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Protein

Pre-mRNA-processing-splicing factor 8

Gene

PRPF8

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

Functioni

Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site.1 Publication1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • mRNA processing Source: ProtInc
  • mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: UniProtKB
  • RNA splicing, via transesterification reactions Source: UniProtKB
  • spliceosomal tri-snRNP complex assembly Source: UniProtKB

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing-splicing factor 8
Alternative name(s):
220 kDa U5 snRNP-specific protein
PRP8 homolog
Splicing factor Prp8
p220
Gene namesi
Name:PRPF8
Synonyms:PRPC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000174231.16
HGNCiHGNC:17340 PRPF8
MIMi607300 gene
neXtProtiNX_Q6P2Q9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 13 (RP13)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:600059
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0226262301P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 PublicationCorresponds to variant dbSNP:rs121434239EnsemblClinVar.1
Natural variantiVAR_0226272304F → L in RP13. 2 PublicationsCorresponds to variant dbSNP:rs121434240EnsemblClinVar.1
Natural variantiVAR_0226282309H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant dbSNP:rs121434236EnsemblClinVar.1
Natural variantiVAR_0226292309H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant dbSNP:rs121434236EnsemblClinVar.1
Natural variantiVAR_0226302310R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 4 Publications1
Natural variantiVAR_0226312310R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 PublicationsCorresponds to variant dbSNP:rs121434238EnsemblClinVar.1
Natural variantiVAR_0226322314F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 2 Publications1
Natural variantiVAR_0226332334Y → N in RP13. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1788V → D: Strongly reduced interaction with RNA. 1 Publication1
Mutagenesisi1789T → P: Strongly reduced interaction with RNA. 1 Publication1

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

DisGeNETi10594
GeneReviewsiPRPF8
MalaCardsiPRPF8
MIMi600059 phenotype
OpenTargetsiENSG00000174231
Orphaneti791 Retinitis pigmentosa
PharmGKBiPA33815

Polymorphism and mutation databases

BioMutaiPRPF8
DMDMi67460824

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000970402 – 2335Pre-mRNA-processing-splicing factor 8Add BLAST2334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei859PhosphoserineCombined sources1
Modified residuei1358PhosphoserineCombined sources1
Modified residuei1425N6,N6-dimethyllysineCombined sources1
Modified residuei1463N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ6P2Q9
MaxQBiQ6P2Q9
PaxDbiQ6P2Q9
PeptideAtlasiQ6P2Q9
PRIDEiQ6P2Q9

PTM databases

CarbonylDBiQ6P2Q9
iPTMnetiQ6P2Q9
PhosphoSitePlusiQ6P2Q9
SwissPalmiQ6P2Q9

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000174231
CleanExiHS_PRPF8
ExpressionAtlasiQ6P2Q9 baseline and differential
GenevisibleiQ6P2Q9 HS

Organism-specific databases

HPAiCAB009941
CAB015457

Interactioni

Subunit structurei

Part of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H homology domain) with AAR2 (PubMed:26527271).18 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115842, 187 interactors
CORUMiQ6P2Q9
DIPiDIP-29614N
IntActiQ6P2Q9, 63 interactors
MINTiQ6P2Q9
STRINGi9606.ENSP00000304350

Structurei

Secondary structure

12335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1761 – 1763Combined sources3
Turni1765 – 1767Combined sources3
Helixi1768 – 1772Combined sources5
Beta strandi1773 – 1775Combined sources3
Beta strandi1777 – 1781Combined sources5
Beta strandi1785 – 1792Combined sources8
Beta strandi1794 – 1796Combined sources3
Beta strandi1798 – 1803Combined sources6
Beta strandi1805 – 1810Combined sources6
Turni1812 – 1814Combined sources3
Beta strandi1816 – 1822Combined sources7
Helixi1824 – 1827Combined sources4
Helixi1833 – 1851Combined sources19
Helixi1854 – 1856Combined sources3
Beta strandi1859 – 1865Combined sources7
Helixi1866 – 1868Combined sources3
Helixi1869 – 1875Combined sources7
Turni1876 – 1878Combined sources3
Beta strandi1883 – 1886Combined sources4
Helixi1893 – 1898Combined sources6
Helixi1900 – 1908Combined sources9
Beta strandi1913 – 1918Combined sources6
Turni1919 – 1922Combined sources4
Helixi1923 – 1925Combined sources3
Helixi1929 – 1945Combined sources17
Helixi1947 – 1953Combined sources7
Helixi1973 – 1989Combined sources17
Helixi1999 – 2001Combined sources3
Helixi2004 – 2012Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E9LX-ray1.95A1760-2016[»]
3ENBX-ray1.85A/B1769-1990[»]
3JCRelectron microscopy7.00A1-2335[»]
3LRUX-ray1.85A/B1831-1990[»]
4JK7X-ray1.40A/B1769-1990[»]
4JK8X-ray1.15A/B1769-1990[»]
4JK9X-ray1.50A/B1769-1990[»]
4JKAX-ray1.32A/B1769-1990[»]
4JKBX-ray1.30A/B1769-1990[»]
4JKCX-ray1.50A/B1769-1990[»]
4JKDX-ray1.55A/B1769-1990[»]
4JKEX-ray1.65A/B1769-1990[»]
4JKFX-ray1.95A/B1769-1990[»]
4JKGX-ray1.80A/B1769-1990[»]
4JKHX-ray1.80A/B1769-1990[»]
4KITX-ray3.60C2064-2335[»]
5MQFelectron microscopy5.90A1-2335[»]
5O9Zelectron microscopy4.50A1-2335[»]
5XJCelectron microscopy3.60A1-2335[»]
ProteinModelPortaliQ6P2Q9
SMRiQ6P2Q9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P2Q9

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2103 – 2234MPNPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni812 – 1303Reverse transcriptase homology domainAdd BLAST492
Regioni1304 – 1577LinkerAdd BLAST274
Regioni1513 – 1526Important for branch point selectionBy similarityAdd BLAST14
Regioni1581 – 1752Restriction endonuclease homology domainAdd BLAST172
Regioni1669 – 2034Involved in interaction with pre-mRNA 5' splice siteAdd BLAST366
Regioni1767 – 2020RNase H homology domainAdd BLAST254
Regioni2301 – 2335Required for interaction with EFTUD2 and SNRNP2001 PublicationAdd BLAST35

Domaini

The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion.By similarity
Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved.By similarity
Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize the protein structure.By similarity
Contains a region with structural similarity to RNase H, but lacks RNase H activity.By similarity

Phylogenomic databases

eggNOGiKOG1795 Eukaryota
COG5178 LUCA
GeneTreeiENSGT00390000015210
HOGENOMiHOG000184103
HOVERGENiHBG052796
InParanoidiQ6P2Q9
KOiK12856
OMAiQNKVNTV
OrthoDBiEOG091G003B
PhylomeDBiQ6P2Q9
TreeFamiTF105613

Family and domain databases

CDDicd13838 RNase_H_like_Prp8_IV, 1 hit
InterProiView protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR012591 PRO8NT
IPR012592 PROCN
IPR012984 PROCT
IPR027652 PRP8
IPR021983 PRP8_domainIV
IPR019581 Prp8_U5-snRNA-bd
IPR019580 Prp8_U6-snRNA-bd
IPR012337 RNaseH-like_sf
IPR019582 RRM_spliceosomal_PrP8
PANTHERiPTHR11140 PTHR11140, 1 hit
PfamiView protein in Pfam
PF01398 JAB, 1 hit
PF08082 PRO8NT, 1 hit
PF08083 PROCN, 1 hit
PF08084 PROCT, 1 hit
PF12134 PRP8_domainIV, 1 hit
PF10598 RRM_4, 1 hit
PF10597 U5_2-snRNA_bdg, 1 hit
PF10596 U6-snRNA_bdg, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD149576 Pre-mRNA-splicing_factor-8, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
SUPFAMiSSF53098 SSF53098, 2 hits
PROSITEiView protein in PROSITE
PS50249 MPN, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q6P2Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK
60 70 80 90 100
FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL
110 120 130 140 150
KLLENMPMPW EQIRDVPVLY HITGAISFVN EIPWVIEPVY ISQWGSMWIM
160 170 180 190 200
MRREKRDRRH FKRMRFPPFD DEEPPLDYAD NILDVEPLEA IQLELDPEED
210 220 230 240 250
APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR LANQLLTDLV
260 270 280 290 300
DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
310 320 330 340 350
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF
360 370 380 390 400
YFDPLINPIS HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN
410 420 430 440 450
GIALLWAPRP FNLRSGRTRR ALDIPLVKNW YREHCPAGQP VKVRVSYQKL
460 470 480 490 500
LKYYVLNALK HRPPKAQKKR YLFRSFKATK FFQSTKLDWV EVGLQVCRQG
510 520 530 540 550
YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF GNAFHLCREV
560 570 580 590 600
LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
610 620 630 640 650
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER
660 670 680 690 700
WLGNLLARQF EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG
710 720 730 740 750
IKQNKARTIL QHLSEAWRCW KANIPWKVPG LPTPIENMIL RYVKAKADWW
760 770 780 790 800
TNTAHYNRER IRRGATVDKT VCKKNLGRLT RLYLKAEQER QHNYLKDGPY
810 820 830 840 850
ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY
860 870 880 890 900
SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
910 920 930 940 950
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL
960 970 980 990 1000
LVYKWCQGIN NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI
1010 1020 1030 1040 1050
VDHNIADYMT AKNNVVINYK DMNHTNSYGI IRGLQFASFI VQYYGLVMDL
1060 1070 1080 1090 1100
LVLGLHRASE MAGPPQMPND FLSFQDIATE AAHPIRLFCR YIDRIHIFFR
1110 1120 1130 1140 1150
FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM RLMKHDVNLG
1160 1170 1180 1190 1200
RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
1210 1220 1230 1240 1250
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA
1260 1270 1280 1290 1300
SGSTTFTKIV NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK
1310 1320 1330 1340 1350
IGLNSKMPSR FPPVVFYTPK ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI
1360 1370 1380 1390 1400
THFRSGMSHE EDQLIPNLYR YIQPWESEFI DSQRVWAEYA LKRQEAIAQN
1410 1420 1430 1440 1450
RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT DFKQYQVLKQ
1460 1470 1480 1490 1500
NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
1510 1520 1530 1540 1550
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG
1560 1570 1580 1590 1600
FQVQLDLTGI FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE
1610 1620 1630 1640 1650
LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD
1660 1670 1680 1690 1700
VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTTD NMSIYPSPTG
1710 1720 1730 1740 1750
VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL YVLRERIRKG
1760 1770 1780 1790 1800
LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
1810 1820 1830 1840 1850
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR
1860 1870 1880 1890 1900
SLPVEEQPKQ IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE
1910 1920 1930 1940 1950
KFGDLILKAT EPQMVLFNLY DDWLKTISSY TAFSRLILIL RALHVNNDRA
1960 1970 1980 1990 2000
KVILKPDKTT ITEPHHIWPT LTDEEWIKVE VQLKDLILAD YGKKNNVNVA
2010 2020 2030 2040 2050
SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT ATQTRTVNKH
2060 2070 2080 2090 2100
GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
2110 2120 2130 2140 2150
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ
2160 2170 2180 2190 2200
WGTHQTVHLP GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM
2210 2220 2230 2240 2250
ADNPSWDGEK TIIITCSFTP GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG
2260 2270 2280 2290 2300
YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN YNFMGVRHDP NMKYELQLAN
2310 2320 2330
PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA
Length:2,335
Mass (Da):273,600
Last modified:June 7, 2005 - v2
Checksum:iE823A15C60EA61C9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184D → N in BAA22563 (Ref. 2) Curated1
Sequence conflicti492 – 493VG → GW in BAA22563 (Ref. 2) Curated2
Sequence conflicti604M → V in BAA22563 (Ref. 2) Curated1
Sequence conflicti806A → T in BAA22563 (Ref. 2) Curated1
Sequence conflicti997L → V in BAA22563 (Ref. 2) Curated1
Sequence conflicti1390A → S in BAA22563 (Ref. 2) Curated1
Sequence conflicti1867G → D in BAA22563 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02262268K → E. Corresponds to variant dbSNP:rs1043391Ensembl.1
Natural variantiVAR_022623227R → H1 PublicationCorresponds to variant dbSNP:rs11559304Ensembl.1
Natural variantiVAR_022624874P → L1 PublicationCorresponds to variant dbSNP:rs1043396Ensembl.1
Natural variantiVAR_0226251293N → H1 PublicationCorresponds to variant dbSNP:rs1043399Ensembl.1
Natural variantiVAR_0226262301P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 PublicationCorresponds to variant dbSNP:rs121434239EnsemblClinVar.1
Natural variantiVAR_0226272304F → L in RP13. 2 PublicationsCorresponds to variant dbSNP:rs121434240EnsemblClinVar.1
Natural variantiVAR_0226282309H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant dbSNP:rs121434236EnsemblClinVar.1
Natural variantiVAR_0226292309H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant dbSNP:rs121434236EnsemblClinVar.1
Natural variantiVAR_0226302310R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 4 Publications1
Natural variantiVAR_0226312310R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 PublicationsCorresponds to variant dbSNP:rs121434238EnsemblClinVar.1
Natural variantiVAR_0226322314F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 2 Publications1
Natural variantiVAR_0226332334Y → N in RP13. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092565 mRNA Translation: AAC61776.1
AB007510 mRNA Translation: BAA22563.1
BC064370 mRNA Translation: AAH64370.1
CCDSiCCDS11010.1
RefSeqiNP_006436.3, NM_006445.3
UniGeneiHs.181368

Genome annotation databases

EnsembliENST00000304992; ENSP00000304350; ENSG00000174231
ENST00000572621; ENSP00000460348; ENSG00000174231
ENST00000614672; ENSP00000479194; ENSG00000274442
ENST00000634039; ENSP00000488611; ENSG00000274442
GeneIDi10594
KEGGihsa:10594
UCSCiuc002fte.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPRP8_HUMAN
AccessioniPrimary (citable) accession number: Q6P2Q9
Secondary accession number(s): O14547, O75965
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 23, 2018
This is version 160 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome

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