A0A2R8YFV2 · A0A2R8YFV2_HUMAN
- ProteinWIZ zinc finger
- GeneWIZ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1699 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | midbody | |
Cellular Component | nucleoplasm |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A2R8YFV2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,809 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1030 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1031 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1037 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1044 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1046 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1054 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1058 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1060 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1065 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1073 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1201 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1203 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1357 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1385 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1677 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-77 | Disordered | ||||
Sequence: MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISDGQPHPGLS | ||||||
Domain | 315-337 | C2H2-type | ||||
Sequence: FPCIECSIYFKQKEHLLEHMSQH | ||||||
Domain | 352-379 | C2H2-type | ||||
Sequence: LACGECGWAFADPTALEQHRQLHQASRE | ||||||
Region | 424-447 | Disordered | ||||
Sequence: MREPPGQTTKEPFGGSSGAGSPSP | ||||||
Region | 594-626 | Disordered | ||||
Sequence: LGRNKSTVHPQGLGERRRPWSEEEEEEEEEEDV | ||||||
Domain | 817-839 | C2H2-type | ||||
Sequence: MRCDFCGAGFDTRAGLSSHARAH | ||||||
Region | 867-891 | Disordered | ||||
Sequence: AEQPPSPLGREPGGPPGSFLTSRRP | ||||||
Domain | 918-940 | C2H2-type | ||||
Sequence: TTCEVCGACFETRKGLSSHARSH | ||||||
Region | 1020-1086 | Disordered | ||||
Sequence: FSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPE | ||||||
Compositional bias | 1049-1067 | Polar residues | ||||
Sequence: NPEDKSPQLSLSPRPASPK | ||||||
Domain | 1091-1118 | C2H2-type | ||||
Sequence: IRCEFCGEFFENRKGLSSHARSHLRQMG | ||||||
Region | 1139-1222 | Disordered | ||||
Sequence: RTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPK | ||||||
Compositional bias | 1185-1202 | Pro residues | ||||
Sequence: AKKLPPPPGSPLGHSPTA | ||||||
Domain | 1275-1302 | C2H2-type | ||||
Sequence: IRCEFCGEFFENRKGLSSHARSHLRQMG | ||||||
Region | 1331-1379 | Disordered | ||||
Sequence: KEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVP | ||||||
Compositional bias | 1351-1365 | Pro residues | ||||
Sequence: APGPVQSPLPLSPLA | ||||||
Domain | 1445-1467 | C2H2-type | ||||
Sequence: ACCELCGLYFENRKALASHARAH | ||||||
Region | 1511-1602 | Disordered | ||||
Sequence: TKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDT | ||||||
Compositional bias | 1575-1591 | Basic and acidic residues | ||||
Sequence: HQRQNINKFERRQARPP | ||||||
Region | 1677-1699 | Disordered | ||||
Sequence: SKADPPPEESQAPQAQTAAAEAP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,699
- Mass (Da)183,745
- Last updated2018-06-20 v1
- Checksum93688CB1B8FBE529
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O95785 | WIZ_HUMAN | WIZ | 1651 | ||
M0QXA7 | M0QXA7_HUMAN | WIZ | 968 | ||
M0QXF8 | M0QXF8_HUMAN | WIZ | 133 | ||
A0A3B3IS05 | A0A3B3IS05_HUMAN | WIZ | 96 | ||
A0A669KBG4 | A0A669KBG4_HUMAN | WIZ | 933 | ||
A0A669KBH9 | A0A669KBH9_HUMAN | WIZ | 1066 | ||
A0A669KAV7 | A0A669KAV7_HUMAN | WIZ | 1889 | ||
B9EGQ5 | B9EGQ5_HUMAN | WIZ | 832 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1049-1067 | Polar residues | ||||
Sequence: NPEDKSPQLSLSPRPASPK | ||||||
Compositional bias | 1185-1202 | Pro residues | ||||
Sequence: AKKLPPPPGSPLGHSPTA | ||||||
Compositional bias | 1351-1365 | Pro residues | ||||
Sequence: APGPVQSPLPLSPLA | ||||||
Compositional bias | 1575-1591 | Basic and acidic residues | ||||
Sequence: HQRQNINKFERRQARPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006128 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC007059 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011492 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |