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Protein

pre-mRNA 3' end processing protein WDR33

Gene

WDR33

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

Functioni

Essential for both cleavage and polyadenylation of pre-mRNA 3' ends.1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA cleavage Source: GO_Central
  • mRNA polyadenylation Source: GO_Central
  • postreplication repair Source: UniProtKB
  • spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

SignaLinkiQ9C0J8.

Names & Taxonomyi

Protein namesi
Recommended name:
pre-mRNA 3' end processing protein WDR33
Alternative name(s):
WD repeat-containing protein 33
WD repeat-containing protein WDC146
Gene namesi
Name:WDR33
Synonyms:WDC146
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:25651. WDR33.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943440.

Polymorphism and mutation databases

BioMutaiWDR33.
DMDMi209572695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 13361335pre-mRNA 3' end processing protein WDR33PRO_0000051382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei7 – 71Phosphoserine3 Publications
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei1210 – 12101Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9C0J8.
PaxDbiQ9C0J8.
PRIDEiQ9C0J8.

PTM databases

PhosphoSiteiQ9C0J8.

Expressioni

Tissue specificityi

Most highly expressed in testis.1 Publication

Gene expression databases

BgeeiQ9C0J8.
CleanExiHS_WDR33.
ExpressionAtlasiQ9C0J8. baseline and differential.
GenevisibleiQ9C0J8. HS.

Organism-specific databases

HPAiHPA026897.
HPA046527.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) module of the pre-mRNA 3'-end processing complex. Interacts with CPSF3/CPSF73.1 Publication

Protein-protein interaction databases

BioGridi120620. 47 interactions.
IntActiQ9C0J8. 20 interactions.
MINTiMINT-1371235.
STRINGi9606.ENSP00000325377.

Structurei

3D structure databases

ProteinModelPortaliQ9C0J8.
SMRiQ9C0J8. Positions 122-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati117 – 15640WD 1Add
BLAST
Repeati159 – 19840WD 2Add
BLAST
Repeati200 – 23940WD 3Add
BLAST
Repeati242 – 28342WD 4Add
BLAST
Repeati286 – 32540WD 5Add
BLAST
Repeati329 – 36941WD 6Add
BLAST
Repeati373 – 41240WD 7Add
BLAST
Domaini618 – 770153Collagen-likeAdd
BLAST

Sequence similaritiesi

Contains 1 collagen-like domain.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00730000111130.
HOGENOMiHOG000126810.
HOVERGENiHBG062379.
KOiK15542.
OMAiTVMEVKL.
OrthoDBiEOG7QG43G.
PhylomeDBiQ9C0J8.
TreeFamiTF317659.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR008160. Collagen.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF00400. WD40. 6 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_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: Q9C0J8-1) [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
MATEIGSPPR FFHMPRFQHQ APRQLFYKRP DFAQQQAMQQ LTFDGKRMRK
60 70 80 90 100
AVNRKTIDYN PSVIKYLENR IWQRDQRDMR AIQPDAGYYN DLVPPIGMLN
110 120 130 140 150
NPMNAVTTKF VRTSTNKVKC PVFVVRWTPE GRRLVTGASS GEFTLWNGLT
160 170 180 190 200
FNFETILQAH DSPVRAMTWS HNDMWMLTAD HGGYVKYWQS NMNNVKMFQA
210 220 230 240 250
HKEAIREASF SPTDNKFATC SDDGTVRIWD FLRCHEERIL RGHGADVKCV
260 270 280 290 300
DWHPTKGLVV SGSKDSQQPI KFWDPKTGQS LATLHAHKNT VMEVKLNLNG
310 320 330 340 350
NWLLTASRDH LCKLFDIRNL KEELQVFRGH KKEATAVAWH PVHEGLFASG
360 370 380 390 400
GSDGSLLFWH VGVEKEVGGM EMAHEGMIWS LAWHPLGHIL CSGSNDHTSK
410 420 430 440 450
FWTRNRPGDK MRDRYNLNLL PGMSEDGVEY DDLEPNSLAV IPGMGIPEQL
460 470 480 490 500
KLAMEQEQMG KDESNEIEMT IPGLDWGMEE VMQKDQKKVP QKKVPYAKPI
510 520 530 540 550
PAQFQQAWMQ NKVPIPAPNE VLNDRKEDIK LEEKKKTQAE IEQEMATLQY
560 570 580 590 600
TNPQLLEQLK IERLAQKQVE QIQPPPSSGT PLLGPQPFPG QGPMSQIPQG
610 620 630 640 650
FQQPHPSQQM PMNMAQMGPP GPQGQFRPPG PQGQMGPQGP PLHQGGGGPQ
660 670 680 690 700
GFMGPQGPQG PPQGLPRPQD MHGPQGMQRH PGPHGPLGPQ GPPGPQGSSG
710 720 730 740 750
PQGHMGPQGP PGPQGHIGPQ GPPGPQGHLG PQGPPGTQGM QGPPGPRGMQ
760 770 780 790 800
GPPHPHGIQG GPGSQGIQGP VSQGPLMGLN PRGMQGPPGP RENQGPAPQG
810 820 830 840 850
MIMGHPPQEM RGPHPPGGLL GHGPQEMRGP QEIRGMQGPP PQGSMLGPPQ
860 870 880 890 900
ELRGPPGSQS QQGPPQGSLG PPPQGGMQGP PGPQGQQNPA RGPHPSQGPI
910 920 930 940 950
PFQQQKTPLL GDGPRAPFNQ EGQSTGPPPL IPGLGQQGAQ GRIPPLNPGQ
960 970 980 990 1000
GPGPNKGDSR GPPNHHMGPM SERRHEQSGG PEHGPERGPF RGGQDCRGPP
1010 1020 1030 1040 1050
DRRGPHPDFP DDFSRPDDFH PDKRFGHRLR EFEGRGGPLP QEEKWRRGGP
1060 1070 1080 1090 1100
GPPFPPDHRE FSEGDGRGAA RGPPGAWEGR RPGDERFPRD PEDPRFRGRR
1110 1120 1130 1140 1150
EESFRRGAPP RHEGRAPPRG RDGFPGPEDF GPEENFDASE EAARGRDLRG
1160 1170 1180 1190 1200
RGRGTPRGGR KGLLPTPDEF PRFEGGRKPD SWDGNREPGP GHEHFRDTPR
1210 1220 1230 1240 1250
PDHPPHDGHS PASRERSSSL QGMDMASLPP RKRPWHDGPG TSEHREMEAP
1260 1270 1280 1290 1300
GGPSEDRGGK GRGGPGPAQR VPKSGRSSSL DGEHHDGYHR DEPFGGPPGS
1310 1320 1330
GTPSRGGRSG SNWGRGSNMN SGPPRRGASR GGGRGR
Length:1,336
Mass (Da):145,891
Last modified:October 14, 2008 - v2
Checksum:iDE45F510F93BB783
GO
Isoform 2 (identifier: Q9C0J8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-326: SFSPTDNKFA...IRNLKEELQV → RFIHNIPFSV...YFIPNKEFSL
     327-1336: Missing.

Show »
Length:326
Mass (Da):38,294
Checksum:i1F1F704B877F7904
GO
Isoform 3 (identifier: Q9C0J8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     242-257: GHGADVKCVDWHPTKG → DTCFHHCRCYFLSVKR
     258-326: Missing.
     327-1336: Missing.

Note: No experimental confirmation available.
Show »
Length:257
Mass (Da):30,288
Checksum:i2235A458B412633E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131T → A in BAD97039 (Ref. 3) Curated
Sequence conflicti715 – 7151G → S in BAB32435 (PubMed:11162572).Curated
Isoform 2 (identifier: Q9C0J8-2)
Sequence conflicti274 – 2741R → Q in BAD97039 (Ref. 3) Curated
Sequence conflicti306 – 3061F → S in AAH05401 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331A → S.
Corresponds to variant rs11557686 [ dbSNP | Ensembl ].
VAR_046717
Natural varianti711 – 7111P → R.
Corresponds to variant rs12615078 [ dbSNP | Ensembl ].
VAR_053427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 326118SFSPT…EELQV → RFIHNIPFSVVPIVMVKLFS KCILGAEMHGLCQFLGNFLH PINTIFFFVFTHSPFCWHLS EVVLSRYQPLQYVRDVLSAA FCTGFLFSFMINNVYTLFLF IIYCVRQEYFIPNKEFSL in isoform 2. 3 PublicationsVSP_041333Add
BLAST
Alternative sequencei242 – 25716GHGAD…HPTKG → DTCFHHCRCYFLSVKR in isoform 3. 1 PublicationVSP_042684Add
BLAST
Alternative sequencei258 – 32669Missing in isoform 3. 1 PublicationVSP_042685Add
BLAST
Alternative sequencei327 – 13361010Missing in isoform 2 and isoform 3. 3 PublicationsVSP_041334Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044749 mRNA. Translation: BAB32435.1.
AK002156 mRNA. Translation: BAA92113.1.
AK223319 mRNA. Translation: BAD97039.1.
AC006011 Genomic DNA. Translation: AAX82033.1.
CH471103 Genomic DNA. Translation: EAW95342.1.
CH471103 Genomic DNA. Translation: EAW95343.1.
BC005401 mRNA. Translation: AAH05401.1. Different termination.
BC013990 mRNA. Translation: AAH13990.1.
BC068484 mRNA. Translation: AAH68484.1.
AL834365 mRNA. Translation: CAH10688.1.
CCDSiCCDS2150.1. [Q9C0J8-1]
CCDS42746.1. [Q9C0J8-3]
CCDS46407.1. [Q9C0J8-2]
RefSeqiNP_001006623.1. NM_001006622.2. [Q9C0J8-2]
NP_001006624.1. NM_001006623.2. [Q9C0J8-3]
NP_060853.3. NM_018383.4. [Q9C0J8-1]
UniGeneiHs.554831.

Genome annotation databases

EnsembliENST00000322313; ENSP00000325377; ENSG00000136709. [Q9C0J8-1]
ENST00000393006; ENSP00000376730; ENSG00000136709. [Q9C0J8-3]
ENST00000409658; ENSP00000387186; ENSG00000136709. [Q9C0J8-2]
GeneIDi55339.
KEGGihsa:55339.
UCSCiuc002tpg.2. human. [Q9C0J8-1]
uc002tph.2. human. [Q9C0J8-3]
uc002tpi.2. human. [Q9C0J8-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044749 mRNA. Translation: BAB32435.1.
AK002156 mRNA. Translation: BAA92113.1.
AK223319 mRNA. Translation: BAD97039.1.
AC006011 Genomic DNA. Translation: AAX82033.1.
CH471103 Genomic DNA. Translation: EAW95342.1.
CH471103 Genomic DNA. Translation: EAW95343.1.
BC005401 mRNA. Translation: AAH05401.1. Different termination.
BC013990 mRNA. Translation: AAH13990.1.
BC068484 mRNA. Translation: AAH68484.1.
AL834365 mRNA. Translation: CAH10688.1.
CCDSiCCDS2150.1. [Q9C0J8-1]
CCDS42746.1. [Q9C0J8-3]
CCDS46407.1. [Q9C0J8-2]
RefSeqiNP_001006623.1. NM_001006622.2. [Q9C0J8-2]
NP_001006624.1. NM_001006623.2. [Q9C0J8-3]
NP_060853.3. NM_018383.4. [Q9C0J8-1]
UniGeneiHs.554831.

3D structure databases

ProteinModelPortaliQ9C0J8.
SMRiQ9C0J8. Positions 122-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120620. 47 interactions.
IntActiQ9C0J8. 20 interactions.
MINTiMINT-1371235.
STRINGi9606.ENSP00000325377.

PTM databases

PhosphoSiteiQ9C0J8.

Polymorphism and mutation databases

BioMutaiWDR33.
DMDMi209572695.

Proteomic databases

MaxQBiQ9C0J8.
PaxDbiQ9C0J8.
PRIDEiQ9C0J8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322313; ENSP00000325377; ENSG00000136709. [Q9C0J8-1]
ENST00000393006; ENSP00000376730; ENSG00000136709. [Q9C0J8-3]
ENST00000409658; ENSP00000387186; ENSG00000136709. [Q9C0J8-2]
GeneIDi55339.
KEGGihsa:55339.
UCSCiuc002tpg.2. human. [Q9C0J8-1]
uc002tph.2. human. [Q9C0J8-3]
uc002tpi.2. human. [Q9C0J8-2]

Organism-specific databases

CTDi55339.
GeneCardsiGC02M128458.
HGNCiHGNC:25651. WDR33.
HPAiHPA026897.
HPA046527.
neXtProtiNX_Q9C0J8.
PharmGKBiPA134943440.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00730000111130.
HOGENOMiHOG000126810.
HOVERGENiHBG062379.
KOiK15542.
OMAiTVMEVKL.
OrthoDBiEOG7QG43G.
PhylomeDBiQ9C0J8.
TreeFamiTF317659.

Enzyme and pathway databases

SignaLinkiQ9C0J8.

Miscellaneous databases

ChiTaRSiWDR33. human.
GeneWikiiWDR33.
GenomeRNAii55339.
NextBioi59651.
PROiQ9C0J8.

Gene expression databases

BgeeiQ9C0J8.
CleanExiHS_WDR33.
ExpressionAtlasiQ9C0J8. baseline and differential.
GenevisibleiQ9C0J8. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR008160. Collagen.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF00400. WD40. 6 hits.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel WD40 repeat protein, WDC146, highly expressed during spermatogenesis in a stage-specific manner."
    Ito S., Sakai A., Nomura T., Miki Y., Ouchida M., Sasaki J., Shimizu K.
    Biochem. Biophys. Res. Commun. 280:656-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 2).
    Tissue: Placenta.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Small intestine.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2 AND 3).
    Tissue: Brain, Pancreas and Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1336 (ISOFORM 1).
    Tissue: Melanoma.
  8. "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-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Molecular architecture of the human pre-mRNA 3' processing complex."
    Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J., Yates J.R. III, Frank J., Manley J.L.
    Mol. Cell 33:365-376(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 3' PRE-MRNA END PROCESSING COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH CPSF3.
  11. "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.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiWDR33_HUMAN
AccessioniPrimary (citable) accession number: Q9C0J8
Secondary accession number(s): Q05DP8
, Q53FG9, Q587J1, Q69YF7, Q6NUQ0, Q9NUL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 14, 2008
Last modified: June 24, 2015
This is version 126 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. 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.