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Protein

E3 SUMO-protein ligase ZNF451

Gene

ZNF451

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:26524493, PubMed:26524494). 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 (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). 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' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483).By similarity4 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.2 Publications
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)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 195C2H2-type 1PROSITE-ProRule annotationAdd BLAST27
Zinc fingeri253 – 277C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri315 – 337C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri362 – 386C2H2-type 4PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri498 – 521C2H2-type 5PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri531 – 554C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri606 – 631C2H2-type 7; atypicalPROSITE-ProRule annotationAdd BLAST26
Zinc fingeri636 – 659C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri667 – 690C2H2-type 9PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri753 – 776C2H2-type 10PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri789 – 812C2H2-type 11PROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
  • metal ion binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro
  • SUMO ligase activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00886

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase ZNF4511 Publication (EC:2.3.2.-2 Publications)
Alternative name(s):
Coactivator for steroid receptors1 Publication
E3 SUMO-protein transferase ZNF451Curated
Zinc finger protein 451
Gene namesi
Name:ZNF451
Synonyms:COASTER1 Publication, KIAA0576, KIAA1702
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000112200.16
HGNCiHGNC:21091 ZNF451
MIMi615708 gene
neXtProtiNX_Q9Y4E5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31 – 34IQFV → AQAA: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi37G → GGSGG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication1
Mutagenesisi38 – 41PLRP → ALRA: Reduces E3 SUMO-protein ligase activity by 97% (in vitro). 1 Publication4
Mutagenesisi38 – 41PLRP → GLRG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi39L → LGSGG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication1
Mutagenesisi40R → A: Reduces E3 SUMO-protein ligase activity by 96% (in vitro). 1 Publication1
Mutagenesisi46 – 49IDLV → ADAA: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi48 – 49LV → AA: Impairs interaction with SUMO1. No effect on negative regulation of SMAD4-mediated transcription activation. 2 Publications2
Mutagenesisi188G → E: Mildly reduces E3 SUMO-protein ligase activity. 1 Publication1
Mutagenesisi192R → E: Mildly reduces E3 SUMO-protein ligase activity. 1 Publication1
Mutagenesisi706K → R: No effect on negative regulation of SMAD4-mediated transcription activation. 1 Publication1

Organism-specific databases

DisGeNETi26036
OpenTargetsiENSG00000112200
PharmGKBiPA134967635

Polymorphism and mutation databases

BioMutaiZNF451
DMDMi37999825

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000475981 – 1061E3 SUMO-protein ligase ZNF451Add BLAST1061

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei155PhosphoserineCombined sources1
Modified residuei158Omega-N-methylarginineCombined sources1
Cross-linki167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei432PhosphoserineCombined sources1
Cross-linki434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki543Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki585Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki632Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki706Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki706Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki731Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki777Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki790Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki832Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki843Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki845Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki852Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki951Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki992Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki993Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 3 (identifier: Q9Y4E5-4)
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki247Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki473Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki505Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Sumoylated. Predominantly sumoylated on the N-terminal region that is important for interaction with SUMO1 and SUMO2 (PubMed:18656483, PubMed:26524493, PubMed:26524494). Sumoylation is important for localization in nuclear granules; desumoylation leads to diffuse nucleoplasmic location (PubMed:18656483). Autosumoylated (in vitro) (PubMed:26524493, PubMed:26524494). Sumoylation enhances E3 SUMO-protein ligase activity (PubMed:26524494).3 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y4E5
PaxDbiQ9Y4E5
PeptideAtlasiQ9Y4E5
PRIDEiQ9Y4E5
ProteomicsDBi86178
86179 [Q9Y4E5-2]
86180 [Q9Y4E5-4]

PTM databases

iPTMnetiQ9Y4E5
PhosphoSitePlusiQ9Y4E5

Expressioni

Gene expression databases

BgeeiENSG00000112200 Expressed in 236 organ(s), highest expression level in corpus callosum
CleanExiHS_ZNF451
ExpressionAtlasiQ9Y4E5 baseline and differential
GenevisibleiQ9Y4E5 HS

Organism-specific databases

HPAiHPA028838

Interactioni

Subunit structurei

Homooligomer. Interacts (via N-terminal region) with SUMO1 (PubMed:18656483). Interacts (via N-terminal region) with SUMO2 (PubMed:18656483, PubMed:26524494). Interacts simultaneously with two SUMO2 chains (PubMed:26524493, PubMed:26524494). 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 (PubMed:26524493, PubMed:26524494). Interacts (via C-terminus) with ubiquitin (PubMed:18656483). 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 (PubMed:24324267).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2IP632793EBI-747230,EBI-80168

Protein-protein interaction databases

BioGridi117502, 37 interactors
DIPiDIP-51264N
ELMiQ9Y4E5
IntActiQ9Y4E5, 23 interactors
MINTiQ9Y4E5
STRINGi9606.ENSP00000359740

Structurei

Secondary structure

11061
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9Y4E5
SMRiQ9Y4E5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 344Important for interaction with SUMO1 and SUMO21 PublicationAdd BLAST344
Regioni1 – 246Sufficient for E3 SUMO-protein ligase activity1 PublicationAdd BLAST246
Regioni30 – 37Interaction with SUMO2 11 Publication8
Regioni42 – 50Interaction with SUMO2 21 Publication9
Regioni168 – 525Important for interaction with SMAD41 PublicationAdd BLAST358
Regioni1050 – 1061Important for ubiquitin binding1 PublicationAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi38 – 41PLRPCurated4

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.1 Publication1 Publication

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 195C2H2-type 1PROSITE-ProRule annotationAdd BLAST27
Zinc fingeri253 – 277C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri315 – 337C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri362 – 386C2H2-type 4PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri498 – 521C2H2-type 5PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri531 – 554C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri606 – 631C2H2-type 7; atypicalPROSITE-ProRule annotationAdd BLAST26
Zinc fingeri636 – 659C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri667 – 690C2H2-type 9PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri753 – 776C2H2-type 10PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri789 – 812C2H2-type 11PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITHH Eukaryota
ENOG41116BX LUCA
GeneTreeiENSGT00390000011354
HOVERGENiHBG057364
InParanoidiQ9Y4E5
OMAiFDSQECV
OrthoDBiEOG091G017Z
PhylomeDBiQ9Y4E5
TreeFamiTF331947

Family and domain databases

InterProiView protein in InterPro
IPR013087 Znf_C2H2_type
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 12 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 9 hits
PS50157 ZINC_FINGER_C2H2_2, 5 hits

Sequences (3+)i

Sequence statusi: Complete.

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

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Y4E5-1) [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
MGDPGSEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS
60 70 80 90 100
SDDEEPSTSY TDENIKRKDH IDYQKDKVAL TLARLARHVE VEKQQKEEKN
110 120 130 140 150
RAFREKIDFQ HAHGLQELEF IRGHSDTEAA RLCVDQWLKM PGLKTGTINC
160 170 180 190 200
GTKSSFRRGG HTWVSGKPIL CPIMHCNKEF DNGHLLLGHL KRFDHSPCDP
210 220 230 240 250
TITLHGPFFS SFACVVCYKK FVTQQQYRDH LFDKEATDDG HNNNLLPQII
260 270 280 290 300
QCFACPNCFL LFSRKEECSK HMSGKNHFHQ SFKLGDNKGI AHPISFPSFA
310 320 330 340 350
KKLLISLCKD VPFQVKCVAC HKTLRSHMEL TAHFRVHCRN AGPVAVAEKS
360 370 380 390 400
ITQVAEKFIL RGYCPDCNQV FVDETSTQNH KQNSGHKVRV INSVEESVLL
410 420 430 440 450
YCHSSEGNKD PSSDLHLLLD QSKFSSLKRT MSIKESSSLE CIAIPKKKMN
460 470 480 490 500
LKDKSHEGVA CVQKEKSVVK TWFCECNQRF PSEDAVEKHV FSANTMGYKC
510 520 530 540 550
VVCGKVCDDS GVIRLHMSRI HGGAHLNNFL FWCRTCKKEL TRKDTIMAHV
560 570 580 590 600
TEFHNGHRYF YEMDEVEGET LPSSSTTLDN LTANKPSSAI TVIDHSPANS
610 620 630 640 650
SPRGKWQCRI CEDMFDSQEY VKQHCMSLAS HKFHRYSCAH CRKPFHKIET
660 670 680 690 700
LYRHCQDEHD NEIKIKYFCG LCDLIFNVEE AFLSHYEEHH SIDYVFVSEK
710 720 730 740 750
TETSIKTEDD FPVIETSNQL TCGCRESYIC KVNRKEDYSR CLQIMLDKGK
760 770 780 790 800
LWFRCSLCSA TAQNLTDMNT HIHQVHKEKS DEEEQQYVIK CGTCTKAFHD
810 820 830 840 850
PESAQQHFHR KHCFLQKPSV AHFGSEKSNL YKFTASASHT ERKLKQAINY
860 870 880 890 900
SKSLDMEKGV ENDLSYQNIE EEIVELPDLD YLRTMTHIVF VDFDNWSNFF
910 920 930 940 950
GHLPGHLNQG TFIWGFQGGN TNWKPPLNCK IYNYLNRIGC FFLHPRCSKR
960 970 980 990 1000
KDAADFAICM HAGRLDEQLP KQIPFTILSG DQGFLELENQ FKKTQRPAHI
1010 1020 1030 1040 1050
LNPHHLEGDM MCALLNSISD TTKECDSDDN MGAKNTSIGE EFISTEDVEL
1060
EEAIRRSLEE M
Length:1,061
Mass (Da):121,484
Last modified:October 24, 2003 - v2
Checksum:i8F0446B9FBFF28FA
GO
Isoform 2 (identifier: Q9Y4E5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     870-917: Missing.

Show »
Length:1,013
Mass (Da):115,776
Checksum:i47F3AEA54D754CBB
GO
Isoform 3 (identifier: Q9Y4E5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-1061: ENIKRKDHID...EAIRRSLEEM → RMPESKVPSS...DSPERHGYKN

Show »
Length:559
Mass (Da):63,021
Checksum:i4939846709AC5536
GO

Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PH99E9PH99_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
1,041Annotation score:
D6RB93D6RB93_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
72Annotation score:
D6RIA1D6RIA1_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
158Annotation score:
D6RAV4D6RAV4_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
40Annotation score:
D6RAS1D6RAS1_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
151Annotation score:
Q5VVE8Q5VVE8_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
73Annotation score:
Q5VVF0Q5VVF0_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
75Annotation score:
D6REC5D6REC5_HUMAN
E3 SUMO-protein ligase ZNF451
ZNF451
53Annotation score:

Sequence cautioni

The sequence AAH21712 differs from that shown. Intron retention.Curated
The sequence AAH42450 differs from that shown. Contaminating sequence.Curated
The sequence AAH58853 differs from that shown. Contaminating sequence.Curated
The sequence BAA25502 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB21793 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169I → T in AAL17975 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03531263 – 1061ENIKR…SLEEM → RMPESKVPSSENHRPEMCSS CNVPLPIGDSSSFSGSCSSS PERIVSQTSSVENPLENQKN DQNNSDTKISETETLKSSQN FQTLPSSPLLVPQESLASSE VKENLRIDSSSASQHGRDAI LYLQTQVAEMSRVIRDLQSR SCFRFHHSRPSENSSVPWDI STSKEENLSTVEEETDYKSP SADDKGQPSDPSQSSFTGLL KRMEQRGVIKRVTLQSEAES CEGKPDCVTSKKRLVPPLHP LLRIATTEVFKDPADCHPSS FMGHRVYPVAKDTSPFQPNP PAEGPIVEALEHSKRGNTTS PLDSTSKEMEVMGCRFYHAA SIAARAASYMAYMTQYQRKL WEDMEDLVHDPEFDRGKARC IISDGMDAGLWQLCTTRDIM DSVVRVMAMAIDYRRQAWLR LTSLTKKTQEKISHLPFDGT SLFGQDVKAVVAEDNNIKEN DYKDHKYYNQHRYFYSHDQK AHYHNRGYSKGDWYKPRNHP YRYRKKGDSPERHGYKN in isoform 3. 2 PublicationsAdd BLAST999
Alternative sequenceiVSP_008624870 – 917Missing in isoform 2. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY055204 mRNA Translation: AAL17975.1
AB011148 mRNA Translation: BAA25502.1 Different initiation.
AB051489 mRNA Translation: BAB21793.1 Different initiation.
AL136311 Genomic DNA No translation available.
AL450489 Genomic DNA No translation available.
BC021712 mRNA Translation: AAH21712.2 Sequence problems.
BC042450 mRNA Translation: AAH42450.1 Sequence problems.
BC058853 mRNA Translation: AAH58853.1 Sequence problems.
CCDSiCCDS43477.1 [Q9Y4E5-1]
CCDS4960.1 [Q9Y4E5-2]
CCDS59026.1 [Q9Y4E5-4]
PIRiT00341
RefSeqiNP_001026794.1, NM_001031623.2 [Q9Y4E5-1]
NP_056370.2, NM_015555.2 [Q9Y4E5-2]
UniGeneiHs.485628
Hs.705485

Genome annotation databases

EnsembliENST00000357489; ENSP00000350083; ENSG00000112200 [Q9Y4E5-2]
ENST00000370706; ENSP00000359740; ENSG00000112200 [Q9Y4E5-1]
ENST00000370708; ENSP00000359742; ENSG00000112200 [Q9Y4E5-4]
GeneIDi26036
KEGGihsa:26036
UCSCiuc003pdm.3 human [Q9Y4E5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY055204 mRNA Translation: AAL17975.1
AB011148 mRNA Translation: BAA25502.1 Different initiation.
AB051489 mRNA Translation: BAB21793.1 Different initiation.
AL136311 Genomic DNA No translation available.
AL450489 Genomic DNA No translation available.
BC021712 mRNA Translation: AAH21712.2 Sequence problems.
BC042450 mRNA Translation: AAH42450.1 Sequence problems.
BC058853 mRNA Translation: AAH58853.1 Sequence problems.
CCDSiCCDS43477.1 [Q9Y4E5-1]
CCDS4960.1 [Q9Y4E5-2]
CCDS59026.1 [Q9Y4E5-4]
PIRiT00341
RefSeqiNP_001026794.1, NM_001031623.2 [Q9Y4E5-1]
NP_056370.2, NM_015555.2 [Q9Y4E5-2]
UniGeneiHs.485628
Hs.705485

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5D2MX-ray2.40G2-56[»]
ProteinModelPortaliQ9Y4E5
SMRiQ9Y4E5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117502, 37 interactors
DIPiDIP-51264N
ELMiQ9Y4E5
IntActiQ9Y4E5, 23 interactors
MINTiQ9Y4E5
STRINGi9606.ENSP00000359740

PTM databases

iPTMnetiQ9Y4E5
PhosphoSitePlusiQ9Y4E5

Polymorphism and mutation databases

BioMutaiZNF451
DMDMi37999825

Proteomic databases

EPDiQ9Y4E5
PaxDbiQ9Y4E5
PeptideAtlasiQ9Y4E5
PRIDEiQ9Y4E5
ProteomicsDBi86178
86179 [Q9Y4E5-2]
86180 [Q9Y4E5-4]

Protocols and materials databases

DNASUi26036
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357489; ENSP00000350083; ENSG00000112200 [Q9Y4E5-2]
ENST00000370706; ENSP00000359740; ENSG00000112200 [Q9Y4E5-1]
ENST00000370708; ENSP00000359742; ENSG00000112200 [Q9Y4E5-4]
GeneIDi26036
KEGGihsa:26036
UCSCiuc003pdm.3 human [Q9Y4E5-1]

Organism-specific databases

CTDi26036
DisGeNETi26036
EuPathDBiHostDB:ENSG00000112200.16
GeneCardsiZNF451
HGNCiHGNC:21091 ZNF451
HPAiHPA028838
MIMi615708 gene
neXtProtiNX_Q9Y4E5
OpenTargetsiENSG00000112200
PharmGKBiPA134967635
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITHH Eukaryota
ENOG41116BX LUCA
GeneTreeiENSGT00390000011354
HOVERGENiHBG057364
InParanoidiQ9Y4E5
OMAiFDSQECV
OrthoDBiEOG091G017Z
PhylomeDBiQ9Y4E5
TreeFamiTF331947

Enzyme and pathway databases

UniPathwayi
UPA00886

Miscellaneous databases

ChiTaRSiZNF451 human
GeneWikiiZNF451
GenomeRNAii26036
PROiPR:Q9Y4E5
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112200 Expressed in 236 organ(s), highest expression level in corpus callosum
CleanExiHS_ZNF451
ExpressionAtlasiQ9Y4E5 baseline and differential
GenevisibleiQ9Y4E5 HS

Family and domain databases

InterProiView protein in InterPro
IPR013087 Znf_C2H2_type
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 12 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 9 hits
PS50157 ZINC_FINGER_C2H2_2, 5 hits
ProtoNetiSearch...

Entry informationi

Entry nameiZN451_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4E5
Secondary accession number(s): Q5VVE9
, Q5VVF1, Q86YE4, Q8N380, Q8TD15, Q9C0G1, Q9NQM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: November 7, 2018
This is version 164 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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