Reviewed,
UniProtKB/Swiss-Prot P55196 (AFAD_HUMAN)
Last modified
November 25, 2008.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Afadin Alternative name(s): Protein AF-6 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1816 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. |
| Subunit structure | Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1 and RIT2 By similarity. Interacts with NRXN1 and BCR. |
| Subcellular location | Cell junction › adherens junction. Note= Not found at cell-matrix AJs. |
| Domain | The PDZ/DHR domain interacts with the C-terminus of nectin and the Pro-rich N-terminus domain interacts with F-actin. |
| Involvement in disease | A chromosomal aberration involving MLLT4 is associated with acute leukemias. Translocation t(6;11)(q27;q23) with MLL/HRX. The result is a rogue activator protein. |
| Sequence similarities | Contains 1 dilute domain. Contains 1 FHA domain. Contains 1 PDZ (DHR) domain. Contains 2 Ras-associating domains. |
| Sequence caution | The sequence CAB82312.1 differs from that shown. Reason: Frameshift at positions 1492, 1495 and 1684. |
Ontologies
Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Cell junction |
| Coding sequence diversity | Alternative splicing Chromosomal rearrangement |
| Disease | Proto-oncogene |
| Domain | Coiled coil Repeat |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | cell adhesion Traceable author statement. Source: ProtInc cell-cell signaling Ref.1Traceable author statement. Source: ProtInc signal transduction Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | cell-cell junction Traceable author statement. Source: ProtInc |
| Molecular function | protein C-terminus binding Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 2 (identifier: P55196-1) Also known as: l-afadin; 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. | ||||||
| Isoform 1 (identifier: P55196-2) Also known as: s-afadin; The sequence of this isoform differs from the canonical sequence as follows: 1031-1031: D → DV 1588-1611: LQDEERRRQQQLEEMRKREAEDRA → VKGGVLWLCPSVVPILASACFPWG 1612-1816: Missing. | ||||||
| Isoform 3 (identifier: P55196-3) The sequence of this isoform differs from the canonical sequence as follows: 1666-1743: LCRPPLPRDY...SSTRKSHGDL → PNSYPGSTGA...TELENELNTK 1744-1816: Missing. | ||||||
| Isoform 4 (identifier: P55196-4) The sequence of this isoform differs from the canonical sequence as follows: 137-137: P → PK 391-391: P → PGRRNHFAYYNYHTYE 1031-1031: D → DV 1730-1816: QDKYSSTRKS...KRVTNQLSLS → PNSYPGSTGA...TELENELNTK | ||||||
| Isoform 5 (identifier: P55196-5) The sequence of this isoform differs from the canonical sequence as follows: 391-391: P → PGRRNHFAYYNYHTYE 1031-1031: D → DV 1587-1587: R → RTAMPAISVLDL 1730-1816: QDKYSSTRKS...KRVTNQLSLS → PNSYPGSTGA...TELENELNTK |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1816 | 1816 | Afadin | PRO_0000215918 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Domain | 39 – 133 | 95 | Ras-associating 1 | ||||||||||||||||||||||
| Domain | 245 – 347 | 103 | Ras-associating 2 | ||||||||||||||||||||||
| Domain | 425 – 491 | 67 | FHA | ||||||||||||||||||||||
| Domain | 652 – 892 | 241 | Dilute | ||||||||||||||||||||||
| Domain | 991 – 1076 | 86 | PDZ | ||||||||||||||||||||||
| Coiled coil | 145 – 184 | 40 | Potential | ||||||||||||||||||||||
| Coiled coil | 1391 – 1431 | 41 | Potential | ||||||||||||||||||||||
| Coiled coil | 1506 – 1650 | 145 | Potential | ||||||||||||||||||||||
| Compositional bias | 162 – 174 | 13 | Glu/Lys-rich | ||||||||||||||||||||||
| Compositional bias | 1329 – 1375 | 47 | Pro-rich | ||||||||||||||||||||||
| Compositional bias | 1561 – 1571 | 11 | Asp/Glu-rich (acidic) | ||||||||||||||||||||||
| Compositional bias | 1661 – 1691 | 31 | Pro-rich | ||||||||||||||||||||||
Sites | |||||||||||||||||||||||||
| Site | 26 | 1 | Breakpoint for translocation to form MLL-MLLT4 | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Modified residue | 94 | 1 | Phosphotyrosine | ||||||||||||||||||||||
| Modified residue | 215 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 541 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1090 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1155 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1156 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1165 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1184 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1213 | 1 | Phosphotyrosine By similarity | ||||||||||||||||||||||
| Modified residue | 1215 | 1 | Phosphothreonine | ||||||||||||||||||||||
| Modified residue | 1258 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1313 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||
| Modified residue | 1317 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||
| Modified residue | 1679 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1681 | 1 | Phosphoserine | ||||||||||||||||||||||
| Modified residue | 1704 | 1 | Phosphoserine | ||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||
| Alternative sequence | 137 | 1 | P → PK in isoform 4. | VSP_019254 | |||||||||||||||||||||
| Alternative sequence | 391 | 1 | P → PGRRNHFAYYNYHTYE in isoform 4 and isoform 5. | VSP_019255 | |||||||||||||||||||||
| Alternative sequence | 1031 | 1 | D → DV in isoform 1, isoform 4 and isoform 5. | VSP_019256 | |||||||||||||||||||||
| Alternative sequence | 1587 | 1 | R → RTAMPAISVLDL in isoform 5. | VSP_019257 | |||||||||||||||||||||
| Alternative sequence | 1588 – 1611 | 24 | LQDEE…AEDRA → VKGGVLWLCPSVVPILASAC FPWG in isoform 1. | VSP_000217 | |||||||||||||||||||||
| Alternative sequence | 1612 – 1816 | 205 | Missing in isoform 1. | VSP_000218 | |||||||||||||||||||||
| Alternative sequence | 1666 – 1743 | 78 | LCRPP…SHGDL → PNSYPGSTGAAVGAHDACRD AKEKRSKSQDADSPGSSGAP ENLTFKERQRLFSQGQDVSN KVKASRKLTELENELNTK in isoform 3. | VSP_000219 | |||||||||||||||||||||
| Alternative sequence | 1730 – 1816 | 87 | QDKYS…QLSLS → PNSYPGSTGAAVGAHDACRD AKEKRSKSQDADSPGSSGAP ENLTFKERQRLFSQGQDVSN KVKASRKLTELENELNTK in isoform 4 and isoform 5. | VSP_019258 | |||||||||||||||||||||
| Alternative sequence | 1744 – 1816 | 73 | Missing in isoform 3. | VSP_000220 | |||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||
| Sequence conflict | 373 | 1 | G → V in AAC50059. Ref.1 | ||||||||||||||||||||||
| Sequence conflict | 1408 | 1 | R → P in AAC50059. Ref.1 | ||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Beta strand | 990 – 997 | 8 | |||||||||||||||||||||||
| Beta strand | 999 – 1001 | 3 | |||||||||||||||||||||||
| Beta strand | 1004 – 1009 | 6 | |||||||||||||||||||||||
| Beta strand | 1018 – 1024 | 7 | |||||||||||||||||||||||
| Helix | 1029 – 1032 | 4 | |||||||||||||||||||||||
| Beta strand | 1037 – 1044 | 8 | |||||||||||||||||||||||
| Helix | 1054 – 1062 | 9 | |||||||||||||||||||||||
| Beta strand | 1066 – 1074 | 9 | |||||||||||||||||||||||
Sequences
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Clusters with