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Protein

Regulation of nuclear pre-mRNA domain-containing protein 1B

Gene

RPRD1B

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

Functioni

Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation.2 Publications

GO - Molecular functioni

  • RNA polymerase II core binding Source: UniProtKB

GO - Biological processi

  • dephosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of cell cycle process Source: UniProtKB
  • snRNA transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulation of nuclear pre-mRNA domain-containing protein 1B
Alternative name(s):
Cell cycle-related and expression-elevated protein in tumor
Gene namesi
Name:RPRD1B
Synonyms:C20orf77, CREPT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16209. RPRD1B.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HPA
  • cytoplasm Source: HPA
  • DNA-directed RNA polymerase II, holoenzyme Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402043.

Polymorphism and mutation databases

BioMutaiRPRD1B.
DMDMi23813907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 326325Regulation of nuclear pre-mRNA domain-containing protein 1BPRO_0000079441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei134 – 1341PhosphoserineCombined sources
Modified residuei161 – 1611PhosphotyrosineCombined sources
Modified residuei166 – 1661PhosphoserineCombined sources
Modified residuei299 – 2991PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NQG5.
MaxQBiQ9NQG5.
PaxDbiQ9NQG5.
PeptideAtlasiQ9NQG5.
PRIDEiQ9NQG5.

PTM databases

iPTMnetiQ9NQG5.
PhosphoSiteiQ9NQG5.

Expressioni

Tissue specificityi

Preferentially expressed in a range of tumor tissues including colon, lung, liver, breast, prostate, stomach, uterine endometrium and cervical cancers with higher levels in tumors than in adjacent non-tumor tissue (at protein level).1 Publication

Gene expression databases

BgeeiQ9NQG5.
CleanExiHS_RPRD1B.
ExpressionAtlasiQ9NQG5. baseline and differential.
GenevisibleiQ9NQG5. HS.

Interactioni

Subunit structurei

Associates with the RNA polymerase II complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POLR2AP249285EBI-747925,EBI-295301

GO - Molecular functioni

  • RNA polymerase II core binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121820. 79 interactions.
DIPiDIP-61537N.
IntActiQ9NQG5. 11 interactions.
MINTiMINT-1475221.
STRINGi9606.ENSP00000362532.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Helixi20 – 3213Combined sources
Helixi34 – 363Combined sources
Helixi37 – 5014Combined sources
Helixi53 – 553Combined sources
Helixi56 – 7015Combined sources
Turni71 – 733Combined sources
Helixi76 – 827Combined sources
Helixi85 – 11329Combined sources
Helixi119 – 12911Combined sources
Helixi177 – 20226Combined sources
Helixi206 – 2083Combined sources
Helixi211 – 2166Combined sources
Helixi220 – 29879Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FLAX-ray2.20A/B/C/D172-305[»]
4FU3X-ray1.90A/B2-135[»]
4HFGX-ray2.00A/B2-135[»]
4NADX-ray2.80A/B177-326[»]
4Q94X-ray1.85A/B2-135[»]
4Q96X-ray1.85A/B/D/E2-135[»]
ProteinModelPortaliQ9NQG5.
SMRiQ9NQG5. Positions 2-129, 177-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 133132CIDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the UPF0400 (RTT103) family.Curated
Contains 1 CID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2669. Eukaryota.
ENOG410XRAP. LUCA.
GeneTreeiENSGT00400000022016.
HOGENOMiHOG000007456.
HOVERGENiHBG051177.
InParanoidiQ9NQG5.
KOiK15559.
OMAiPFTEEAD.
OrthoDBiEOG7V1FRR.
PhylomeDBiQ9NQG5.
TreeFamiTF320926.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR032337. CREPT.
IPR008942. ENTH_VHS.
IPR006903. RNA_pol_II-bd.
[Graphical view]
PfamiPF16566. CREPT. 1 hit.
PF04818. CTD_bind. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NQG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFSESALE KKLSELSNSQ QSVQTLSLWL IHHRKHAGPI VSVWHRELRK
60 70 80 90 100
AKSNRKLTFL YLANDVIQNS KRKGPEFTRE FESVLVDAFS HVAREADEGC
110 120 130 140 150
KKPLERLLNI WQERSVYGGE FIQQLKLSME DSKSPPPKAT EEKKSLKRTF
160 170 180 190 200
QQIQEEEDDD YPGSYSPQDP SAGPLLTEEL IKALQDLENA ASGDATVRQK
210 220 230 240 250
IASLPQEVQD VSLLEKITDK EAAERLSKTV DEACLLLAEY NGRLAAELED
260 270 280 290 300
RRQLARMLVE YTQNQKDVLS EKEKKLEEYK QKLARVTQVR KELKSHIQSL
310 320
PDLSLLPNVT GGLAPLPSAG DLFSTD
Length:326
Mass (Da):36,900
Last modified:October 1, 2000 - v1
Checksum:i9057EEF6F3D18215
GO

Sequence cautioni

The sequence AAH01696.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Q → H in AAH33629 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ372938 mRNA. Translation: ABD34791.1.
AK312468 mRNA. Translation: BAG35375.1.
AL109823 Genomic DNA. Translation: CAC01532.1.
CH471077 Genomic DNA. Translation: EAW76045.1.
BC001696 mRNA. Translation: AAH01696.1. Sequence problems.
BC033629 mRNA. Translation: AAH33629.1.
CCDSiCCDS13301.1.
RefSeqiNP_067038.1. NM_021215.3.
UniGeneiHs.278839.

Genome annotation databases

EnsembliENST00000373433; ENSP00000362532; ENSG00000101413.
GeneIDi58490.
KEGGihsa:58490.
UCSCiuc002xho.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ372938 mRNA. Translation: ABD34791.1.
AK312468 mRNA. Translation: BAG35375.1.
AL109823 Genomic DNA. Translation: CAC01532.1.
CH471077 Genomic DNA. Translation: EAW76045.1.
BC001696 mRNA. Translation: AAH01696.1. Sequence problems.
BC033629 mRNA. Translation: AAH33629.1.
CCDSiCCDS13301.1.
RefSeqiNP_067038.1. NM_021215.3.
UniGeneiHs.278839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FLAX-ray2.20A/B/C/D172-305[»]
4FU3X-ray1.90A/B2-135[»]
4HFGX-ray2.00A/B2-135[»]
4NADX-ray2.80A/B177-326[»]
4Q94X-ray1.85A/B2-135[»]
4Q96X-ray1.85A/B/D/E2-135[»]
ProteinModelPortaliQ9NQG5.
SMRiQ9NQG5. Positions 2-129, 177-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121820. 79 interactions.
DIPiDIP-61537N.
IntActiQ9NQG5. 11 interactions.
MINTiMINT-1475221.
STRINGi9606.ENSP00000362532.

PTM databases

iPTMnetiQ9NQG5.
PhosphoSiteiQ9NQG5.

Polymorphism and mutation databases

BioMutaiRPRD1B.
DMDMi23813907.

Proteomic databases

EPDiQ9NQG5.
MaxQBiQ9NQG5.
PaxDbiQ9NQG5.
PeptideAtlasiQ9NQG5.
PRIDEiQ9NQG5.

Protocols and materials databases

DNASUi58490.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373433; ENSP00000362532; ENSG00000101413.
GeneIDi58490.
KEGGihsa:58490.
UCSCiuc002xho.5. human.

Organism-specific databases

CTDi58490.
GeneCardsiRPRD1B.
H-InvDBHIX0015799.
HGNCiHGNC:16209. RPRD1B.
MIMi614694. gene.
neXtProtiNX_Q9NQG5.
PharmGKBiPA162402043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2669. Eukaryota.
ENOG410XRAP. LUCA.
GeneTreeiENSGT00400000022016.
HOGENOMiHOG000007456.
HOVERGENiHBG051177.
InParanoidiQ9NQG5.
KOiK15559.
OMAiPFTEEAD.
OrthoDBiEOG7V1FRR.
PhylomeDBiQ9NQG5.
TreeFamiTF320926.

Enzyme and pathway databases

ReactomeiR-HSA-6807505. RNA polymerase II transcribes snRNA genes.

Miscellaneous databases

ChiTaRSiRPRD1B. human.
GenomeRNAii58490.
PROiQ9NQG5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQG5.
CleanExiHS_RPRD1B.
ExpressionAtlasiQ9NQG5. baseline and differential.
GenevisibleiQ9NQG5. HS.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR032337. CREPT.
IPR008942. ENTH_VHS.
IPR006903. RNA_pol_II-bd.
[Graphical view]
PfamiPF16566. CREPT. 1 hit.
PF04818. CTD_bind. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CREPT accelerates tumorigenesis by regulating the transcription of cell-cycle-related genes."
    Lu D., Wu Y., Wang Y., Ren F., Wang D., Su F., Zhang Y., Yang X., Jin G., Hao X., He D., Zhai Y., Irwin D.M., Hu J., Sung J.J., Yu J., Jia B., Chang Z.
    Cancer Cell 21:92-104(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RNA POLYMERASE II, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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.
    , 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].
    Tissue: Hippocampus.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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: Melanoma.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, FUNCTION.
  13. "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 SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134 AND TYR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRPR1B_HUMAN
AccessioniPrimary (citable) accession number: Q9NQG5
Secondary accession number(s): Q1WDE7, Q6PKF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 117 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 20
    Human chromosome 20: 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
  4. SIMILARITY comments
    Index of protein domains and families
  5. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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 one 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.