A0A669KAV7 · A0A669KAV7_HUMAN
- ProteinWIZ zinc finger
- GeneWIZ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1889 (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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 accessionA0A669KAV7
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 1,906 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) | 929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1073 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1087 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1088 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1094 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1103 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1111 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1117 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1130 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1139 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1359 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1360 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1372 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1391 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1456 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1552 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1573 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1575 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1590 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1718 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1755 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1867 | 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 | 975-997 | C2H2-type | ||||
Sequence: TTCEVCGACFETRKGLSSHARSH | ||||||
Region | 1077-1142 | Disordered | ||||
Sequence: FSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTLDS | ||||||
Compositional bias | 1106-1124 | Polar residues | ||||
Sequence: NPEDKSPQLSLSPRPASPK | ||||||
Domain | 1148-1170 | C2H2-type | ||||
Sequence: LDCQLCGAWFETRKGLSSHARAH | ||||||
Region | 1206-1233 | Disordered | ||||
Sequence: RGALAHPGRPPPTSAALSLLPPPPPAKK | ||||||
Compositional bias | 1219-1233 | Pro residues | ||||
Sequence: SAALSLLPPPPPAKK | ||||||
Domain | 1281-1308 | C2H2-type | ||||
Sequence: IRCEFCGEFFENRKGLSSHARSHLRQMG | ||||||
Region | 1329-1413 | Disordered | ||||
Sequence: RTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKK | ||||||
Compositional bias | 1375-1392 | Pro residues | ||||
Sequence: AKKLPPPPGSPLGHSPTA | ||||||
Domain | 1465-1492 | C2H2-type | ||||
Sequence: IRCEFCGEFFENRKGLSSHARSHLRQMG | ||||||
Region | 1521-1569 | Disordered | ||||
Sequence: KEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVP | ||||||
Compositional bias | 1541-1555 | Pro residues | ||||
Sequence: APGPVQSPLPLSPLA | ||||||
Domain | 1635-1657 | C2H2-type | ||||
Sequence: ACCELCGLYFENRKALASHARAH | ||||||
Region | 1701-1792 | Disordered | ||||
Sequence: TKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDT | ||||||
Compositional bias | 1765-1781 | Basic and acidic residues | ||||
Sequence: HQRQNINKFERRQARPP | ||||||
Region | 1867-1889 | Disordered | ||||
Sequence: SKADPPPEESQAPQAQTAAAEAP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,889
- Mass (Da)203,534
- Last updated2020-06-17 v1
- ChecksumEE7215E0686A2DD7
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 | ||
A0A2R8YFV2 | A0A2R8YFV2_HUMAN | WIZ | 1699 | ||
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 | ||
B9EGQ5 | B9EGQ5_HUMAN | WIZ | 832 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1106-1124 | Polar residues | ||||
Sequence: NPEDKSPQLSLSPRPASPK | ||||||
Compositional bias | 1219-1233 | Pro residues | ||||
Sequence: SAALSLLPPPPPAKK | ||||||
Compositional bias | 1375-1392 | Pro residues | ||||
Sequence: AKKLPPPPGSPLGHSPTA | ||||||
Compositional bias | 1541-1555 | Pro residues | ||||
Sequence: APGPVQSPLPLSPLA | ||||||
Compositional bias | 1765-1781 | 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. |