Q9BXL6 · CAR14_HUMAN
- ProteinCaspase recruitment domain-containing protein 14
- GeneCARD14
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1004 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis
Isoform 3
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 | aggresome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | CARD domain binding | |
Biological Process | activation of NF-kappaB-inducing kinase activity | |
Biological Process | apoptotic process | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | positive regulation of NF-kappaB transcription factor activity | |
Biological Process | positive regulation of protein phosphorylation | |
Biological Process | tumor necrosis factor-mediated signaling pathway |
Keywords
- Biological process
Enzyme and pathway databases
Induces the nucleation of a endosomal- and microtubule-localized signalosome that transmits pro-inflammatory signaling postively regulated by LUBAC and TRAF6. Independently of NF-kappaB, induces hyperproliferative phenotype and PI3K/Akt - mTOR signalling in the skin. Interacts with TRAF2, TRAF6, HOIP/RNF31, HOIL-1, SHARPIN, A20, ABIN1, cIAP1, cIAP2, DIABLO, AP2M1, AP2B1, AP2A1, AP2S1, EpsinR and Clathrin.
Names & Taxonomy
Protein names
- Recommended nameCaspase recruitment domain-containing protein 14
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXL6
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Psoriasis 2 (PSORS2)
- Note
- DescriptionA common, chronic inflammatory disease of the skin with multifactorial etiology. It is characterized by red, scaly plaques usually found on the scalp, elbows and knees. These lesions are caused by abnormal keratinocyte proliferation and infiltration of inflammatory cells into the dermis and epidermis.
- See alsoMIM:602723
Natural variants in PSORS2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078583 | 69 | R>W | in PSORS2; reduces NF-kappa-B activation; dbSNP:rs375624435 | |
VAR_068224 | 117 | G>S | in PSORS2 and PRP; may result in altered splicing of exon 3; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity; dbSNP:rs281875215 | |
VAR_068225 | 138 | E>A | in PSORS2; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity; dbSNP:rs281875214 | |
VAR_068226 | 142 | E>G | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs281875213 | |
VAR_068227 | 142 | E>K | in PSORS2; increases NF-kappaB transcription factor activity; enhances MALT1 protease activity; dbSNP:rs281875212 | |
VAR_068228 | 150 | L>R | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs146214639 | |
VAR_078586 | 151 | R>Q | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs200731780 | |
VAR_078587 | 151 | R>W | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs777305616 | |
VAR_078588 | 197 | E>K | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs200790561 | |
VAR_078589 | 209 | L>P | in PSORS2; uncertain significance; no effect on NF-kappaB transcription factor activity | |
VAR_078590 | 216 | A>T | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs574982768 | |
VAR_078595 | 420 | T>A | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs762364495 | |
VAR_078596 | 602 | S>L | in PSORS2; uncertain significance; does not change NF-kappaB transcription factor activity; dbSNP:rs201285077 | |
VAR_078597 | 639 | A>G | in PSORS2; uncertain significance; does not change NF-kappaB transcription factor activity |
Pityriasis rubra pilaris (PRP)
- Note
- DescriptionA rare, papulosquamous skin disease characterized by the appearance of keratotic follicular papules, well-demarcated salmon-colored erythematous plaques covered with fine powdery scales interspersed with distinct islands of uninvolved skin, and palmoplantar keratoderma. Most cases are sporadic. The rare familial cases show autosomal dominant inheritance with incomplete penetrance and variable expression. Familial PRP usually presents at birth or appears during the first years of life and runs a chronic course. It is characterized by prominent follicular hyperkeratosis, diffuse palmoplantar keratoderma, and erythema.
- See alsoMIM:173200
Natural variants in PRP
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_068224 | 117 | G>S | in PSORS2 and PRP; may result in altered splicing of exon 3; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity; dbSNP:rs281875215 | |
VAR_078584 | 127 | C>S | in PRP | |
VAR_078585 | 136 | Q>L | in PRP | |
VAR_068819 | 138 | missing | in PRP | |
VAR_068820 | 156 | L>P | in PRP; dbSNP:rs387907240 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_068222 | 38 | in dbSNP:rs281875217 | |||
Sequence: R → C | ||||||
Natural variant | VAR_068223 | 62 | in dbSNP:rs115582620 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_078583 | 69 | in PSORS2; reduces NF-kappa-B activation; dbSNP:rs375624435 | |||
Sequence: R → W | ||||||
Natural variant | VAR_068224 | 117 | in PSORS2 and PRP; may result in altered splicing of exon 3; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity; dbSNP:rs281875215 | |||
Sequence: G → S | ||||||
Natural variant | VAR_078584 | 127 | in PRP | |||
Sequence: C → S | ||||||
Natural variant | VAR_078585 | 136 | in PRP | |||
Sequence: Q → L | ||||||
Natural variant | VAR_068225 | 138 | in PSORS2; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity; dbSNP:rs281875214 | |||
Sequence: E → A | ||||||
Natural variant | VAR_068819 | 138 | in PRP | |||
Sequence: Missing | ||||||
Natural variant | VAR_068226 | 142 | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs281875213 | |||
Sequence: E → G | ||||||
Natural variant | VAR_068227 | 142 | in PSORS2; increases NF-kappaB transcription factor activity; enhances MALT1 protease activity; dbSNP:rs281875212 | |||
Sequence: E → K | ||||||
Natural variant | VAR_068228 | 150 | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs146214639 | |||
Sequence: L → R | ||||||
Natural variant | VAR_078586 | 151 | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs200731780 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_078587 | 151 | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs777305616 | |||
Sequence: R → W | ||||||
Natural variant | VAR_068820 | 156 | in PRP; dbSNP:rs387907240 | |||
Sequence: L → P | ||||||
Natural variant | VAR_068229 | 171 | probable risk factor for PSORS2; does not change MALT1 protease activity; dbSNP:rs281875216 | |||
Sequence: H → N | ||||||
Natural variant | VAR_068230 | 176 | in dbSNP:rs144475004 | |||
Sequence: D → H | ||||||
Natural variant | VAR_068231 | 179 | in dbSNP:rs199517469 | |||
Sequence: R → H | ||||||
Natural variant | VAR_068232 | 191 | in dbSNP:rs281875218 | |||
Sequence: V → L | ||||||
Natural variant | VAR_078588 | 197 | in PSORS2; increases NF-kappaB transcription factor activity; dbSNP:rs200790561 | |||
Sequence: E → K | ||||||
Natural variant | VAR_068233 | 200 | in dbSNP:rs114688446 | |||
Sequence: S → N | ||||||
Natural variant | VAR_078589 | 209 | in PSORS2; uncertain significance; no effect on NF-kappaB transcription factor activity | |||
Sequence: L → P | ||||||
Natural variant | VAR_078590 | 216 | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs574982768 | |||
Sequence: A → T | ||||||
Natural variant | VAR_078591 | 218 | decreases NF-kappaB transcription factor activity; dbSNP:rs747854314 | |||
Sequence: R → C | ||||||
Natural variant | VAR_068234 | 285 | risk factor for PSORS2; dbSNP:rs281875219 | |||
Sequence: D → G | ||||||
Natural variant | VAR_078592 | 338 | does not change NF-kappaB transcription factor activity; dbSNP:rs200132496 | |||
Sequence: M → V | ||||||
Natural variant | VAR_078593 | 350 | in dbSNP:rs1412261979 | |||
Sequence: L → P | ||||||
Natural variant | VAR_078594 | 357 | ||||
Sequence: L → P | ||||||
Natural variant | VAR_078595 | 420 | in PSORS2; uncertain significance; decreases NF-kappaB transcription factor activity; dbSNP:rs762364495 | |||
Sequence: T → A | ||||||
Natural variant | VAR_024401 | 547 | in dbSNP:rs2066964 | |||
Sequence: R → S | ||||||
Natural variant | VAR_048608 | 585 | in dbSNP:rs34367357 | |||
Sequence: V → I | ||||||
Natural variant | VAR_068235 | 593 | in dbSNP:rs281875220 | |||
Sequence: I → N | ||||||
Natural variant | VAR_078596 | 602 | in PSORS2; uncertain significance; does not change NF-kappaB transcription factor activity; dbSNP:rs201285077 | |||
Sequence: S → L | ||||||
Natural variant | VAR_078597 | 639 | in PSORS2; uncertain significance; does not change NF-kappaB transcription factor activity | |||
Sequence: A → G | ||||||
Natural variant | VAR_068236 | 682 | in dbSNP:rs117918077 | |||
Sequence: R → W | ||||||
Natural variant | VAR_068237 | 714 | in dbSNP:rs151150961 | |||
Sequence: G → S | ||||||
Natural variant | VAR_059196 | 820 | in dbSNP:rs11652075 | |||
Sequence: R → W | ||||||
Natural variant | VAR_022043 | 883 | in dbSNP:rs2289541 | |||
Sequence: R → H | ||||||
Natural variant | VAR_061080 | 962 | in dbSNP:rs34850974 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_068238 | 973 | in dbSNP:rs144285237 | |||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,447 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000144088 | 1-1004 | UniProt | Caspase recruitment domain-containing protein 14 | |||
Sequence: MGELCRRDSALTALDEETLWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDVYTLVTGLQPDVDFSNFSGLMETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTREPCPREKQRLVRMHAICPRDDSDCSLVSSTESQLLSDLSATSSRELVDSFRSSSPAPPSQQSLYKRVAEDFGEEPWSFSSCLEIPEGDPGALPGAKAGDPHLDYELLDTADLPQLESSLQPVSPGRLDVSESGVLMRRRPARRILSQVTMLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNTDGYKRLLQDLEAKVATSGDSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQGCGCWHAHRVNSYTMKDTAAHGTIPNYSRAQQQLIALIQDMTQQCTVTRKPSSGGPQKLVRIVSMDKAKASPLRLSFDRGQLDPSRMEGSSTCFWAESCLTLVPYTLVRPHRPARPRPVLLVPRAVGKILSEKLCLLQGFKKCLAEYLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKMAKKLKKGLQRLGTSEEQLLEAARQEEGDLDRAPCLYSSLAPDGWSDLDGLLSCVRQAIADEQKKVVWTEQSPR | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 470 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 474 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 544 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 787 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1002 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms a complex with MALT1 and BCL10; resulting in the formation of a CBM (CARD14-BLC10-MALT1) complex (PubMed:27071417, PubMed:27113748).
Interacts with TRAF2, TRAF3 and TRAF6 (PubMed:21302310).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BXL6-1 | BCL10 O95999 | 2 | EBI-50436205, EBI-958922 | |
BINARY | Q9BXL6-2 | BCL10 O95999 | 2 | EBI-12114736, EBI-958922 | |
BINARY | Q9BXL6-2 | PRPF31 Q8WWY3 | 4 | EBI-12114736, EBI-1567797 | |
BINARY | Q9BXL6-2 | ZNF648 Q5T619 | 3 | EBI-12114736, EBI-11985915 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-107 | CARD | ||||
Sequence: DEETLWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDVYTLVTGLQ | ||||||
Coiled coil | 128-409 | |||||
Sequence: LAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE | ||||||
Region | 409-568 | Maintains the protein in an inactive state | ||||
Sequence: EPPGVLKQEARTREPCPREKQRLVRMHAICPRDDSDCSLVSSTESQLLSDLSATSSRELVDSFRSSSPAPPSQQSLYKRVAEDFGEEPWSFSSCLEIPEGDPGALPGAKAGDPHLDYELLDTADLPQLESSLQPVSPGRLDVSESGVLMRRRPARRILSQ | ||||||
Domain | 568-658 | PDZ | ||||
Sequence: QVTMLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNT | ||||||
Domain | 807-990 | Guanylate kinase-like | ||||
Sequence: AESCLTLVPYTLVRPHRPARPRPVLLVPRAVGKILSEKLCLLQGFKKCLAEYLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKMAKKLKKGLQRLGTSEEQLLEAARQEEGDLDRAPCLYSSLAPDGWSDLDGLLSCVRQAIA |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9BXL6-1
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.
- Name1
- SynonymsCARD14fl, CARMA2fl
- Length1,004
- Mass (Da)113,270
- Last updated2010-05-18 v2
- Checksum761CBAC219956076
Q9BXL6-2
- Name2
- SynonymsShort, CARD14sh, CARMA2sh
- Differences from canonical
- 741-1004: Missing
Q9BXL6-3
- Name3
- SynonymsCardless, CARD14cardless, CARMA2cl
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494BZY0 | A0A494BZY0_HUMAN | CARD14 | 553 | ||
A0A494C1N2 | A0A494C1N2_HUMAN | CARD14 | 1013 | ||
A0A494C199 | A0A494C199_HUMAN | CARD14 | 636 | ||
A0A494C0J4 | A0A494C0J4_HUMAN | CARD14 | 854 | ||
A0A3B3ITQ9 | A0A3B3ITQ9_HUMAN | CARD14 | 84 | ||
I3L414 | I3L414_HUMAN | CARD14 | 493 | ||
I3L3F1 | I3L3F1_HUMAN | CARD14 | 475 | ||
I3L1Z7 | I3L1Z7_HUMAN | CARD14 | 70 | ||
A0A994J6G4 | A0A994J6G4_HUMAN | CARD14 | 678 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047400 | 1-237 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047401 | 619-671 | in isoform 3 | |||
Sequence: DYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNTDGYKRLLQDLEAK → SRARPLLSPGLLMGTVAAGGVTQADFTSPRRCRSTLGWASALSWADVKRSAHL | ||||||
Alternative sequence | VSP_047402 | 672-1004 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047403 | 741-1004 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF322642 EMBL· GenBank· DDBJ | AAG53403.1 EMBL· GenBank· DDBJ | mRNA | ||
AY032927 EMBL· GenBank· DDBJ | AAK54453.1 EMBL· GenBank· DDBJ | mRNA | ||
EU652409 EMBL· GenBank· DDBJ | ACF49506.1 EMBL· GenBank· DDBJ | mRNA | ||
AC087741 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC018142 EMBL· GenBank· DDBJ | AAH18142.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001326 EMBL· GenBank· DDBJ | AAH01326.1 EMBL· GenBank· DDBJ | mRNA |