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Protein

RNA polymerase II-associated protein 3

Gene

RPAP3

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

Functioni

Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II-associated protein 3
Gene namesi
Name:RPAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26151. RPAP3.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401982.

Polymorphism and mutation databases

BioMutaiRPAP3.
DMDMi158564023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 665664RNA polymerase II-associated protein 3PRO_0000302794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei116 – 1161Phosphoserine2 Publications
Modified residuei119 – 1191Phosphoserine3 Publications
Modified residuei121 – 1211Phosphoserine2 Publications
Modified residuei481 – 4811Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H6T3.
PaxDbiQ9H6T3.
PRIDEiQ9H6T3.

PTM databases

PhosphoSiteiQ9H6T3.

Miscellaneous databases

PMAP-CutDBQ9H6T3.

Expressioni

Gene expression databases

BgeeiQ9H6T3.
CleanExiHS_RPAP3.
GenevisibleiQ9H6T3. HS.

Organism-specific databases

HPAiHPA038311.
HPA038312.

Interactioni

Subunit structurei

Tightly associated with the RNA polymerase II complex (PubMed:17643375). Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3 (PubMed:20864032). Interacts with PIH1D1 (PubMed:21078300).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AA1P079003EBI-356928,EBI-296047
PFDN2Q9UHV92EBI-356928,EBI-359873
URI1O947632EBI-356928,EBI-357067
UXTQ9UBK92EBI-356928,EBI-357355
WDR92Q96MX65EBI-356928,EBI-2434101

Protein-protein interaction databases

BioGridi122783. 60 interactions.
DIPiDIP-47508N.
IntActiQ9H6T3. 34 interactions.
MINTiMINT-1140426.
STRINGi9606.ENSP00000005386.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi130 – 14516Combined sources
Helixi149 – 16214Combined sources
Helixi168 – 17912Combined sources
Helixi183 – 19614Combined sources
Helixi201 – 21313Combined sources
Helixi217 – 23014Combined sources
Helixi235 – 24915Combined sources
Helixi268 – 27710Combined sources
Helixi278 – 2803Combined sources
Helixi281 – 29414Combined sources
Helixi298 – 31013Combined sources
Helixi317 – 32812Combined sources
Helixi333 – 34513Combined sources
Helixi350 – 36314Combined sources
Helixi366 – 37914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CGVX-ray2.54A/B/C/D120-255[»]
4CGWX-ray3.00A/B265-381[»]
ProteinModelPortaliQ9H6T3.
SMRiQ9H6T3. Positions 89-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4134TPR 1Add
BLAST
Repeati133 – 16634TPR 2Add
BLAST
Repeati168 – 20033TPR 3Add
BLAST
Repeati201 – 23434TPR 4Add
BLAST
Repeati282 – 31534TPR 5Add
BLAST
Repeati317 – 34933TPR 6Add
BLAST
Repeati350 – 38334TPR 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 708Poly-Lys

Sequence similaritiesi

Belongs to the RPAP3 family.Curated
Contains 7 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00790000122996.
HOGENOMiHOG000154181.
HOVERGENiHBG059892.
InParanoidiQ9H6T3.
OMAiLQDFMRD.
OrthoDBiEOG7KSX8F.
PhylomeDBiQ9H6T3.
TreeFamiTF106243.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR025986. RPAP3-like_C.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13877. RPAP3_C. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H6T3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTSANKAIEL QLQVKQNAEE LQDFMRDLEN WEKDIKQKDM ELRRQNGVPE
60 70 80 90 100
ENLPPIRNGN FRKKKKGKAK ESSKKTREEN TKNRIKSYDY EAWAKLDVDR
110 120 130 140 150
ILDELDKDDS THESLSQESE SEEDGIHVDS QKALVLKEKG NKYFKQGKYD
160 170 180 190 200
EAIDCYTKGM DADPYNPVLP TNRASAYFRL KKFAVAESDC NLAVALNRSY
210 220 230 240 250
TKAYSRRGAA RFALQKLEEA KKDYERVLEL EPNNFEATNE LRKISQALAS
260 270 280 290 300
KENSYPKEAD IVIKSTEGER KQIEAQQNKQ QAISEKDRGN GFFKEGKYER
310 320 330 340 350
AIECYTRGIA ADGANALLPA NRAMAYLKIQ KYEEAEKDCT QAILLDGSYS
360 370 380 390 400
KAFARRGTAR TFLGKLNEAK QDFETVLLLE PGNKQAVTEL SKIKKELIEK
410 420 430 440 450
GHWDDVFLDS TQRQNVVKPI DNPPHPGSTK PLKKVIIEET GNLIQTIDVP
460 470 480 490 500
DSTTAAAPEN NPINLANVIA ATGTTSKKNS SQDDLFPTSD TPRAKVLKIE
510 520 530 540 550
EVSDTSSLQP QASLKQDVCQ SYSEKMPIEI EQKPAQFATT VLPPIPANSF
560 570 580 590 600
QLESDFRQLK SSPDMLYQYL KQIEPSLYPK LFQKNLDPDV FNQIVKILHD
610 620 630 640 650
FYIEKEKPLL IFEILQRLSE LKRFDMAVMF MSETEKKIAR ALFNHIDKSG
660
LKDSSVEELK KRYGG
Length:665
Mass (Da):75,719
Last modified:September 11, 2007 - v2
Checksum:i70D5A965E4F1EE35
GO
Isoform 2 (identifier: Q9H6T3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-429: Missing.

Note: No experimental confirmation available.
Show »
Length:631
Mass (Da):71,866
Checksum:iB175E5AE9E55FC08
GO
Isoform 3 (identifier: Q9H6T3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.

Note: No experimental confirmation available.
Show »
Length:506
Mass (Da):57,108
Checksum:i5E45C03E06E599EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti484 – 4841D → V in BAB15170 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti564 – 5641D → Y.
Corresponds to variant rs11168196 [ dbSNP | Ensembl ].
VAR_057354

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159Missing in isoform 3. 1 PublicationVSP_044882Add
BLAST
Alternative sequencei396 – 42934Missing in isoform 2. 1 PublicationVSP_027957Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025561 mRNA. Translation: BAB15170.1.
AK299465 mRNA. Translation: BAG61431.1.
AC004241 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57938.1.
BC056415 mRNA. Translation: AAH56415.1.
CCDSiCCDS53782.1. [Q9H6T3-3]
CCDS53783.1. [Q9H6T3-2]
CCDS8753.1. [Q9H6T3-1]
RefSeqiNP_001139547.1. NM_001146075.1. [Q9H6T3-2]
NP_001139548.1. NM_001146076.1. [Q9H6T3-3]
NP_078880.2. NM_024604.2. [Q9H6T3-1]
UniGeneiHs.437855.

Genome annotation databases

EnsembliENST00000005386; ENSP00000005386; ENSG00000005175. [Q9H6T3-1]
ENST00000380650; ENSP00000370024; ENSG00000005175. [Q9H6T3-2]
ENST00000432584; ENSP00000401823; ENSG00000005175. [Q9H6T3-3]
GeneIDi79657.
KEGGihsa:79657.
UCSCiuc001rpr.3. human. [Q9H6T3-1]
uc001rps.3. human. [Q9H6T3-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025561 mRNA. Translation: BAB15170.1.
AK299465 mRNA. Translation: BAG61431.1.
AC004241 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57938.1.
BC056415 mRNA. Translation: AAH56415.1.
CCDSiCCDS53782.1. [Q9H6T3-3]
CCDS53783.1. [Q9H6T3-2]
CCDS8753.1. [Q9H6T3-1]
RefSeqiNP_001139547.1. NM_001146075.1. [Q9H6T3-2]
NP_001139548.1. NM_001146076.1. [Q9H6T3-3]
NP_078880.2. NM_024604.2. [Q9H6T3-1]
UniGeneiHs.437855.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CGVX-ray2.54A/B/C/D120-255[»]
4CGWX-ray3.00A/B265-381[»]
ProteinModelPortaliQ9H6T3.
SMRiQ9H6T3. Positions 89-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122783. 60 interactions.
DIPiDIP-47508N.
IntActiQ9H6T3. 34 interactions.
MINTiMINT-1140426.
STRINGi9606.ENSP00000005386.

PTM databases

PhosphoSiteiQ9H6T3.

Polymorphism and mutation databases

BioMutaiRPAP3.
DMDMi158564023.

Proteomic databases

MaxQBiQ9H6T3.
PaxDbiQ9H6T3.
PRIDEiQ9H6T3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000005386; ENSP00000005386; ENSG00000005175. [Q9H6T3-1]
ENST00000380650; ENSP00000370024; ENSG00000005175. [Q9H6T3-2]
ENST00000432584; ENSP00000401823; ENSG00000005175. [Q9H6T3-3]
GeneIDi79657.
KEGGihsa:79657.
UCSCiuc001rpr.3. human. [Q9H6T3-1]
uc001rps.3. human. [Q9H6T3-2]

Organism-specific databases

CTDi79657.
GeneCardsiGC12M048057.
H-InvDBHIX0010575.
HGNCiHGNC:26151. RPAP3.
HPAiHPA038311.
HPA038312.
MIMi611477. gene.
neXtProtiNX_Q9H6T3.
PharmGKBiPA162401982.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00790000122996.
HOGENOMiHOG000154181.
HOVERGENiHBG059892.
InParanoidiQ9H6T3.
OMAiLQDFMRD.
OrthoDBiEOG7KSX8F.
PhylomeDBiQ9H6T3.
TreeFamiTF106243.

Miscellaneous databases

ChiTaRSiRPAP3. human.
GenomeRNAii79657.
NextBioi68830.
PMAP-CutDBQ9H6T3.
PROiQ9H6T3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6T3.
CleanExiHS_RPAP3.
GenevisibleiQ9H6T3. HS.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR025986. RPAP3-like_C.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13877. RPAP3_C. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 3).
    Tissue: Tongue.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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] (ISOFORM 2).
    Tissue: Blood.
  5. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
    Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
    Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-116; SER-119; SER-121 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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.
  8. "PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced apoptosis."
    Inoue M., Saeki M., Egusa H., Niwa H., Kamisaki Y.
    Biochem. Biophys. Res. Commun. 403:340-344(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIH1D1.
  9. "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stability."
    Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S., Skehel J.M., de Lange T., Boulton S.J.
    Mol. Cell 39:839-850(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE R2TP COMPLEX.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-116; SER-119 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRPAP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H6T3
Secondary accession number(s): B4DRW9, Q6PHR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: June 24, 2015
This is version 107 of the entry and version 2 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 12
    Human chromosome 12: 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

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.