Miscellaneous databases

ChiTaRSiRPA3. human.
EvolutionaryTraceiP35244.
GeneWikiiRPA3.
GenomeRNAii6119.
NextBioi23763.
PROiP35244.
SOURCEiSearch...

Gene expression databases

BgeeiP35244.
CleanExiHS_RPA3.
ExpressionAtlasiP35244. baseline and differential.
GenevestigatoriP35244.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR013970. Rfa2.
[Graphical view]
PfamiPF08661. Rep_fac-A_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A."
    Umbricht C.B., Kelly T.J.
    J. Biol. Chem. 268:6131-6138(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  3. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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].
  5. "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].
    Tissue: Kidney and Lung.
  6. "Mammalian DNA nucleotide excision repair reconstituted with purified protein components."
    Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V., Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.
    Cell 80:859-868(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
  7. "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex."
    Keshav K.F., Chen C., Dutta A.
    Mol. Cell. Biol. 15:3119-3128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA4.
  8. "The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair."
    Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.
    J. Biol. Chem. 273:1453-1461(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
  9. "Replication protein A stimulates long patch DNA base excision repair."
    DeMott M.S., Zigman S., Bambara R.A.
    J. Biol. Chem. 273:27492-27498(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BASE EXCISION REPAIR.
  10. "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 VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "An alternative form of replication protein a prevents viral replication in vitro."
    Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S.
    J. Biol. Chem. 284:5324-5331(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ARPA COMPLEX, FUNCTION OF THE ARPA COMPLEX.
  12. "Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA."
    Salas T.R., Petruseva I., Lavrik O., Saintome C.
    Nucleic Acids Res. 37:38-46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SINGLE-STRANDED DNA-BINDING.
  13. "An alternative form of replication protein a expressed in normal human tissues supports DNA repair."
    Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J., Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.
    J. Biol. Chem. 285:4788-4797(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ARPA COMPLEX.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry."
    Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., Jimenez A.E., Jin J., Zou L.
    Mol. Cell 53:235-246(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA."
    Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.
    EMBO J. 21:1855-1863(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RPA1 AND RPA2.

Entry informationi

Entry nameiRFA3_HUMAN
AccessioniPrimary (citable) accession number: P35244
Secondary accession number(s): Q549U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 29, 2015
This is version 142 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 7
    Human chromosome 7: 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

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.