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Protein

Protein RRP5 homolog

Gene

PDCD11

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

Functioni

Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA.1 Publication
Involved in the biogenesis of rRNA.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: GO_Central
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

rRNA processing

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RRP5 homolog
Alternative name(s):
NF-kappa-B-binding protein
Short name:
NFBP
Programmed cell death protein 11
Gene namesi
Name:PDCD11
Synonyms:KIAA0185
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:13408. PDCD11.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • nucleolus Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • small-subunit processome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134909758.

Polymorphism and mutation databases

BioMutaiPDCD11.
DMDMi145559523.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 18711870Protein RRP5 homologPRO_0000205762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei7 – 71PhosphoserineCombined sources
Modified residuei438 – 4381PhosphoserineCombined sources
Cross-linki1030 – 1030Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei1360 – 13601PhosphoserineCombined sources
Modified residuei1362 – 13621PhosphoserineCombined sources
Modified residuei1476 – 14761PhosphoserineBy similarity
Modified residuei1493 – 14931PhosphoserineCombined sources
Modified residuei1498 – 14981PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14690.
MaxQBiQ14690.
PaxDbiQ14690.
PeptideAtlasiQ14690.
PRIDEiQ14690.

2D gel databases

SWISS-2DPAGEQ14690.

PTM databases

iPTMnetiQ14690.
PhosphoSiteiQ14690.
SwissPalmiQ14690.

Expressioni

Gene expression databases

BgeeiQ14690.
CleanExiHS_PDCD11.
ExpressionAtlasiQ14690. baseline and differential.
GenevisibleiQ14690. HS.

Organism-specific databases

HPAiCAB026472.
HPA017924.

Interactioni

Subunit structurei

Interacts with NF-kappa-B p50/NFKB1 and NF-kappa-B p65/RELA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NFKB1P198382EBI-300028,EBI-300010

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116633. 43 interactions.
IntActiQ14690. 16 interactions.
MINTiMINT-1388150.
STRINGi9606.ENSP00000358812.

Structurei

Secondary structure

1
1871
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni181 – 1833Combined sources
Beta strandi189 – 1979Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi212 – 2165Combined sources
Helixi217 – 22711Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi252 – 2565Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI5NMR-A173-278[»]
ProteinModelPortaliQ14690.
SMRiQ14690. Positions 173-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14690.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 17189S1 motif 1PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 25872S1 motif 2PROSITE-ProRule annotationAdd
BLAST
Domaini281 – 34666S1 motif 3PROSITE-ProRule annotationAdd
BLAST
Domaini365 – 43672S1 motif 4PROSITE-ProRule annotationAdd
BLAST
Domaini453 – 52270S1 motif 5PROSITE-ProRule annotationAdd
BLAST
Domaini542 – 61170S1 motif 6PROSITE-ProRule annotationAdd
BLAST
Domaini636 – 70772S1 motif 7PROSITE-ProRule annotationAdd
BLAST
Domaini729 – 79870S1 motif 8PROSITE-ProRule annotationAdd
BLAST
Domaini1036 – 110974S1 motif 9PROSITE-ProRule annotationAdd
BLAST
Domaini1149 – 122274S1 motif 10PROSITE-ProRule annotationAdd
BLAST
Domaini1230 – 129869S1 motif 11PROSITE-ProRule annotationAdd
BLAST
Domaini1324 – 139673S1 motif 12PROSITE-ProRule annotationAdd
BLAST
Repeati1599 – 163133HAT 1Add
BLAST
Repeati1705 – 173733HAT 2Add
BLAST
Repeati1775 – 180733HAT 3Add
BLAST
Repeati1809 – 184436HAT 4Add
BLAST

Sequence similaritiesi

Contains 4 HAT repeats.Curated
Contains 12 S1 motif domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1070. Eukaryota.
COG0539. LUCA.
GeneTreeiENSGT00390000012228.
HOGENOMiHOG000088607.
HOVERGENiHBG108419.
InParanoidiQ14690.
KOiK14792.
OMAiLCHRSEM.
OrthoDBiEOG7Q2N55.
PhylomeDBiQ14690.
TreeFamiTF105697.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.50.140. 11 hits.
InterProiIPR003107. HAT.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR008847. Suf.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF00575. S1. 4 hits.
PF05843. Suf. 1 hit.
[Graphical view]
SMARTiSM00386. HAT. 7 hits.
SM00316. S1. 13 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
SSF50249. SSF50249. 11 hits.
PROSITEiPS50126. S1. 12 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q14690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANLEESFPR GGTRKIHKPE KAFQQSVEQD NLFDISTEEG STKRKKSQKG
60 70 80 90 100
PAKTKKLKIE KRESSKSARE KFEILSVESL CEGMRILGCV KEVNELELVI
110 120 130 140 150
SLPNGLQGFV QVTEICDAYT KKLNEQVTQE QPLKDLLHLP ELFSPGMLVR
160 170 180 190 200
CVVSSLGITD RGKKSVKLSL NPKNVNRVLS AEALKPGMLL TGTVSSLEDH
210 220 230 240 250
GYLVDIGVDG TRAFLPLLKA QEYIRQKNKG AKLKVGQYLN CIVEKVKGNG
260 270 280 290 300
GVVSLSVGHS EVSTAIATEQ QSWNLNNLLP GLVVKAQVQK VTPFGLTLNF
310 320 330 340 350
LTFFTGVVDF MHLDPKKAGT YFSNQAVRAC ILCVHPRTRV VHLSLRPIFL
360 370 380 390 400
QPGRPLTRLS CQNLGAVLDD VPVQGFFKKA GATFRLKDGV LAYARLSHLS
410 420 430 440 450
DSKNVFNPEA FKPGNTHKCR IIDYSQMDEL ALLSLRTSII EAQYLRYHDI
460 470 480 490 500
EPGAVVKGTV LTIKSYGMLV KVGEQMRGLV PPMHLADILM KNPEKKYHIG
510 520 530 540 550
DEVKCRVLLC DPEAKKLMMT LKKTLIESKL PVITCYADAK PGLQTHGFII
560 570 580 590 600
RVKDYGCIVK FYNNVQGLVP KHELSTEYIP DPERVFYTGQ VVKVVVLNCE
610 620 630 640 650
PSKERMLLSF KLSSDPEPKK EPAGHSQKKG KAINIGQLVD VKVLEKTKDG
660 670 680 690 700
LEVAVLPHNI RAFLPTSHLS DHVANGPLLH HWLQAGDILH RVLCLSQSEG
710 720 730 740 750
RVLLCRKPAL VSTVEGGQDP KNFSEIHPGM LLIGFVKSIK DYGVFIQFPS
760 770 780 790 800
GLSGLAPKAI MSDKFVTSTS DHFVEGQTVA AKVTNVDEEK QRMLLSLRLS
810 820 830 840 850
DCGLGDLAIT SLLLLNQCLE ELQGVRSLMS NRDSVLIQTL AEMTPGMFLD
860 870 880 890 900
LVVQEVLEDG SVVFSGGPVP DLVLKASRYH RAGQEVESGQ KKKVVILNVD
910 920 930 940 950
LLKLEVHVSL HQDLVNRKAR KLRKGSEHQA IVQHLEKSFA IASLVETGHL
960 970 980 990 1000
AAFSLTSHLN DTFRFDSEKL QVGQGVSLTL KTTEPGVTGL LLAVEGPAAK
1010 1020 1030 1040 1050
RTMRPTQKDS ETVDEDEEVD PALTVGTIKK HTLSIGDMVT GTVKSIKPTH
1060 1070 1080 1090 1100
VVVTLEDGII GCIHASHILD DVPEGTSPTT KLKVGKTVTA RVIGGRDMKT
1110 1120 1130 1140 1150
FKYLPISHPR FVRTIPELSV RPSELEDGHT ALNTHSVSPM EKIKQYQAGQ
1160 1170 1180 1190 1200
TVTCFLKKYN VVKKWLEVEI APDIRGRIPL LLTSLSFKVL KHPDKKFRVG
1210 1220 1230 1240 1250
QALRATVVGP DSSKTLLCLS LTGPHKLEEG EVAMGRVVKV TPNEGLTVSF
1260 1270 1280 1290 1300
PFGKIGTVSI FHMSDSYSET PLEDFVPQKV VRCYILSTAD NVLTLSLRSS
1310 1320 1330 1340 1350
RTNPETKSKV EDPEINSIQD IKEGQLLRGY VGSIQPHGVF FRLGPSVVGL
1360 1370 1380 1390 1400
ARYSHVSQHS PSKKALYNKH LPEGKLLTAR VLRLNHQKNL VELSFLPGDT
1410 1420 1430 1440 1450
GKPDVLSASL EGQLTKQEER KTEAEERDQK GEKKNQKRNE KKNQKGQEEV
1460 1470 1480 1490 1500
EMPSKEKQQP QKPQAQKRGG RECRESGSEQ ERVSKKPKKA GLSEEDDSLV
1510 1520 1530 1540 1550
DVYYREGKEE AEETNVLPKE KQTKPAEAPR LQLSSGFAWN VGLDSLTPAL
1560 1570 1580 1590 1600
PPLAESSDSE EDEKPHQATI KKSKKERELE KQKAEKELSR IEEALMDPGR
1610 1620 1630 1640 1650
QPESADDFDR LVLSSPNSSI LWLQYMAFHL QATEIEKARA VAERALKTIS
1660 1670 1680 1690 1700
FREEQEKLNV WVALLNLENM YGSQESLTKV FERAVQYNEP LKVFLHLADI
1710 1720 1730 1740 1750
YAKSEKFQEA GELYNRMLKR FRQEKAVWIK YGAFLLRRSQ AAASHRVLQR
1760 1770 1780 1790 1800
ALECLPSKEH VDVIAKFAQL EFQLGDAERA KAIFENTLST YPKRTDVWSV
1810 1820 1830 1840 1850
YIDMTIKHGS QKDVRDIFER VIHLSLAPKR MKFFFKRYLD YEKQHGTEKD
1860 1870
VQAVKAKALE YVEAKSSVLE D
Length:1,871
Mass (Da):208,701
Last modified:April 17, 2007 - v3
Checksum:i8ED3665EB503CBB0
GO

Sequence cautioni

The sequence AAG01992.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence AAH49838.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH64486.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH80560.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI11041.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA11502.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1431 – 14311Missing in AAH49838 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti397 – 3971S → N.
Corresponds to variant rs7074814 [ dbSNP | Ensembl ].
VAR_054485
Natural varianti623 – 6231A → S.
Corresponds to variant rs11598673 [ dbSNP | Ensembl ].
VAR_031669
Natural varianti780 – 7801A → S.
Corresponds to variant rs11591914 [ dbSNP | Ensembl ].
VAR_054486
Natural varianti1216 – 12161L → F.2 Publications
Corresponds to variant rs2986014 [ dbSNP | Ensembl ].
VAR_031670
Natural varianti1453 – 14531P → S.
Corresponds to variant rs2274289 [ dbSNP | Ensembl ].
VAR_054487
Natural varianti1871 – 18711D → A.1 Publication
Corresponds to variant rs7831 [ dbSNP | Ensembl ].
VAR_014930

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D80007 mRNA. Translation: BAA11502.1. Different initiation.
AL139339, AL591408, AL603983 Genomic DNA. Translation: CAH71487.1.
AL591408, AL139339, AL603983 Genomic DNA. Translation: CAI16749.1.
AL603983, AL139339, AL591408 Genomic DNA. Translation: CAI15102.1.
CH471066 Genomic DNA. Translation: EAW49641.1.
BC049838 mRNA. Translation: AAH49838.1. Sequence problems.
BC064486 mRNA. Translation: AAH64486.1. Sequence problems.
BC080560 mRNA. Translation: AAH80560.1. Sequence problems.
BC111040 mRNA. Translation: AAI11041.1. Sequence problems.
AY007124 mRNA. Translation: AAG01992.1. Sequence problems.
CCDSiCCDS31276.1.
RefSeqiNP_055791.1. NM_014976.1.
XP_011537841.1. XM_011539539.1.
UniGeneiHs.239499.

Genome annotation databases

EnsembliENST00000369797; ENSP00000358812; ENSG00000148843.
GeneIDi22984.
KEGGihsa:22984.
UCSCiuc001kwy.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D80007 mRNA. Translation: BAA11502.1. Different initiation.
AL139339, AL591408, AL603983 Genomic DNA. Translation: CAH71487.1.
AL591408, AL139339, AL603983 Genomic DNA. Translation: CAI16749.1.
AL603983, AL139339, AL591408 Genomic DNA. Translation: CAI15102.1.
CH471066 Genomic DNA. Translation: EAW49641.1.
BC049838 mRNA. Translation: AAH49838.1. Sequence problems.
BC064486 mRNA. Translation: AAH64486.1. Sequence problems.
BC080560 mRNA. Translation: AAH80560.1. Sequence problems.
BC111040 mRNA. Translation: AAI11041.1. Sequence problems.
AY007124 mRNA. Translation: AAG01992.1. Sequence problems.
CCDSiCCDS31276.1.
RefSeqiNP_055791.1. NM_014976.1.
XP_011537841.1. XM_011539539.1.
UniGeneiHs.239499.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI5NMR-A173-278[»]
ProteinModelPortaliQ14690.
SMRiQ14690. Positions 173-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116633. 43 interactions.
IntActiQ14690. 16 interactions.
MINTiMINT-1388150.
STRINGi9606.ENSP00000358812.

PTM databases

iPTMnetiQ14690.
PhosphoSiteiQ14690.
SwissPalmiQ14690.

Polymorphism and mutation databases

BioMutaiPDCD11.
DMDMi145559523.

2D gel databases

SWISS-2DPAGEQ14690.

Proteomic databases

EPDiQ14690.
MaxQBiQ14690.
PaxDbiQ14690.
PeptideAtlasiQ14690.
PRIDEiQ14690.

Protocols and materials databases

DNASUi22984.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369797; ENSP00000358812; ENSG00000148843.
GeneIDi22984.
KEGGihsa:22984.
UCSCiuc001kwy.2. human.

Organism-specific databases

CTDi22984.
GeneCardsiPDCD11.
H-InvDBHIX0009176.
HGNCiHGNC:13408. PDCD11.
HPAiCAB026472.
HPA017924.
MIMi612333. gene.
neXtProtiNX_Q14690.
PharmGKBiPA134909758.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1070. Eukaryota.
COG0539. LUCA.
GeneTreeiENSGT00390000012228.
HOGENOMiHOG000088607.
HOVERGENiHBG108419.
InParanoidiQ14690.
KOiK14792.
OMAiLCHRSEM.
OrthoDBiEOG7Q2N55.
PhylomeDBiQ14690.
TreeFamiTF105697.

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

ChiTaRSiPDCD11. human.
EvolutionaryTraceiQ14690.
GenomeRNAii22984.
PROiQ14690.
SOURCEiSearch...

Gene expression databases

BgeeiQ14690.
CleanExiHS_PDCD11.
ExpressionAtlasiQ14690. baseline and differential.
GenevisibleiQ14690. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.50.140. 11 hits.
InterProiIPR003107. HAT.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
IPR003029. S1_domain.
IPR008847. Suf.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF00575. S1. 4 hits.
PF05843. Suf. 1 hit.
[Graphical view]
SMARTiSM00386. HAT. 7 hits.
SM00316. S1. 13 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
SSF50249. SSF50249. 11 hits.
PROSITEiPS50126. S1. 12 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
    DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-1216.
    Tissue: Bone marrow.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 1-1442, VARIANT PHE-1216.
    Tissue: Lymphoma and Uterus.
  5. Bienvenut W.V., Matallanas D., Kolch W.
    Submitted (JUL-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10 AND 1343-1352, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma.
  6. Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1508-1871, VARIANT ALA-1871.
    Tissue: Brain.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Identification of a novel protein from glial cells based on its ability to interact with NF-kappaB subunits."
    Sweet T., Khalili K., Sawaya B.E., Amini S.
    J. Cell. Biochem. 90:884-891(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKB1 AND RELA, SUBCELLULAR LOCATION.
  9. "Evidence for involvement of NFBP in processing of ribosomal RNA."
    Sweet T., Yen W., Khalili K., Amini S.
    J. Cell. Physiol. 214:381-388(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493 AND SER-1498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-1360 AND SER-1362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-7; SER-438 AND SER-1498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  19. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Solution structure of the S1 RNA binding domain from human hypothetical protein BAA11502."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 173-278.

Entry informationi

Entry nameiRRP5_HUMAN
AccessioniPrimary (citable) accession number: Q14690
Secondary accession number(s): Q2TA92
, Q5W093, Q6P2J3, Q86VQ8, Q9H4P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: July 6, 2016
This is version 154 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.