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Protein

RNA polymerase II-associated protein 1

Gene

RPAP1

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. Required for interaction of the RNA polymerase II complex with acetylated histone H3.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II-associated protein 1
Gene namesi
Name:RPAP1
Synonyms:KIAA1403
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:24567. RPAP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134914340.

Polymorphism and mutation databases

BioMutaiRPAP1.
DMDMi296452978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13931393RNA polymerase II-associated protein 1PRO_0000284841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei321 – 3211PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BWH6.
MaxQBiQ9BWH6.
PaxDbiQ9BWH6.
PRIDEiQ9BWH6.

PTM databases

iPTMnetiQ9BWH6.
PhosphoSiteiQ9BWH6.

Expressioni

Gene expression databases

BgeeiQ9BWH6.
CleanExiHS_RPAP1.
ExpressionAtlasiQ9BWH6. baseline and differential.
GenevisibleiQ9BWH6. HS.

Organism-specific databases

HPAiHPA041739.

Interactioni

Subunit structurei

Part of an RNA polymerase II complex that contains POLR2A, POLR2B, POLR2C, POLR2D, POLR2E, POLR2F, POLR2G, POLR2H, POLR2I, POLR2J, POLR2K, POLR2L, RPAP1, FCP1 plus the general transcription factors TFIIB and TFIIF.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POLR2LP628753EBI-1048085,EBI-359527
POT1Q9NUX52EBI-1048085,EBI-752420

Protein-protein interaction databases

BioGridi117487. 49 interactions.
IntActiQ9BWH6. 5 interactions.
MINTiMINT-3062678.
STRINGi9606.ENSP00000306123.

Structurei

3D structure databases

ProteinModelPortaliQ9BWH6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi827 – 1286460Leu-richAdd
BLAST

Sequence similaritiesi

Belongs to the RPAP1 family.Curated

Phylogenomic databases

eggNOGiKOG1894. Eukaryota.
ENOG410XNVT. LUCA.
GeneTreeiENSGT00390000007594.
HOGENOMiHOG000154180.
HOVERGENiHBG057248.
InParanoidiQ9BWH6.
OMAiQWVLVLE.
PhylomeDBiQ9BWH6.
TreeFamiTF324391.

Family and domain databases

InterProiIPR013929. RNA_pol_II_AP1_C.
IPR013930. RNA_pol_II_AP1_N.
[Graphical view]
PfamiPF08620. RPAP1_C. 1 hit.
PF08621. RPAP1_N. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9BWH6-1) [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
MLSRPKPGES EVDLLHFQSQ FLAAGAAPAV QLVKKGNRGG GDANSDRPPL
60 70 80 90 100
QDHRDVVMLD NLPDLPPALV PSPPKRARPS PGHCLPEDED PEERLRRHDQ
110 120 130 140 150
HITAVLTKII ERDTSSVAVN LPVPSGVAFP AVFLRSRDTQ GKSATSGKRS
160 170 180 190 200
IFAQEIAARR IAEAKGPSVG EVVPNVGPPE GAVTCETPTP RNQGCQLPGS
210 220 230 240 250
SHSFQGPNLV TGKGLRDQEA EQEAQTIHEE NIARLQAMAP EEILQEQQRL
260 270 280 290 300
LAQLDPSLVA FLRSHSHTQE QTGETASEEQ RPGGPSANVT KEEPLMSAFA
310 320 330 340 350
SEPRKRDKLE PEAPALALPV TPQKEWLHMD TVELEKLHWT QDLPPVRRQQ
360 370 380 390 400
TQERMQARFS LQGELLAPDV DLPTHLGLHH HGEEAERAGY SLQELFHLTR
410 420 430 440 450
SQVSQQRALA LHVLAQVISR AQAGEFGDRL AGSVLSLLLD AGFLFLLRFS
460 470 480 490 500
LDDRVDGVIA TAIRALRALL VAPGDEELLD STFSWYHGAL TFPLMPSQED
510 520 530 540 550
KEDEDEDEEC PAGKAKRKSP EEESRPPPDL ARHDVIKGLL ATSLLPRLRY
560 570 580 590 600
VLEVTYPGPA VVLDILAVLI RLARHSLESA TRVLECPRLI ETIVREFLPT
610 620 630 640 650
SWSPVGAGPT PSLYKVPCAT AMKLLRVLAS AGRNIAARLL SSFDLRSRLC
660 670 680 690 700
RIIAEAPQEL ALPPEEAEML STEALRLWAV AASYGQGGYL YRELYPVLMR
710 720 730 740 750
ALQVVPRELS THPPQPLSMQ RIASLLTLLT QLTLAAGSTP AETISDSAEA
760 770 780 790 800
SLSATPSLVT WTQVSGLQPL VEPCLRQTLK LLSRPEMWRA VGPVPVACLL
810 820 830 840 850
FLGAYYQAWS QQPSSCPEDW LQDMQRLSEE LLLPLLSQPT LGSLWDSLRH
860 870 880 890 900
CSLLCNPLSC VPALEAPPSL VSLGCSGGCP RLSLAGSASP FPFLTALLSL
910 920 930 940 950
LNTLAQIHKG LCGQLAAILA APGLQNYFLQ CVAPGAAPHL TPFSAWALRH
960 970 980 990 1000
EYHLQYLALA LAQKAAALQP LPATHAALYH GMALALLSRL LPGSEYLTHE
1010 1020 1030 1040 1050
LLLSCVFRLE FLPERTSGGP EAADFSDQLS LGSSRVPRCG QGTLLAQACQ
1060 1070 1080 1090 1100
DLPSIRNCYL THCSPARASL LASQALHRGE LQRVPTLLLP MPTEPLLPTD
1110 1120 1130 1140 1150
WPFLPLIRLY HRASDTPSGL SPTDTMGTAM RVLQWVLVLE SWRPQALWAV
1160 1170 1180 1190 1200
PPAARLARLM CVFLVDSELF RESPVQHLVA ALLAQLCQPQ VLPNLNLDCR
1210 1220 1230 1240 1250
LPGLTSFPDL YANFLDHFEA VSFGDHLFGA LVLLPLQRRF SVTLRLALFG
1260 1270 1280 1290 1300
EHVGALRALS LPLTQLPVSL ECYTVPPEDN LALLQLYFRT LVTGALRPRW
1310 1320 1330 1340 1350
CPVLYAVAVA HVNSFIFSQD PQSSDEVKAA RRSMLQKTWL LADEGLRQHL
1360 1370 1380 1390
LHYKLPNSTL PEGFELYSQL PPLRQHYLQR LTSTVLQNGV SET
Length:1,393
Mass (Da):152,755
Last modified:May 18, 2010 - v3
Checksum:i0DB7C1B49590172F
GO
Isoform 2 (identifier: Q9BWH6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1306: LPVSLECYTV...RPRWCPVLYA → VLSQPSRTCK...RGLRESMKRA
     1307-1393: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:1,315
Mass (Da):143,582
Checksum:i3D9EC009EA2CE308
GO
Isoform 3 (identifier: Q9BWH6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-621: Missing.

Show »
Length:772
Mass (Da):84,735
Checksum:i74075BBA34A7FBAA
GO

Sequence cautioni

The sequence BAA92641.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti760 – 7601T → A in BAB14247 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651K → M.
Corresponds to variant rs2297382 [ dbSNP | Ensembl ].
VAR_057738
Natural varianti429 – 4291R → Q.
Corresponds to variant rs2289741 [ dbSNP | Ensembl ].
VAR_057739
Natural varianti506 – 5061E → K.2 Publications
Corresponds to variant rs1200345 [ dbSNP | Ensembl ].
VAR_060348
Natural varianti525 – 5251R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036469
Natural varianti582 – 5821R → G.
Corresponds to variant rs11630901 [ dbSNP | Ensembl ].
VAR_057740
Natural varianti825 – 8251Q → E.4 Publications
Corresponds to variant rs8027526 [ dbSNP | Ensembl ].
VAR_060349
Natural varianti1108 – 11081R → G.
Corresponds to variant rs7170898 [ dbSNP | Ensembl ].
VAR_060350

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 621621Missing in isoform 3. 1 PublicationVSP_024679Add
BLAST
Alternative sequencei1266 – 130641LPVSL…PVLYA → VLSQPSRTCKGTLHWASGAV LSLEELWKTSASSSYLLGAL RGLRESMKRA in isoform 2. 1 PublicationVSP_024680Add
BLAST
Alternative sequencei1307 – 139387Missing in isoform 2. 1 PublicationVSP_024681Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037824 mRNA. Translation: BAA92641.1. Different initiation.
AK022794 mRNA. Translation: BAB14247.1.
AC016134 Genomic DNA. No translation available.
BC000246 mRNA. Translation: AAH00246.2.
AL117479 mRNA. Translation: CAB55952.1.
AL157487 mRNA. Translation: CAB75675.2.
CCDSiCCDS10079.1. [Q9BWH6-1]
PIRiT17262.
T46928.
RefSeqiNP_056355.2. NM_015540.3. [Q9BWH6-1]
XP_005254354.1. XM_005254297.1. [Q9BWH6-1]
UniGeneiHs.371045.

Genome annotation databases

EnsembliENST00000304330; ENSP00000306123; ENSG00000103932. [Q9BWH6-1]
ENST00000562303; ENSP00000455363; ENSG00000103932. [Q9BWH6-2]
GeneIDi26015.
KEGGihsa:26015.
UCSCiuc001zod.5. human. [Q9BWH6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037824 mRNA. Translation: BAA92641.1. Different initiation.
AK022794 mRNA. Translation: BAB14247.1.
AC016134 Genomic DNA. No translation available.
BC000246 mRNA. Translation: AAH00246.2.
AL117479 mRNA. Translation: CAB55952.1.
AL157487 mRNA. Translation: CAB75675.2.
CCDSiCCDS10079.1. [Q9BWH6-1]
PIRiT17262.
T46928.
RefSeqiNP_056355.2. NM_015540.3. [Q9BWH6-1]
XP_005254354.1. XM_005254297.1. [Q9BWH6-1]
UniGeneiHs.371045.

3D structure databases

ProteinModelPortaliQ9BWH6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117487. 49 interactions.
IntActiQ9BWH6. 5 interactions.
MINTiMINT-3062678.
STRINGi9606.ENSP00000306123.

PTM databases

iPTMnetiQ9BWH6.
PhosphoSiteiQ9BWH6.

Polymorphism and mutation databases

BioMutaiRPAP1.
DMDMi296452978.

Proteomic databases

EPDiQ9BWH6.
MaxQBiQ9BWH6.
PaxDbiQ9BWH6.
PRIDEiQ9BWH6.

Protocols and materials databases

DNASUi26015.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304330; ENSP00000306123; ENSG00000103932. [Q9BWH6-1]
ENST00000562303; ENSP00000455363; ENSG00000103932. [Q9BWH6-2]
GeneIDi26015.
KEGGihsa:26015.
UCSCiuc001zod.5. human. [Q9BWH6-1]

Organism-specific databases

CTDi26015.
GeneCardsiRPAP1.
H-InvDBHIX0012155.
HGNCiHGNC:24567. RPAP1.
HPAiHPA041739.
MIMi611475. gene.
neXtProtiNX_Q9BWH6.
PharmGKBiPA134914340.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1894. Eukaryota.
ENOG410XNVT. LUCA.
GeneTreeiENSGT00390000007594.
HOGENOMiHOG000154180.
HOVERGENiHBG057248.
InParanoidiQ9BWH6.
OMAiQWVLVLE.
PhylomeDBiQ9BWH6.
TreeFamiTF324391.

Miscellaneous databases

ChiTaRSiRPAP1. human.
GenomeRNAii26015.
NextBioi47776.
PROiQ9BWH6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWH6.
CleanExiHS_RPAP1.
ExpressionAtlasiQ9BWH6. baseline and differential.
GenevisibleiQ9BWH6. HS.

Family and domain databases

InterProiIPR013929. RNA_pol_II_AP1_C.
IPR013930. RNA_pol_II_AP1_N.
[Graphical view]
PfamiPF08620. RPAP1_C. 1 hit.
PF08621. RPAP1_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS LYS-506 AND GLU-825.
    Tissue: Brain.
  2. "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.
  3. "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] (ISOFORM 3), VARIANT GLU-825.
    Tissue: Teratocarcinoma.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    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 1), VARIANTS LYS-506 AND GLU-825.
    Tissue: Eye.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 761-1393, VARIANT GLU-825.
    Tissue: Mammary cancer and Testis.
  7. "RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits."
    Jeronimo C., Langelier M.-F., Zeghouf M., Cojocaru M., Bergeron D., Baali D., Forget D., Mnaimneh S., Davierwala A.P., Pootoolal J., Chandy M., Canadien V., Beattie B.K., Richards D.P., Workman J.L., Hughes T.R., Greenblatt J., Coulombe B.
    Mol. Cell. Biol. 24:7043-7058(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
  8. "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.
  9. "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-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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 THR-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-525.

Entry informationi

Entry nameiRPAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9BWH6
Secondary accession number(s): Q9H9I2
, Q9NSQ5, Q9P2E4, Q9UFS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 109 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. 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.