Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein Wiz

Gene

WIZ

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

Functioni

May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri267 – 28923C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri304 – 32623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri353 – 37523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri416 – 43924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri701 – 72323C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri769 – 79123C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri870 – 89223C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1043 – 106523C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1227 – 124923C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1397 – 141923C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1596 – 162227C2H2-type 11PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  • protein heterotrimerization Source: UniProtKB
  • protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Wiz
Alternative name(s):
Widely-interspaced zinc finger-containing protein
Zinc finger protein 803
Gene namesi
Name:WIZ
Synonyms:ZNF803
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30917. WIZ.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162409232.

Polymorphism and mutation databases

BioMutaiWIZ.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16511651Protein WizPRO_0000286054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki939 – 939Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki988 – 988Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei996 – 9961PhosphoserineCombined sources
Modified residuei998 – 9981PhosphothreonineCombined sources
Modified residuei1006 – 10061PhosphoserineCombined sources
Modified residuei1012 – 10121PhosphoserineCombined sources
Modified residuei1017 – 10171PhosphoserineCombined sources
Modified residuei1025 – 10251PhosphoserineCombined sources
Modified residuei1079 – 10791PhosphoserineCombined sources
Modified residuei1106 – 11061PhosphoserineCombined sources
Cross-linki1108 – 1108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1112 – 1112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1122 – 11221PhosphoserineCombined sources
Modified residuei1127 – 11271PhosphoserineCombined sources
Modified residuei1134 – 11341PhosphoserineCombined sources
Modified residuei1146 – 11461PhosphoserineCombined sources
Modified residuei1151 – 11511PhosphoserineCombined sources
Modified residuei1162 – 11621N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
Modified residuei1162 – 11621N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
Cross-linki1177 – 1177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1263 – 12631PhosphoserineCombined sources
Cross-linki1282 – 1282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1309 – 13091PhosphoserineCombined sources
Modified residuei1314 – 13141PhosphoserineCombined sources
Cross-linki1343 – 1343Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1356 – 1356Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1370 – 1370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1372 – 1372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1382 – 1382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1448 – 1448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1477 – 1477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1480 – 14801PhosphoserineCombined sources
Modified residuei1517 – 15171PhosphoserineCombined sources
Cross-linki1523 – 1523Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1523 – 1523Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 3 (identifier: O95785-3)
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki39 – 39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki258 – 258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 4 (identifier: O95785-4)
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki42 – 42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO95785.
MaxQBiO95785.
PeptideAtlasiO95785.
PRIDEiO95785.

PTM databases

iPTMnetiO95785.
PhosphoSiteiO95785.

Expressioni

Gene expression databases

BgeeiO95785.
CleanExiHS_WIZ.
ExpressionAtlasiO95785. baseline and differential.
GenevisibleiO95785. HS.

Organism-specific databases

HPAiHPA022923.

Interactioni

Subunit structurei

Interacts with EHMT1, EHMT2, CTBP1 and CTBP2 (By similarity). Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.By similarity1 Publication

Protein-protein interaction databases

BioGridi121845. 63 interactions.
IntActiO95785. 40 interactions.
MINTiMINT-4867330.

Structurei

3D structure databases

ProteinModelPortaliO95785.
SMRiO95785. Positions 260-331, 353-383, 406-440, 697-726, 754-791.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1030 – 10345Interaction with CTBP1 and CTBP2 1By similarity
Regioni1214 – 12185Interaction with CTBP1 and CTBP2 2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi567 – 57610Poly-Glu
Compositional biasi624 – 6296Poly-Gln
Compositional biasi753 – 7575Poly-Lys
Compositional biasi1096 – 117883Pro-richAdd
BLAST

Domaini

The C2H2-type zinc finger 11 mediates interaction with EHMT1 and EHMT2.By similarity

Sequence similaritiesi

Contains 11 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri267 – 28923C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri304 – 32623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri353 – 37523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri416 – 43924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri701 – 72323C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri769 – 79123C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri870 – 89223C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1043 – 106523C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1227 – 124923C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1397 – 141923C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1596 – 162227C2H2-type 11PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00530000063587.
HOGENOMiHOG000065754.
HOVERGENiHBG108678.
InParanoidiO95785.
OrthoDBiEOG71RXJ5.
PhylomeDBiO95785.
TreeFamiTF333705.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 11 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95785-1) [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
MEGSLAGSLA APDRPQGPER LPGPAPRENI EGGAEAAEGE GGIFRSTRYL
60 70 80 90 100
PVTKEGPRDI LDGRGGISGT PDGRGPWEHP LVQEAGEGIL SERRFEDSVI
110 120 130 140 150
VRTMKPHAEL EGSRRFLHHR GEPRLLEKHA QGRPRFDWLQ DEDEQGSPQD
160 170 180 190 200
AGLHLDLPAQ PPPLAPFRRV FVPVEDTPKT LDMAVVGGRE DLEDLEGLAQ
210 220 230 240 250
PSEWGLPTSA SEVATQTWTV NSEASVERLQ PLLPPIRTGP YLCELLEEVA
260 270 280 290 300
EGVASPDEDE DEEPAVFPCI ECSIYFKQKE HLLEHMSQHR RAPGQEPPAD
310 320 330 340 350
LAPLACGECG WAFADPTALE QHRQLHQASR EKIIEEIQKL KQVPGDEGRE
360 370 380 390 400
ARLQCPKCVF GTNSSRAYVQ HAKLHMREPP GQTTKEPFGG SSGAGSPSPE
410 420 430 440 450
ASALLYQPYG AAVGLSACVF CGFPAPSESL LREHVRLVHA HPHWEEDGEA
460 470 480 490 500
YEEDPASQPG TSQDAHACFP DTAVDYFGKA EPSLAPMWRE NPAGYDPSLA
510 520 530 540 550
FGPGCQQLSI RDFPLSKPLL HGTGQRPLGR LAFPSTLAST PYSLQLGRNK
560 570 580 590 600
STVHPQGLGE RRRPWSEEEE EEEEEEDVVL TSEMDFSPEN GVFSPLATPS
610 620 630 640 650
LIPQAALELK QAFREALQAV EATQGQQQQL RGMVPIVLVA KLGPQVMAAA
660 670 680 690 700
RVPPRLQPEE LGLAGAHPLD FLLLDAPLGG PLGLDTLLDG DPAMALKHEE
710 720 730 740 750
RKCPYCPDRF HNGIGLANHV RGHLNRVGVS YNVRHFISAE EVKAIERRFS
760 770 780 790 800
FQKKKKKVAN FDPGTFSLMR CDFCGAGFDT RAGLSSHARA HLRDFGITNW
810 820 830 840 850
ELTVSPINIL QELLATSAAE QPPSPLGREP GGPPGSFLTS RRPRLPLTVP
860 870 880 890 900
FPPTWAEDPG PAYGDAQSLT TCEVCGACFE TRKGLSSHAR SHLRQLGVAE
910 920 930 940 950
SESSGAPIDL LYELVKQKGL PDAHLGLPPG LAKKSSSLKE VVAGAPRPGL
960 970 980 990 1000
LSLAKPLDAP AVNKAIKSPP GFSAKGLGHP PSSPLLKKTP LALAGSPTPK
1010 1020 1030 1040 1050
NPEDKSPQLS LSPRPASPKA QWPQSEDEGP LNLTSGPEPA RDIRCEFCGE
1060 1070 1080 1090 1100
FFENRKGLSS HARSHLRQMG VTEWYVNGSP IDTLREILKR RTQSRPGGPP
1110 1120 1130 1140 1150
NPPGPSPKAL AKMMGGAGPG SSLEARSPSD LHISPLAKKL PPPPGSPLGH
1160 1170 1180 1190 1200
SPTASPPPTA RKMFPGLAAP SLPKKLKPEQ IRVEIKREML PGALHGELHP
1210 1220 1230 1240 1250
SEGPWGAPRE DMTPLNLSSR AEPVRDIRCE FCGEFFENRK GLSSHARSHL
1260 1270 1280 1290 1300
RQMGVTEWSV NGSPIDTLRE ILKKKSKPCL IKKEPPAGDL APALAEDGPP
1310 1320 1330 1340 1350
TVAPGPVQSP LPLSPLAGRP GKPGAGPAQV PRELSLTPIT GAKPSATGYL
1360 1370 1380 1390 1400
GSVAAKRPLQ EDRLLPAEVK AKTYIQTELP FKAKTLHEKT SHSSTEACCE
1410 1420 1430 1440 1450
LCGLYFENRK ALASHARAHL RQFGVTEWCV NGSPIETLSE WIKHRPQKVG
1460 1470 1480 1490 1500
AYRSYIQGGR PFTKKFRSAG HGRDSDKRPS LGLAPGGLAV VGRSAGGEPG
1510 1520 1530 1540 1550
PEAGRAADGG ERPLAASPPG TVKAEEHQRQ NINKFERRQA RPPDASAARG
1560 1570 1580 1590 1600
GEDTNDLQQK LEEVRQPPPR VRPVPSLVPR PPQTSLVKFV GNIYTLKCRF
1610 1620 1630 1640 1650
CEVEFQGPLS IQEEWVRHLQ RHILEMNFSK ADPPPEESQA PQAQTAAAEA

P
Length:1,651
Mass (Da):178,674
Last modified:May 1, 2007 - v2
Checksum:i9DB0485964578310
GO
Isoform 2 (identifier: O95785-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-757: Missing.
     867-1034: Missing.

Show »
Length:794
Mass (Da):85,380
Checksum:i19284DFA21E8DF0D
GO
Isoform 3 (identifier: O95785-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MEGSLAGSLA...AEGEGGIFRS → MDLGSPSLPK...GSKQELQDLK
     47-865: Missing.
     1034-1034: T → TLDSDGGREL...DVEPSPLNLS

Note: No experimental confirmation available.Combined sources
Show »
Length:965
Mass (Da):102,978
Checksum:iB41B51E8CAA3FB9F
GO
Isoform 4 (identifier: O95785-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MEGSLAGSLA...EGGIFRSTRY → MVAMDLGSPS...GSKQELQDLK
     50-865: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:835
Mass (Da):89,356
Checksum:iC686BA9551332063
GO

Sequence cautioni

The sequence BAB55234.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1373 – 13731T → A in BAD18551 (PubMed:15057824).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949MEGSL…RSTRY → MVAMDLGSPSLPKKSLPVPG ALEQVASRLSSKVAAEVPHG SKQELQDLK in isoform 4. 1 PublicationVSP_057207Add
BLAST
Alternative sequencei1 – 4646MEGSL…GIFRS → MDLGSPSLPKKSLPVPGALE QVASRLSSKVAAEVPHGSKQ ELQDLK in isoform 3. 1 PublicationVSP_054509Add
BLAST
Alternative sequencei47 – 865819Missing in isoform 3. 1 PublicationVSP_054510Add
BLAST
Alternative sequencei50 – 865816Missing in isoform 4. 1 PublicationVSP_057208Add
BLAST
Alternative sequencei69 – 757689Missing in isoform 2. 1 PublicationVSP_024951Add
BLAST
Alternative sequencei867 – 1034168Missing in isoform 2. 1 PublicationVSP_024952Add
BLAST
Alternative sequencei1034 – 10341T → TLDSDGGRELDCQLCGAWFE TRKGLSSHARAHLRHLGVSD PDAKGSPIDVLHGLIRRDGV QIRLPPRRGALAHPGRPPPT SAALSLLPPPPPAKKAKLKA AGMASPWGKQDLSAAAAAGI FWASDVEPSPLNLS in isoform 3. 1 PublicationVSP_054511

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027615 mRNA. Translation: BAB55234.1. Different initiation.
AK122890 mRNA. Translation: BAG53783.1.
AK131404 mRNA. Translation: BAD18551.1.
AC006128 Genomic DNA. Translation: AAC97985.1.
AC007059 Genomic DNA. Translation: AAD19817.1.
AC007059 Genomic DNA. Translation: AAD19818.1.
AC011492 Genomic DNA. No translation available.
BC002329 mRNA. Translation: AAH02329.2.
BC007551 mRNA. Translation: AAH07551.1.
BC062360 mRNA. Translation: AAH62360.1.
BC098445 mRNA. Translation: AAH98445.1.
BC144332 mRNA. Translation: AAI44333.1.
AL390184 mRNA. Translation: CAB99102.1.
CCDSiCCDS42516.1. [O95785-2]
PIRiT51885.
RefSeqiNP_067064.2. NM_021241.2. [O95785-2]
XP_005260069.1. XM_005260012.1. [O95785-4]
UniGeneiHs.442138.

Genome annotation databases

EnsembliENST00000263381; ENSP00000263381; ENSG00000011451. [O95785-2]
ENST00000545156; ENSP00000445824; ENSG00000011451. [O95785-3]
ENST00000599686; ENSP00000469534; ENSG00000011451. [O95785-4]
GeneIDi58525.
KEGGihsa:58525.
UCSCiuc002nba.5. human. [O95785-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027615 mRNA. Translation: BAB55234.1. Different initiation.
AK122890 mRNA. Translation: BAG53783.1.
AK131404 mRNA. Translation: BAD18551.1.
AC006128 Genomic DNA. Translation: AAC97985.1.
AC007059 Genomic DNA. Translation: AAD19817.1.
AC007059 Genomic DNA. Translation: AAD19818.1.
AC011492 Genomic DNA. No translation available.
BC002329 mRNA. Translation: AAH02329.2.
BC007551 mRNA. Translation: AAH07551.1.
BC062360 mRNA. Translation: AAH62360.1.
BC098445 mRNA. Translation: AAH98445.1.
BC144332 mRNA. Translation: AAI44333.1.
AL390184 mRNA. Translation: CAB99102.1.
CCDSiCCDS42516.1. [O95785-2]
PIRiT51885.
RefSeqiNP_067064.2. NM_021241.2. [O95785-2]
XP_005260069.1. XM_005260012.1. [O95785-4]
UniGeneiHs.442138.

3D structure databases

ProteinModelPortaliO95785.
SMRiO95785. Positions 260-331, 353-383, 406-440, 697-726, 754-791.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121845. 63 interactions.
IntActiO95785. 40 interactions.
MINTiMINT-4867330.

PTM databases

iPTMnetiO95785.
PhosphoSiteiO95785.

Polymorphism and mutation databases

BioMutaiWIZ.

Proteomic databases

EPDiO95785.
MaxQBiO95785.
PeptideAtlasiO95785.
PRIDEiO95785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263381; ENSP00000263381; ENSG00000011451. [O95785-2]
ENST00000545156; ENSP00000445824; ENSG00000011451. [O95785-3]
ENST00000599686; ENSP00000469534; ENSG00000011451. [O95785-4]
GeneIDi58525.
KEGGihsa:58525.
UCSCiuc002nba.5. human. [O95785-1]

Organism-specific databases

CTDi58525.
GeneCardsiWIZ.
HGNCiHGNC:30917. WIZ.
HPAiHPA022923.
neXtProtiNX_O95785.
PharmGKBiPA162409232.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063587.
HOGENOMiHOG000065754.
HOVERGENiHBG108678.
InParanoidiO95785.
OrthoDBiEOG71RXJ5.
PhylomeDBiO95785.
TreeFamiTF333705.

Miscellaneous databases

ChiTaRSiWIZ. human.
GenomeRNAii58525.
PROiO95785.

Gene expression databases

BgeeiO95785.
CleanExiHS_WIZ.
ExpressionAtlasiO95785. baseline and differential.
GenevisibleiO95785. HS.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 11 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[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 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1136-1651 (ISOFORM 1).
    Tissue: Brain.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1042-1651 (ISOFORM 1).
    Tissue: B-cell, Brain, Muscle and Skin.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1496-1651 (ISOFORM 1).
    Tissue: Brain.
  5. "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.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-1134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
    Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
    Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH REST; CDYL; SETB1; EHMT1 AND EHMT2.
  9. Cited for: METHYLATION AT LYS-1162, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006; SER-1012; SER-1017; SER-1127; SER-1134; SER-1146 AND SER-1151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996; SER-1006; SER-1012 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996; THR-998; SER-1006; SER-1012; SER-1017; SER-1079; SER-1134; SER-1263; SER-1309; SER-1314 AND SER-1517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-996; THR-998; SER-1006; SER-1012 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-996; THR-998; SER-1006; SER-1012; SER-1017; SER-1025; SER-1106; SER-1122; SER-1127; SER-1134; SER-1146; SER-1480 AND SER-1517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  16. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-988; LYS-1108; LYS-1112; LYS-1177; LYS-1356; LYS-1370; LYS-1372; LYS-1382 AND LYS-1523, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39 (ISOFORM 3), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-1523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-939; LYS-988; LYS-1112; LYS-1282; LYS-1343; LYS-1356; LYS-1372; LYS-1477 AND LYS-1523, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-258 (ISOFORM 3), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1282; LYS-1370; LYS-1372; LYS-1382; LYS-1448 AND LYS-1523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWIZ_HUMAN
AccessioniPrimary (citable) accession number: O95785
Secondary accession number(s): B3KVH1
, B7ZM82, M0QY21, Q4G0E0, Q6P6B0, Q6ZN24, Q7LDY6, Q7LDZ1, Q96IG5, Q96SQ6, Q9BUR8, Q9NPT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 6, 2016
This is version 121 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. 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.