O15061 · SYNEM_HUMAN
- ProteinSynemin
- GeneSYNM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1565 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteromeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells.
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 | adherens junction | |
Cellular Component | costamere | |
Cellular Component | intermediate filament | |
Cellular Component | intermediate filament cytoskeleton | |
Cellular Component | neurofilament cytoskeleton | |
Cellular Component | sarcolemma | |
Molecular Function | intermediate filament binding | |
Molecular Function | structural constituent of cytoskeleton | |
Molecular Function | structural constituent of muscle | |
Molecular Function | vinculin binding | |
Biological Process | fast-twitch skeletal muscle fiber contraction | |
Biological Process | intermediate filament cytoskeleton organization |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSynemin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15061
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_012295 | 272 | in dbSNP:rs2305445 | |||
Sequence: V → A | ||||||
Natural variant | VAR_012296 | 330 | in dbSNP:rs5030691 | |||
Sequence: V → I | ||||||
Natural variant | VAR_012297 | 338 | ||||
Sequence: R → W | ||||||
Natural variant | VAR_059378 | 355 | in dbSNP:rs3743242 | |||
Sequence: R → W | ||||||
Natural variant | VAR_059379 | 462 | in dbSNP:rs3134595 | |||
Sequence: G → S | ||||||
Natural variant | VAR_012298 | 567 | in dbSNP:rs3743244 | |||
Sequence: P → L | ||||||
Natural variant | VAR_012299 | 612 | in dbSNP:rs5030692 | |||
Sequence: E → A | ||||||
Natural variant | VAR_012300 | 761 | in dbSNP:rs3743247 | |||
Sequence: P → L | ||||||
Natural variant | VAR_012301 | 946 | in dbSNP:rs5030694 | |||
Sequence: R → W | ||||||
Natural variant | VAR_012302 | 976 | in dbSNP:rs5030695 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_012303 | 1059 | in dbSNP:rs5030697 | |||
Sequence: P → L | ||||||
Natural variant | VAR_012304 | 1067 | in dbSNP:rs5030698 | |||
Sequence: R → P | ||||||
Natural variant | VAR_012305 | 1077 | in dbSNP:rs5030699 | |||
Sequence: S → L | ||||||
Natural variant | VAR_059380 | 1130 | in dbSNP:rs9920074 | |||
Sequence: G → S | ||||||
Natural variant | VAR_059381 | 1345 | in dbSNP:rs7167599 | |||
Sequence: G → A | ||||||
Natural variant | VAR_012306 | 1386 | in dbSNP:rs2292288 | |||
Sequence: E → G | ||||||
Natural variant | VAR_012307 | 1462 | in dbSNP:rs2292287 | |||
Sequence: F → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,105 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000063778 | 1-1565 | UniProt | Synemin | |||
Sequence: MLSWRLQTGPEKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSEFRNKSYHYTDSLLQRENERNLFSRQKAPLASFNHSSALYSNLSGHRGSQTGTSIGGDARRGFLGSGYSSSATTQQENSYGKAVSSQTNVRTFSPTYGLLRNTEAQVKTFPDRPKAGDTREVPVYIGEDSTIARESYRDRRDKVAAGASESTRSNERTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDAGGGTGREAEARELRFRLGTSDATGSLQGDSMTETVAENIVTSILKQFTQSPETEASADSFPDTKVTYVDRKELPGERKTKTEIVVESKLTEDVDVSDEAGLDYLLSKDIKEVGLKGKSAEQMIGDIINLGLKGREGRAKVVNVEIVEEPVSYVSGEKPEEFSVPFKVEEVEDVSPGPWGLVKEEEGYGESDVTFSVNQHRRTKQPQENTTHVEEVTEAGDSEGEQSYFVSTPDEHPGGHDRDDGSVYGQIHIEEESTIRYSWQDEIVQGTRRRTQKDGAVGEKVVKPLDVPAPSLEGDLGSTHWKEQARSGEFHAEPTVIEKEIKIPHEFHTSMKGISSKEPRQQLVEVIGQLEETLPERMREELSALTREGQGGPGSVSVDVKKVQGAGGSSVTLVAEVNVSQTVDADRLDLEELSKDEASEMEKAVESVVRESLSRQRSPAPGSPDEEGGAEAPAAGIRFRRWATRELYIPSGESEVAGGASHSSGQRTPQGPVSATVEVSSPTGFAQSQVLEDVSQAARHIKLGPSEVWRTERMSYEGPTAEVVEVSAGGDLSQAASPTGASRSVRHVTLGPGQSPLSREVIFLGPAPACPEAWGSPEPGPAESSADMDGSGRHSTFGCRQFHAEKEIIFQGPISAAGKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQMDVSNVEAIRSRTQEAGALGVSDRGSWRDADSRNDQAVGVSFKASAGEGDQAHREQGKEQAMFDKKVQLQRMVDQRSVISDEKKVALLYLDNEEEENDGHWF | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 163 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 386 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 421 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 429 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 429 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 465 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 598 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 633 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 651 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 653 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 699 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 777 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 777 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 824 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 897 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 904 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 913 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 936 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 981 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1038 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1040 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1044 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1044 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1049 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1049 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1070 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1077 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1077 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1080 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1087 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1094 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1109 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1153 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1163 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1165 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1181 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1184 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1435 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1485 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1487 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 1489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1504 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1540 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 2 is strongly detected in adult heart, fetal skeletal muscles and fetal heart. Isoform 1 is weakly detected in fetal heart and also in fetal skeletal muscle. Isoform 1 and isoform 2 are detected in adult bladder (at protein level). The mRNA is predominantly expressed in heart and muscle with some expression in brain which may be due to tissue-specific isoforms.
Developmental stage
In lens, first detected at 16 weeks when expression is weakly and uniformly distributed. Subsequently, expression becomes much stronger in the epithelium of the anterior part at 25 weeks and later. In retina, weakly expressed at 15 weeks in the nerve fiber and ganglion cell layers (NFL and GCL). From 25 weeks onwards, much stronger expression is observed in the endfeet of Mueller cells, the NFL, and GCL, and much lower expression is observed in a minor subpopulation of cells in the inner cell layer (INL). At 30 and 36 weeks, expression remains in the neural retina, and subsequently becomes stronger in the NFL, GCL, and INL and is decreased in Mueller cells. At 36 weeks, also expressed at the external border of the outer nuclear layer (ONL) (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GFAP and VIM (By similarity).
Isoform 1 interacts with TLN1 and VCL. Isoform 2 interacts with DES and DTNA. Isoform 1 and isoform 2 interact with DMD and UTRN.
Isoform 1 interacts with TLN1 and VCL. Isoform 2 interacts with DES and DTNA. Isoform 1 and isoform 2 interact with DMD and UTRN.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15061 | TTN Q8WZ42 | 3 | EBI-7843148, EBI-681210 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-10 | Head | ||||
Sequence: MLSWRLQTGP | ||||||
Region | 11-49 | Coil 1A | ||||
Sequence: EKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGR | ||||||
Region | 11-320 | Interaction with DMD and UTRN | ||||
Sequence: EKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESN | ||||||
Domain | 11-322 | IF rod | ||||
Sequence: EKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESNPE | ||||||
Region | 50-58 | Linker 1 | ||||
Sequence: EGLWAEGQA | ||||||
Region | 59-163 | Coil 1B | ||||
Sequence: RCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLT | ||||||
Region | 164-186 | Linker 12 | ||||
Sequence: MHFRARATGPAAPPPRLREVHDS | ||||||
Region | 187-300 | Coil 2 | ||||
Sequence: YALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQV | ||||||
Region | 301-1565 | Tail | ||||
Sequence: KTGLSLEVATYRALLEGESNPEIVIWAEHVENMPSEFRNKSYHYTDSLLQRENERNLFSRQKAPLASFNHSSALYSNLSGHRGSQTGTSIGGDARRGFLGSGYSSSATTQQENSYGKAVSSQTNVRTFSPTYGLLRNTEAQVKTFPDRPKAGDTREVPVYIGEDSTIARESYRDRRDKVAAGASESTRSNERTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDAGGGTGREAEARELRFRLGTSDATGSLQGDSMTETVAENIVTSILKQFTQSPETEASADSFPDTKVTYVDRKELPGERKTKTEIVVESKLTEDVDVSDEAGLDYLLSKDIKEVGLKGKSAEQMIGDIINLGLKGREGRAKVVNVEIVEEPVSYVSGEKPEEFSVPFKVEEVEDVSPGPWGLVKEEEGYGESDVTFSVNQHRRTKQPQENTTHVEEVTEAGDSEGEQSYFVSTPDEHPGGHDRDDGSVYGQIHIEEESTIRYSWQDEIVQGTRRRTQKDGAVGEKVVKPLDVPAPSLEGDLGSTHWKEQARSGEFHAEPTVIEKEIKIPHEFHTSMKGISSKEPRQQLVEVIGQLEETLPERMREELSALTREGQGGPGSVSVDVKKVQGAGGSSVTLVAEVNVSQTVDADRLDLEELSKDEASEMEKAVESVVRESLSRQRSPAPGSPDEEGGAEAPAAGIRFRRWATRELYIPSGESEVAGGASHSSGQRTPQGPVSATVEVSSPTGFAQSQVLEDVSQAARHIKLGPSEVWRTERMSYEGPTAEVVEVSAGGDLSQAASPTGASRSVRHVTLGPGQSPLSREVIFLGPAPACPEAWGSPEPGPAESSADMDGSGRHSTFGCRQFHAEKEIIFQGPISAAGKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQMDVSNVEAIRSRTQEAGALGVSDRGSWRDADSRNDQAVGVSFKASAGEGDQAHREQGKEQAMFDKKVQLQRMVDQRSVISDEKKVALLYLDNEEEENDGHWF | ||||||
Region | 401-421 | Disordered | ||||
Sequence: SGYSSSATTQQENSYGKAVSS | ||||||
Region | 472-609 | Disordered | ||||
Sequence: YRDRRDKVAAGASESTRSNERTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRAEVSPKGLQTPVKDAGGGTGR | ||||||
Compositional bias | 492-589 | Basic and acidic residues | ||||
Sequence: RTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRA | ||||||
Compositional bias | 1019-1036 | Basic and acidic residues | ||||
Sequence: LSKDEASEMEKAVESVVR | ||||||
Region | 1019-1060 | Disordered | ||||
Sequence: LSKDEASEMEKAVESVVRESLSRQRSPAPGSPDEEGGAEAPA | ||||||
Region | 1080-1105 | Disordered | ||||
Sequence: SEVAGGASHSSGQRTPQGPVSATVEV | ||||||
Compositional bias | 1083-1105 | Polar residues | ||||
Sequence: AGGASHSSGQRTPQGPVSATVEV | ||||||
Region | 1152-1463 | Interaction with TLN1 and VCL | ||||
Sequence: VSAGGDLSQAASPTGASRSVRHVTLGPGQSPLSREVIFLGPAPACPEAWGSPEPGPAESSADMDGSGRHSTFGCRQFHAEKEIIFQGPISAAGKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQ | ||||||
Region | 1198-1221 | Disordered | ||||
Sequence: EAWGSPEPGPAESSADMDGSGRHS | ||||||
Region | 1244-1563 | Interaction with DMD and UTRN | ||||
Sequence: GKVGDYFATEESVGTQTSVRQLQLGPKEGFSGQIQFTAPLSDKVELGVIGDSVHMEGLPGSSTSIRHISIGPQRHQTTQQIVYHGLVPQLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSEHIAIRGPVSRTFVLAGSADSPELGKLADSSRTLRHIAPGPKETSFTFQMDVSNVEAIRSRTQEAGALGVSDRGSWRDADSRNDQAVGVSFKASAGEGDQAHREQGKEQAMFDKKVQLQRMVDQRSVISDEKKVALLYLDNEEEENDGH | ||||||
Region | 1332-1415 | Disordered | ||||
Sequence: QLGESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSGVSRSFRHIRLGPTETETSE | ||||||
Compositional bias | 1335-1396 | Polar residues | ||||
Sequence: ESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSG | ||||||
Region | 1505-1525 | Disordered | ||||
Sequence: FKASAGEGDQAHREQGKEQAM | ||||||
Compositional bias | 1511-1525 | Basic and acidic residues | ||||
Sequence: EGDQAHREQGKEQAM |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O15061-1
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
- SynonymsAlpha
- Length1,565
- Mass (Da)172,868
- Last updated2022-02-23 v3
- ChecksumC76056C65127C1C8
O15061-2
- Name2
- SynonymsBeta
- Differences from canonical
- 1152-1463: Missing
O15061-3
- Name3
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A075B7B1 | A0A075B7B1_HUMAN | SYNM | 1253 | ||
H0YL34 | H0YL34_HUMAN | SYNM | 967 | ||
C9JIE4 | C9JIE4_HUMAN | SYNM | 339 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 4 | in Ref. 1; CAC83858/CAC83859 and 3; CAG27071 | ||||
Sequence: W → L | ||||||
Sequence conflict | 24 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: Missing | ||||||
Sequence conflict | 52 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: Missing | ||||||
Sequence conflict | 197 | in Ref. 3; CAG27071 | ||||
Sequence: E → G | ||||||
Sequence conflict | 241 | in Ref. 3; CAG27071 | ||||
Sequence: A → T | ||||||
Sequence conflict | 274 | in Ref. 3; CAG27071 | ||||
Sequence: D → G | ||||||
Sequence conflict | 318 | in Ref. 3; CAG27071 | ||||
Sequence: E → G | ||||||
Sequence conflict | 322 | in Ref. 1; CAC83858/CAC83859 and 3; CAG27071 | ||||
Sequence: E → Q | ||||||
Alternative sequence | VSP_036478 | 336-339 | in isoform 3 | |||
Sequence: EFRN → DGCE | ||||||
Alternative sequence | VSP_036479 | 340-1565 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 373 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: A → V | ||||||
Compositional bias | 492-589 | Basic and acidic residues | ||||
Sequence: RTVILGKKTEVKATREQERNRPETIRTKPEEKMFDSKEKASEERNLRWEELTKLDKEARQRESQQMKEKAKEKDSPKEKSVREREVPISLEVSQDRRA | ||||||
Sequence conflict | 555 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 564 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: K → N | ||||||
Sequence conflict | 655 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 666 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: T → A | ||||||
Sequence conflict | 687 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: V → L | ||||||
Sequence conflict | 720 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: K → N | ||||||
Sequence conflict | 845 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: D → N | ||||||
Sequence conflict | 856 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 874 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: R → P | ||||||
Sequence conflict | 965 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: R → K | ||||||
Sequence conflict | 1004 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: N → D | ||||||
Sequence conflict | 1019 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: L → V | ||||||
Compositional bias | 1019-1036 | Basic and acidic residues | ||||
Sequence: LSKDEASEMEKAVESVVR | ||||||
Sequence conflict | 1039 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: L → M | ||||||
Sequence conflict | 1076 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: P → L | ||||||
Compositional bias | 1083-1105 | Polar residues | ||||
Sequence: AGGASHSSGQRTPQGPVSATVEV | ||||||
Sequence conflict | 1151 | in Ref. 1; CAC83859 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_002465 | 1152-1463 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1292 | in Ref. 1; CAC83859 | ||||
Sequence: I → T | ||||||
Compositional bias | 1335-1396 | Polar residues | ||||
Sequence: ESGDSESTVHGEGSADVHQATHSHTSGRQTVMTEKSTFQSVVSESPQEDSAEDTSGAEMTSG | ||||||
Sequence conflict | 1493 | in Ref. 6; AAI10067 | ||||
Sequence: A → R | ||||||
Sequence conflict | 1509 | in Ref. 1; CAC83858/CAC83859 | ||||
Sequence: A → V | ||||||
Compositional bias | 1511-1525 | Basic and acidic residues | ||||
Sequence: EGDQAHREQGKEQAM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ310521 EMBL· GenBank· DDBJ | CAC83858.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ310522 EMBL· GenBank· DDBJ | CAC83859.1 EMBL· GenBank· DDBJ | mRNA | ||
AF359284 EMBL· GenBank· DDBJ | AAK57487.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ697971 EMBL· GenBank· DDBJ | CAG27071.1 EMBL· GenBank· DDBJ | mRNA | ||
AB002351 EMBL· GenBank· DDBJ | BAA20810.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC036108 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC223423 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC110066 EMBL· GenBank· DDBJ | AAI10067.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC151243 EMBL· GenBank· DDBJ | AAI51244.1 EMBL· GenBank· DDBJ | mRNA |