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Q5VT52 (RPRD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulation of nuclear pre-mRNA domain-containing protein 2
Gene names
Name:RPRD2
Synonyms:KIAA0460
ORF Names:HSPC099
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Associates with the RNA polymerase II complex. Ref.18

Sequence similarities

Contains 1 CID domain.

Sequence caution

The sequence AAF28922.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH45623.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from direct assay Ref.18. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5VT52-1)

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.
Isoform 2 (identifier: Q5VT52-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5VT52-3)

The sequence of this isoform differs from the canonical sequence as follows:
     146-171: Missing.
Isoform 4 (identifier: Q5VT52-4)

The sequence of this isoform differs from the canonical sequence as follows:
     147-152: TTFKTQ → KCLFLS
     153-1461: Missing.
Note: Gene prediction based on EST data.
Isoform 5 (identifier: Q5VT52-5)

The sequence of this isoform differs from the canonical sequence as follows:
     146-171: Missing.
     932-960: SKNDSFFTPDSNHNSLSQSTTGHLSLPQK → KHPCRSHGSPTHVRRGESPGLHHFHHVDD
     961-1461: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14611461Regulation of nuclear pre-mRNA domain-containing protein 2
PRO_0000244355

Regions

Domain19 – 149131CID
Compositional bias4 – 1916Gly/Ser-rich
Compositional bias457 – 950494Ser-rich
Compositional bias1054 – 10574Poly-Gln
Compositional bias1152 – 11587Poly-Gly
Compositional bias1195 – 1459265Pro-rich

Amino acid modifications

Modified residue3561Phosphoserine Ref.17
Modified residue3581Phosphothreonine Ref.17
Modified residue3741Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17
Modified residue4731Phosphoserine Ref.14 Ref.15
Modified residue4761Phosphoserine Ref.14
Modified residue4791Phosphoserine Ref.12
Modified residue4821Phosphothreonine Ref.14 Ref.15
Modified residue4851Phosphoserine Ref.12 Ref.14
Modified residue5171Phosphothreonine Ref.12 Ref.15
Modified residue5931Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17
Modified residue5981Phosphothreonine Ref.14
Modified residue6141Phosphoserine Ref.10 Ref.12 Ref.14 Ref.15
Modified residue6651Phosphoserine Ref.14
Modified residue7231Phosphothreonine Ref.9 Ref.12 Ref.15
Modified residue7321Phosphothreonine Ref.14
Modified residue7581Phosphoserine Ref.10 Ref.12
Modified residue7621Phosphoserine Ref.10
Modified residue8261Phosphoserine Ref.14
Modified residue9001Phosphoserine Ref.12
Modified residue9091Phosphoserine Ref.12 Ref.14
Modified residue9281Phosphoserine Ref.12 Ref.15
Modified residue10681Phosphoserine By similarity
Modified residue10991Phosphoserine Ref.9 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 3737Missing in isoform 2.
VSP_019546
Alternative sequence146 – 17126Missing in isoform 3 and isoform 5.
VSP_019547
Alternative sequence147 – 1526TTFKTQ → KCLFLS in isoform 4.
VSP_035574
Alternative sequence153 – 14611309Missing in isoform 4.
VSP_035575
Alternative sequence932 – 96029SKNDS…SLPQK → KHPCRSHGSPTHVRRGESPG LHHFHHVDD in isoform 5.
VSP_053733
Alternative sequence961 – 1461501Missing in isoform 5.
VSP_053734
Natural variant3511M → V.
Corresponds to variant rs41273537 [ dbSNP | Ensembl ].
VAR_061700

Experimental info

Sequence conflict1671W → C in AAF28922. Ref.6
Sequence conflict1741T → A in BAG51793. Ref.1
Sequence conflict12971P → L in BAG51793. Ref.1
Sequence conflict13851G → R in BAG51793. Ref.1

Secondary structure

.................... 1461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: E08CAF3148F89F67

FASTA1,461156,020
        10         20         30         40         50         60 
MAAGGGGGSS KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHSTIVY 

        70         80         90        100        110        120 
HWMKWLRRSA YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSV 

       130        140        150        160        170        180 
ERIFKIWEDR NVYPEEMIVA LREALSTTFK TQKQLKENLN KQPNKQWKKS QTSTNPKAAL 

       190        200        210        220        230        240 
KSKIVAEFRS QALIEELLLY KRSEDQIELK EKQLSTMRVD VCSTETLKCL KDKTGGKKFS 

       250        260        270        280        290        300 
KEFEEASSKL EEFVNGLDKQ VKNGPSLTEA LENAGIFYEA QYKEVKVVAN AYKTFANRVN 

       310        320        330        340        350        360 
NLKKKLDQLK STLPDPEESP VPSPSMDAPS PTGSESPFQG MGGEESQSPT MESEKSATPE 

       370        380        390        400        410        420 
PVTDNRDVED MELSDVEDDG SKIIVEDRKE KPAEKSAVST SVPTKPTENI SKASSCTPVP 

       430        440        450        460        470        480 
VTMTATPPLP KPVNTSLSPS PALALPNLAN VDLAKISSIL SSLTSVMKNT GVSPASRPSP 

       490        500        510        520        530        540 
GTPTSPSNLT SGLKTPAPAT TTSHNPLANI LSKVEITPES ILSALSKTQT QSAPALQGLS 

       550        560        570        580        590        600 
SLLQSVTGNP VPASEAASQS TSASPANTTV STIKGRNLPS SAQPFIPKSF NYSPNSSTSE 

       610        620        630        640        650        660 
VSSTSASKAS IGQSPGLPST TFKLPSNSLG FTATHNTSPA APPTEVTICQ SSEVSKPKLE 

       670        680        690        700        710        720 
SESTSPSLEM KIHNFLKGNP GFSGLNLNIP ILSSLGSSAP SESHPSDFQR GPTSTSIDNI 

       730        740        750        760        770        780 
DGTPVRDERS GTPTQDEMMD KPTSSSVDTM SLLSKIISPG SSTPSSTRSP PPGRDESYPR 

       790        800        810        820        830        840 
ELSNSVSTYR PFGLGSESPY KQPSDGMERP SSLMDSSQEK FYPDTSFQED EDYRDFEYSG 

       850        860        870        880        890        900 
PPPSAMMNLE KKPAKSILKS SKLSDTTEYQ PILSSYSHRA QEFGVKSAFP PSVRALLDSS 

       910        920        930        940        950        960 
ENCDRLSSSP GLFGAFSVRG NEPGSDRSPS PSKNDSFFTP DSNHNSLSQS TTGHLSLPQK 

       970        980        990       1000       1010       1020 
QYPDSPHPVP HRSLFSPQNT LAAPTGHPPT SGVEKVLAST ISTTSTIEFK NMLKNASRKP 

      1030       1040       1050       1060       1070       1080 
SDDKHFGQAP SKGTPSDGVS LSNLTQPSLT ATDQQQQEEH YRIETRVSSS CLDLPDSTEE 

      1090       1100       1110       1120       1130       1140 
KGAPIETLGY HSASNRRMSG EPIQTVESIR VPGKGNRGHG REASRVGWFD LSTSGSSFDN 

      1150       1160       1170       1180       1190       1200 
GPSSASELAS LGGGGSGGLT GFKTAPYKER APQFQESVGS FRSNSFNSTF EHHLPPSPLE 

      1210       1220       1230       1240       1250       1260 
HGTPFQREPV GPSSAPPVPP KDHGGIFSRD APTHLPSVDL SNPFTKEAAL AHAAPPPPPG 

      1270       1280       1290       1300       1310       1320 
EHSGIPFPTP PPPPPPGEHS SSGGSGVPFS TPPPPPPPVD HSGVVPFPAP PLAEHGVAGA 

      1330       1340       1350       1360       1370       1380 
VAVFPKDHSS LLQGTLAEHF GVLPGPRDHG GPTQRDLNGP GLSRVRESLT LPSHSLEHLG 

      1390       1400       1410       1420       1430       1440 
PPHGGGGGGG SNSSSGPPLG PSHRDTISRS GIILRSPRPD FRPREPFLSR DPFHSLKRPR 

      1450       1460 
PPFARGPPFF APKRPFFPPR Y 

« Hide

Isoform 2 [UniParc].

Checksum: EFB18C42C73F5B93
Show »

FASTA1,424152,588
Isoform 3 [UniParc].

Checksum: 3425769AF329312E
Show »

FASTA1,435152,876
Isoform 4 [UniParc].

Checksum: 4FFBE10E974AC878
Show »

FASTA15217,001
Isoform 5 [UniParc].

Checksum: A3D3BB446939BB42
Show »

FASTA934100,272

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
Tissue: Placenta and Trachea.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Salivary gland.
[3]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 3).
Tissue: Testis.
[6]"Human partial CDS cloned from CD34+ stem cells."
Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 (ISOFORM 1).
Tissue: Umbilical cord blood.
[7]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1461 (ISOFORM 1).
Tissue: Brain.
[8]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; THR-723 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-758 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[12]"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-374; SER-479; SER-485; THR-517; SER-593; SER-614; THR-723; SER-758; SER-900; SER-909; SER-928 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 SER-374; SER-473; SER-476; THR-482; SER-485; SER-593; THR-598; SER-614; SER-665; THR-732; SER-826; SER-909 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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 SER-374; SER-473; THR-482; THR-517; SER-593; SER-614; THR-723; SER-928 AND SER-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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-356; THR-358; SER-374 AND SER-593, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Control of the RNA polymerase II phosphorylation state in promoter regions by CTD interaction domain-containing proteins RPRD1A and RPRD1B."
Ni Z., Olsen J.B., Guo X., Zhong G., Ruan E.D., Marcon E., Young P., Guo H., Li J., Moffat J., Emili A., Greenblatt J.F.
Transcription 2:237-242(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK056707 mRNA. Translation: BAG51793.1.
AK291703 mRNA. Translation: BAF84392.1.
AK304380 mRNA. Translation: BAG65218.1.
BX641025 mRNA. Translation: CAE46016.1.
AL356356, AL611942, BX284695 Genomic DNA. Translation: CAI15496.1.
AL356356, AL611942, BX284695 Genomic DNA. Translation: CAI15497.1.
AL611942, AL356356, BX284695 Genomic DNA. Translation: CAH70313.1.
AL611942, AL356356, BX284695 Genomic DNA. Translation: CAH70314.1.
AL611942 Genomic DNA. Translation: CAH70315.1.
BX284695, AL356356, AL611942 Genomic DNA. Translation: CAI17373.1.
BX284695, AL356356, AL611942 Genomic DNA. Translation: CAI17374.1.
CH471121 Genomic DNA. Translation: EAW53552.1.
BC045623 mRNA. Translation: AAH45623.2. Different initiation.
AF161362 mRNA. Translation: AAF28922.1. Different initiation.
AB007929 mRNA. Translation: BAA32305.2.
CCDSCCDS44216.1. [Q5VT52-1]
PIRT00074.
RefSeqNP_056018.2. NM_015203.3. [Q5VT52-1]
XP_005245088.1. XM_005245031.2. [Q5VT52-3]
XP_005245089.1. XM_005245032.2. [Q5VT52-5]
UniGeneHs.213666.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FLBX-ray1.80A19-149[»]
ProteinModelPortalQ5VT52.
SMRQ5VT52. Positions 19-149, 190-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116852. 14 interactions.
IntActQ5VT52. 4 interactions.
MINTMINT-1603162.

PTM databases

PhosphoSiteQ5VT52.

Polymorphism databases

DMDM74746888.

Proteomic databases

MaxQBQ5VT52.
PaxDbQ5VT52.
PRIDEQ5VT52.

Protocols and materials databases

DNASU23248.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369067; ENSP00000358063; ENSG00000163125. [Q5VT52-4]
ENST00000369068; ENSP00000358064; ENSG00000163125. [Q5VT52-1]
ENST00000401000; ENSP00000383785; ENSG00000163125. [Q5VT52-3]
ENST00000539519; ENSP00000445482; ENSG00000163125. [Q5VT52-5]
ENST00000579067; ENSP00000462536; ENSG00000266562. [Q5VT52-3]
ENST00000582942; ENSP00000463855; ENSG00000266562. [Q5VT52-5]
ENST00000584319; ENSP00000464492; ENSG00000266562. [Q5VT52-4]
ENST00000584841; ENSP00000463897; ENSG00000266562. [Q5VT52-1]
GeneID23248.
KEGGhsa:23248.
UCSCuc001eup.4. human. [Q5VT52-3]
uc009wlr.3. human. [Q5VT52-1]

Organism-specific databases

CTD23248.
GeneCardsGC01P150335.
H-InvDBHIX0019981.
HGNCHGNC:29039. RPRD2.
HPAHPA045778.
MIM614695. gene.
neXtProtNX_Q5VT52.
PharmGKBPA162402062.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331230.
HOVERGENHBG104176.
InParanoidQ5VT52.
OMATLGYHNA.
PhylomeDBQ5VT52.
TreeFamTF320926.

Gene expression databases

ArrayExpressQ5VT52.
BgeeQ5VT52.
CleanExHS_RPRD2.
GenevestigatorQ5VT52.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR006903. RNA_pol_II-bd.
[Graphical view]
PfamPF04818. CTD_bind. 1 hit.
[Graphical view]
SMARTSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS51391. CID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPRD2. human.
GeneWikiKIAA0460.
GenomeRNAi23248.
NextBio35477341.
PROQ5VT52.
SOURCESearch...

Entry information

Entry nameRPRD2_HUMAN
AccessionPrimary (citable) accession number: Q5VT52
Secondary accession number(s): A8K6N8 expand/collapse secondary AC list , B3KPT1, B4E2Q6, O75048, Q5VT51, Q5VT53, Q6MZL4, Q86XD2, Q9P0D7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 92 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM