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Protein

E3 SUMO-protein ligase ZNF451

Gene

Znf451

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins. Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation. Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11'. Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9'. Plays a role in regulating the transcription of AR targets (By similarity).By similarity1 Publication

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 19527C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri212 – 23423C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri253 – 27725C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri315 – 33824C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri362 – 38524C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri494 – 51724C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri527 – 55024C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62926C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65724C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri665 – 68824C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri751 – 77424C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri787 – 81024C2H2-type 12PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase ZNF4511 Publication
Alternative name(s):
Zinc finger protein 451 (EC:6.3.2.-1 Publication)
Gene namesi
Name:Znf451
Synonyms:Zfp451
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2137896. Zfp451.

Subcellular locationi

  • Nucleus By similarity
  • NucleusPML body By similarity
  • Nucleusnucleoplasm By similarity

  • Note: Colocalizes with UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules; this probably requires sumoylation. Desumoylation leads to diffuse nucleoplasmic location.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10561056E3 SUMO-protein ligase ZNF451PRO_0000047599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki75 – 75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki106 – 106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki139 – 139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki153 – 153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Cross-linki288 – 288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki420 – 420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei429 – 4291PhosphoserineBy similarity
Cross-linki431 – 431Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki704 – 704Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki704 – 704Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki815 – 815Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki843 – 843Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki849 – 849Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki989 – 989Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Sumoylated. Predominantly sumoylated on the N-terminal region that is important for interaction with SUMO1 and SUMO2. Sumoylation is important for localization in nuclear granules; desumoylation leads to diffuse nucleoplasmic location. Autosumoylated (in vitro). Sumoylation enhances E3 SUMO-protein ligase activity.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8C0P7.
MaxQBiQ8C0P7.
PaxDbiQ8C0P7.
PRIDEiQ8C0P7.

PTM databases

iPTMnetiQ8C0P7.
PhosphoSiteiQ8C0P7.

Expressioni

Gene expression databases

BgeeiQ8C0P7.
CleanExiMM_ZFP451.
ExpressionAtlasiQ8C0P7. baseline and differential.
GenevisibleiQ8C0P7. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts (via N-terminal region) with SUMO1. Interacts (via N-terminal region) with SUMO2. Interacts simultaneously with two SUMO2 chains. Identified in a complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Interacts (via C-terminus) with ubiquitin. Interacts (via N-terminal zinc-finger domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the SMAD4 complex.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019861.

Structurei

3D structure databases

ProteinModelPortaliQ8C0P7.
SMRiQ8C0P7. Positions 158-200, 212-237, 310-337, 491-557, 622-696, 741-781.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 344344Important for interaction with SUMO1 and SUMO2By similarityAdd
BLAST
Regioni1 – 246246Sufficient for E3 SUMO-protein ligase activityBy similarityAdd
BLAST
Regioni30 – 378Interaction with SUMO2 1By similarity
Regioni42 – 509Interaction with SUMO2 2By similarity
Regioni168 – 521354Important for interaction with SMAD4By similarityAdd
BLAST
Regioni1045 – 105612Important for ubiquitin bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 414PLRPCurated

Domaini

Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UBC9 active site, while the second region interacts with another SUMO2 that is non-covalently associated with the same UBE2I/UBC9 chain.By similarity

Sequence similaritiesi

Contains 12 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 19527C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri212 – 23423C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri253 – 27725C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri315 – 33824C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri362 – 38524C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri494 – 51724C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri527 – 55024C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri604 – 62926C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri634 – 65724C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri665 – 68824C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri751 – 77424C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri787 – 81024C2H2-type 12PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00390000011354.
HOGENOMiHOG000155796.
HOVERGENiHBG057364.
InParanoidiQ8C0P7.
OMAiESVLLYC.
PhylomeDBiQ8C0P7.
TreeFamiTF331947.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 12 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C0P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDPGPEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS
60 70 80 90 100
SDDEEPSTSH SDENFKCKDY IDHQKDKVAL TLARLARHVE VEKQQKEEKN
110 120 130 140 150
RAFREKIDFQ HAHGLQELEF IQGHSETEAA RQCVDQWLKM PGLRTNAANS
160 170 180 190 200
GTKRSFQRGG RMWRSEKPIL CPIMHCNKEF DNGHLLLGHL KRFDHSPCDP
210 220 230 240 250
TITLHGPLAN SFACAVCYEH FVTQQQYKDH LLSRTAAADG HSNSLLPQII
260 270 280 290 300
QCYACPQCFL LFSTKDECLK HMSTKNHFHQ SFKLSDNKGT ARPISFPSFA
310 320 330 340 350
KKRLVSLCKD VPFQVKCVAC HQTLRSHMEL TAHFRVRCQN AGPVAIAEKS
360 370 380 390 400
ITQVAKEFIV RGYCSDCNQV FMDVASTQSH KNSGHKITLA NSVEESVLLY
410 420 430 440 450
CHISEGSRPP CDLHLFSQPK ISSLKRILSV KESSAEDCIV PTKKVNLGVE
460 470 480 490 500
SLGGATRVQR QSPAVTAWFC ECRRQFPSEE AVEKHVFSAN TMCYKCVVCG
510 520 530 540 550
KVCEDSGVMR LHMSRFHGGA HLNNFLFWCR TCKKELVKKD AIMAHITEFH
560 570 580 590 600
SGHRYFYEMD EVEEEEEEAM PSSSVESHLN TDKPPSPIAV VDHCPANSPP
610 620 630 640 650
RGRWQCRICE DMFESQECVK QHCMSLTSHR FHRYSCAHCR KTFHKVETLY
660 670 680 690 700
RHCQDEHDSE IMMKYFCGLC DLIFNKEEEF LSHYKEHHSI DYVFVSEKTK
710 720 730 740 750
TSIKTEGDFK IVETSSLLSC GCHESYMCKI NRKEDYDRCL PVLLEKGRLW
760 770 780 790 800
FRCSSCSATA QNVTDINTHV CQVHRKEKSE EEQQYVIKCG ICTKAFQNTE
810 820 830 840 850
SAQQHFHRKH AALQKPTATP GGANRSSTCQ LAASASHAEK NLKQPSSQKH
860 870 880 890 900
SDVEKGAEHD VRCQNIEEEV ELPDVDYLRT MTHIVFVDFD NWSNFFGHLP
910 920 930 940 950
GHLNQGTFIW GFQGGNTNWK PPLSCKVYNY LSRIGCFFLH PRCSKRKDAA
960 970 980 990 1000
DFAICMHAGR LDEQLPKQIP FTILSGDQGF LELENQFKKT QRPAHILNPH
1010 1020 1030 1040 1050
HLEGDMMCAL LNSISDTTKE CDSDDSSGMK GSPAEELRAT EDVELEEAIR

RSLEEM
Length:1,056
Mass (Da):120,070
Last modified:March 1, 2003 - v1
Checksum:i7D8FBC0B50ECA622
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030088 mRNA. Translation: BAC26778.1.
CCDSiCCDS14865.1.
RefSeqiNP_001277628.1. NM_001290699.1.
NP_598578.1. NM_133817.3.
UniGeneiMm.289103.
Mm.440137.

Genome annotation databases

EnsembliENSMUST00000019861; ENSMUSP00000019861; ENSMUSG00000042197.
GeneIDi98403.
KEGGimmu:98403.
UCSCiuc007anz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030088 mRNA. Translation: BAC26778.1.
CCDSiCCDS14865.1.
RefSeqiNP_001277628.1. NM_001290699.1.
NP_598578.1. NM_133817.3.
UniGeneiMm.289103.
Mm.440137.

3D structure databases

ProteinModelPortaliQ8C0P7.
SMRiQ8C0P7. Positions 158-200, 212-237, 310-337, 491-557, 622-696, 741-781.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019861.

PTM databases

iPTMnetiQ8C0P7.
PhosphoSiteiQ8C0P7.

Proteomic databases

EPDiQ8C0P7.
MaxQBiQ8C0P7.
PaxDbiQ8C0P7.
PRIDEiQ8C0P7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019861; ENSMUSP00000019861; ENSMUSG00000042197.
GeneIDi98403.
KEGGimmu:98403.
UCSCiuc007anz.2. mouse.

Organism-specific databases

CTDi98403.
MGIiMGI:2137896. Zfp451.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00390000011354.
HOGENOMiHOG000155796.
HOVERGENiHBG057364.
InParanoidiQ8C0P7.
OMAiESVLLYC.
PhylomeDBiQ8C0P7.
TreeFamiTF331947.

Enzyme and pathway databases

UniPathwayiUPA00886.

Miscellaneous databases

PROiQ8C0P7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0P7.
CleanExiMM_ZFP451.
ExpressionAtlasiQ8C0P7. baseline and differential.
GenevisibleiQ8C0P7. MM.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 12 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiZN451_MOUSE
AccessioniPrimary (citable) accession number: Q8C0P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.