P16452 · EPB42_HUMAN
- ProteinProtein 4.2
- GeneEPB42
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids691 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane.
Miscellaneous
The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2.
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 | ankyrin-1 complex | |
Cellular Component | cortical cytoskeleton | |
Cellular Component | cytoskeleton | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein-glutamine gamma-glutamyltransferase activity | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | cell morphogenesis | |
Biological Process | erythrocyte maturation | |
Biological Process | hemoglobin metabolic process | |
Biological Process | multicellular organismal-level iron ion homeostasis | |
Biological Process | regulation of cell shape | |
Biological Process | spleen development |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein 4.2
- Short namesP4.2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP16452
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: Cytoplasmic surface of erythrocyte membranes.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spherocytosis 5 (SPH5)
- Note
- DescriptionSpherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported.
- See alsoMIM:612690
Natural variants in SPH5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_007482 | 112 | A>T | in SPH5; Nippon/Fukuoka; dbSNP:rs104894487 | |
VAR_058099 | 145 | D>Y | in SPH5; Komatsu; dbSNP:rs143682977 | |
VAR_012268 | 280 | R>Q | in SPH5; Tozeur; dbSNP:rs121917734 | |
VAR_058100 | 287 | R>C | in SPH5; Shiga; dbSNP:rs515726212 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_007482 | 112 | in SPH5; Nippon/Fukuoka; dbSNP:rs104894487 | |||
Sequence: A → T | ||||||
Natural variant | VAR_058099 | 145 | in SPH5; Komatsu; dbSNP:rs143682977 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_012268 | 280 | in SPH5; Tozeur; dbSNP:rs121917734 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_058100 | 287 | in SPH5; Shiga; dbSNP:rs515726212 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 845 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000213720 | 2-691 | Protein 4.2 | |||
Sequence: GQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVALTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWDFGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVLGSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNISTKGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLKAPSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVGLQRLTVEVDCNMFQNLTNYKSVTVVAPELSA | ||||||
Modified residue | 248 | Phosphoserine; by PKA | ||||
Sequence: S |
Post-translational modification
Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the ankyrin-1 complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 (PubMed:35835865).
Interacts with SLC4A1 (via the cytoplasmic domain); this interaction is mediated by the SLC4A1 Band 3-I dimer (PubMed:35835865).
Interacts with ANK1 (via ANK 1-13 repeats) (PubMed:35835865).
Interacts with AQP1 (via the C-terminal) (PubMed:35835865).
Interacts with SLC4A1 (via the cytoplasmic domain); this interaction is mediated by the SLC4A1 Band 3-I dimer (PubMed:35835865).
Interacts with ANK1 (via ANK 1-13 repeats) (PubMed:35835865).
Interacts with AQP1 (via the C-terminal) (PubMed:35835865).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P16452 | KLK6 Q92876 | 3 | EBI-1182496, EBI-2432309 | |
BINARY | P16452 | SPINK7 P58062 | 3 | EBI-1182496, EBI-1182445 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 31-39 | Band 3 binding | ||||
Sequence: LFVRRGQPF |
Sequence similarities
Belongs to the transglutaminase superfamily. Transglutaminase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P16452-1
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.
- NameShort
- NoteMajor isoform.
- Length691
- Mass (Da)77,009
- Last updated2008-11-25 v3
- Checksum38225C311E478580
P16452-2
- NameLong
- Differences from canonical
- 3-3: Q → QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD
P16452-3
- Name3
- Differences from canonical
- 324-395: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006416 | 3 | in isoform Long | |||
Sequence: Q → QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD | ||||||
Alternative sequence | VSP_055340 | 324-395 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 350 | in Ref. 1; AAA74589/AAA52385 and 2; AAA35798 | ||||
Sequence: H → D | ||||||
Sequence conflict | 376 | in Ref. 1; AAA74589/AAA52385 and 2; AAA35798 | ||||
Sequence: L → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M60298 EMBL· GenBank· DDBJ | AAA74589.1 EMBL· GenBank· DDBJ | mRNA | ||
L06519 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06447 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06448 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06449 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06450 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06511 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06512 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06513 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06515 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06516 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06517 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L06518 EMBL· GenBank· DDBJ | AAA52385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29399 EMBL· GenBank· DDBJ | AAA35798.1 EMBL· GenBank· DDBJ | mRNA | ||
M30647 EMBL· GenBank· DDBJ | AAA36401.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
M30646 EMBL· GenBank· DDBJ | AAA36402.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AC068724 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471125 EMBL· GenBank· DDBJ | EAW92591.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC096093 EMBL· GenBank· DDBJ | AAH96093.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096094 EMBL· GenBank· DDBJ | AAH96094.1 EMBL· GenBank· DDBJ | mRNA | ||
BC099627 EMBL· GenBank· DDBJ | AAH99627.1 EMBL· GenBank· DDBJ | mRNA |