A2AJ76 · HMCN2_MOUSE
- ProteinHemicentin-2
- GeneHmcn2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids5100 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | basement membrane | |
Cellular Component | cell cortex | |
Cellular Component | cell junction | |
Cellular Component | cleavage furrow | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | neuronal cell body | |
Cellular Component | plasma membrane | |
Molecular Function | axon guidance receptor activity | |
Molecular Function | calcium ion binding | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | synapse organization |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameHemicentin-2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA2AJ76
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutants are viable and fertile with no gross phenotypes (PubMed:32035013).
Double knockout of Hmcn1 and Hmcn2 results in no overt phenotypes with mice being viable and fertile (PubMed:32035013).
Double knockout of Hmcn1 and Hmcn2 results in no overt phenotypes with mice being viable and fertile (PubMed:32035013).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 313 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MTPGAQLLPLLVAISTAVA | ||||||
Chain | PRO_0000395109 | 20-5100 | Hemicentin-2 | |||
Sequence: AVVTSDAPTKTLSPATGDATLAFVFDVTGSMWDDLMQVIDGASRILERSLSSRSRVIANYALVPFHDPDIGPVTLTADPVVFQRELRELYVQGGGDCPEMSVGAIKAAVEVANPGSFIYVFSDARAKDYHKKKELLQLLQLKQSQVVFVLTGDCGDRTHPGYLVFEEIASTSSGQVFQLDKQQVSEVLKWVESAIQASKVHLLSADHEEEGEHTWRIPFDPSLKEVTIALSGPGPEIEVRDPLGRVLQTDEGLNVLLNIPDSAKVVAFKPEHPGLWAIKVYSSGRHSVRISGISNINFRAGFSMQPSLDLNHTIEWPLQGVPISLVINSTGLQAPGHLESVELSHSSGRSLLTLPTQLLSNGSTHQLWAGPPFHVPKERFYLKVKGKDHEGNPLLRVSGVSYSAVAPGVPLVSMAPKIHGYLQQPLLVSCSVYSTLPFQLQLQRDGERLGEERYFQESGNSSWEIPRASKAEEGTYQCIAVSRAGSGRASAQIVITDPPPQLVPGPNVTVSPGETAILSCQVLGETPYNLTWVRDWRALPATTGRISQLSDLSLEVRSIIPTDGGQYQCVASNPNGVTRATTWLLVREAPQVSINARSQRFSQGVEVRVSCSASGYPTPHISWSREGLALPEDSRIHVDAQGTLIIQGLAPEDAGNYSCQATNEVGTDEETVTLYYTDPPSVSAVNAVVLTAVGEEAVLLCAASGVPPPRVIWYRGGLEVILAPGDSRSGTLRIPEAQERDAGLYTCKAVNELGDASAEIQLVVGNAPRLTDPPQDVTVELGKSVFLTCRATGRPPPIVTWRRGDGQALEPGRGSRTGQRDSGVLVFERVSLEDQAPYVCEARNVFGKAQAEARLVVTGHAPPQIANSASVVRVLEGQPVSLTCVILAGRPLPERRWLKAGSPLPPGNRHAVRADGSLHLDRALQEDAGRYSCVATNVAGSQHRDVELVVQVPPRIHPTSTHHVTNEGVPASLPCIASGVPTPKITWTKETNALTTSGHYSVSRNGTLVIVQPSPQDAGAYVCTATNSVGFSSQEMWLSVNTKPMIKMNGSQAVDVPLRVTVKAGEEVTLDCEAQGSPTPLLTWTKDANPLLPVTNRYELLPSGSLRLAQAQVGDNGLYGCTASNPAGATSRRYVLRVQVPPQVQPGPRVLKVLAGEALDLNCVAEGNPQPQLNWFKDGMALMGEGAQGSVHFAAVKTSDAGLYRCEASNSAGTDTWKLELLVLEPPHWGTDETKSLLERVAGENASLPCPAQGTPKPRITWRRGPSSEPLNGRPDVAVLDEGSLFLSSVSLADSGEYECQATNEVGSASRRAKLVVYVPPSIREEGHITNVSGLAGQPLTLECDINGFPAPEVAWLKDGQLVGDSGGGWDGEEASGHRLLDGSRSLHFPRIQESHSGLYSCQAENQAGSAQRDFNLAVFIPPSLLGAGAAQEVLGLAGADVTLECQTSGVPTPQVEWTKDGQPILPGDPHILLQEDGQVLRIISSHLGDEGQYQCVAFSPAGQQAKDFQLSIHSPPTIWGSNETGEVTVLEGHTAQLLCEARGMPSPAITWYKDGTLLAPSSEVVYSKGGRQLQLVKAQPSDAGLYTCQASNPAGITKKSTSLEVYVPPTIEGADGGPYLVQAVAGRPVALECVARGHPPPTISWQHEGLPVVDSNGTWLEAGGALQLENPGEASGGLYSCVASSPAGEAVLQYSVEMQVPPQLLVAEGMGQVTATVGQSLDLPCQASGSPVPTIQWLQNGRPAEELAGVQLASQGTILHISHVELNHSGLFACQATNEAGTAGAEVEVSVHGKQVSVNLGASFSAHHWWGEPHSPFPATCNPPVCRHWSAYPKPSLVERWRGRGNLRGQPSGTVREPGLTLLSQIEKADLRDEGVYTCSATNLAGESKKDVTLKVLVPPNIEPGPVNKVVLENASVTLECLASGVPPPDVSWFKGRQPISTQRRVIVSADGRVLHIERVQLSDAGSYRCVATNVAGSAGLKYGLRVNVPPRITLPPNLPGPVLLGTPFRLTCNATGTPRPTLIWLKDGNPVSPEGIPGLKVFPGGQVLTVASARASDSGSYSCVAVSAVGEDRRDVILQVHMPPSILGEELNMSVVVNESVTLECQSHAVPPPVLRWQKDGRPLEPHPGIRLSADKALLEVDRAAVWDAGHYTCEAINQAGRSEKHFNLHVWVPPAFPSKEPYTLTVTEGQTARLSCDCQGIPFPKISWRKDGQPLPGEGDSLEQVLAVGRLLYLGQAQSAQEGTYTCECSNAAGTSSQEQSLEVLVPPQVTGLWEPLTTVSVIQDGNTTLACNATGKPLPVVTWQRDGQPVSVEPGLRLQNQNHSLHVERAQASHAGGYSCVAENTAGRAERRFALSVLAPPHLTGDSDSLTNVTATLHGSFTLLCEAAGVPAPTVQWFQEGQPISPREGTYLLAGGWMLKMTQAQEQDRGLYSCLASNEAGEARRNFSVEVLVPPSIENEDLEEVIKVPEGQTAQLECNATGHPPPKVTWFKDGQSLTVEDPYEMSPDGAFLWIPQANLSNAGHYSCIASNAVGEKTKHTQLSVLVVPTILGVPEKNANEEVTVTINNPISLICEALAFPSPNITWMKDGSPFEASKNIQLLPGTHGLQILNAQKEDAGQYTCVVTNELGEATKNYHVEVLIPPSISKDDPLGEVSVKEVKTKVNSSLTLECECWATPPPSISWYKDGRPVTPSHRLSVLGEGRLLQIQPTQVSDSGRYLCVATNVAGEDDQDFNVLIQVPPMFQKMGDVDAGFEPLPHEEEAQGRVTEYREIVENNPAYLYCDTNAIPPPELTWYREGQPLSAADGVSVLQGGRILQLPLVQAEDAGRYSCKAANEVGEDWLHYELLVLTPPVIPGDTQELVEEVTVNASSAVSLECPALGNPAPAVSWFQNGLPVSPSPRLQVLEEGQVLKVATAEVADAASYMCVAENQAGSAEKLFTLKVQVPPQISDWTTSQLTATLNSSVSLPCEVYAHPNPEVTWYKDGQPLSLGQEAFLLPGTHTLRLARAQPADSGTYLCEALNAAGRDQKMVQLNVLVPPSFKQAPGGPQEAIQVRAGDKAILSCETDSLPEPAVTWFKDQQPLALGQRIQGLQGGQTLEILDSQASDKGVYSCKVSNTAGEAIRTFVLAIQVPPTFEKPERETVNQVAGRTLVLACDVSGIPAPTVTWLKDRLPVESSVVHGVVSRGGRLQLSHLQPAQAGTYTCVAENAQAEARKDFVVSVLVPPQIQDSGMAQEHNVLEKQEIRLHCEAEGQPPPDITWLKDGGLLDQHVGPHLRFYLDGSTLVLKGLRTADSGAYTCVAHNPAGEDARLHTVNVLVPPTIKQQAGDTGTLVSRTGELVTMVCPVQGSPPIHVSWLKDGLPLPLSQRTLLHSSGRTLRISQVQLADSGVFTCVAASPAGVADRNFTLLVLVPPILEPVEFQNNVMAAQGSEVVLPCEARGSPLPLVSWMKDGEPLLPQSLEQGPGLKLESVSVGDAGTYSCTAASEAGEARRHFQLTVMDPPHIEESGETSELSLTPGAHLELLCEARGIPPPNITWHKDGQALRRTENDSQAGRVLRVDNAGLYTCLAESPAGEVEKSFRVRVQAPPNVVGPRGPRSVVGLAPGQLILECSVEAEPAPEIEWHRGGVLLQADAHTHFPEQGRFLKLQALSTADGGDYSCTARNRAGSTSVAFRVEIHTAPTIQSGPNTVNVSVNRTTLLPCQTHGVPTPLVSWRKDGIPLHPGSPRLEFLPEGSLRIHPVLAQDAGHYLCLASNSAGSDRKGLDLRVFEPPAIAPGPSNLTLTAYSPASLPCEARGSPKPLVTWWKDGQKLDLRLQQGAYRLLPSNALFLTAPSPQDSAQFECVVSNEVGESRRRYQVTVHVPPTIADDQTHFTVTRMAPVILTCHSTGSPTPAVSWSKAGTQLGARGSGYRILPSGALEIERALPLHAGRYTCTARNSAGVARKHMVLTVQASPVVKPLPSVVQVVASEEVLLPCEASGIPQPMVIWQKEGLSIPEGAHMQVLPSGQLRIMHASPEDAGNYFCIAQNSVGSAMAKTRLVVQVPPVIENGLPDLSTIEGSHALLPCTAKGSPEPAITWEKDGHLVSGAEGKFTLQPSGELLVKNSEGQDAGTYICTAENAVGRARRRVHLTILTLPVLTTLPGDRSLRLGDRLWLRCVARGSPTPRIGWTINDQPVTEGVSEQDGGSTLQRAAVTREDSGTYTCWAENRVGRVQAVSFVHVKEAPVLQGEAFSYLVEPVGGSIQLHCVVRGDPAPDIHWTKDGLPLPISRLHFQLQNGSLTILRTKMDDAGRYQCLAVNEMGTVKKVVTVVLQSAPVFQVEPQDVTVRSGVDVELRCRATGEPVPTIEWLRAGRPLQAGRKLRALPDGSLWLEHVEAGDAGVYECVAHNHLGSVTAKALLAVRGEPRGSRGSMTGVINGQEFGMATLNISVLQQGSSEAPTIWSSISQVPASVGPLMRVLVVTIAPIYWALARESGEALNGYSLTGGSFQQESQMEFSTGELLTMTQVARGLDPDGLLLVDMKINGMIPESLADGDLRVQDFQEHYVQTGPGQLFAGSTQRFLHDSLPASLRCNHSIQYDETRGLQPQLVQHLRASSISSAFDPEAEALNFQLTTALQTEENEVGCPEGFEPDVQGAFCVDKDECSGGPSPCSHTCRNAPGHFSCSCPTGFSLAWDHRNCRDVDECAGNTHLCQEEQRCVNLLGSYNCLASCRPGFRVTADGSNCEDVDECLEQLDECHYNQLCENTPGGHHCGCPRGYRQQGHSLPCLDINECLQLPTPCVYQCQNLQGSYRCLCPPGQTLLRDGRTCIPLERNRQNITIVSHRSPFGPWLRSRVPRPSSSYHTWVSLRPGSGALNSVGRAWCPPGFIRQDGVCADLDECRVRSLCQHACQNTEGSYYCLCPSGYRLLPSGKNCQDINECEEDGIECGPGQMCFNTRGSFQCVDTPCPTTYRQGSSPGTCFRRCSQDCSASGPSTLQYRLLPLPLGVRAHHDVARLAAFSEAGIPANRTELTVLEPDPRSPFALRQLRAGQGAVYTRRALTRAGLYRLTVRAAAPRHQSVYILLIAVSPYPY | ||||||
Glycosylation | 330 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 347 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 380 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 449↔497 | |||||
Sequence: CSVYSTLPFQLQLQRDGERLGEERYFQESGNSSWEIPRASKAEEGTYQC | ||||||
Glycosylation | 479 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 526 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 539↔588 | |||||
Sequence: CQVLGETPYNLTWVRDWRALPATTGRISQLSDLSLEVRSIIPTDGGQYQC | ||||||
Glycosylation | 548 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 630↔678 | |||||
Sequence: CSASGYPTPHISWSREGLALPEDSRIHVDAQGTLIIQGLAPEDAGNYSC | ||||||
Glycosylation | 675 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 720↔766 | |||||
Sequence: CAASGVPPPRVIWYRGGLEVILAPGDSRSGTLRIPEAQERDAGLYTC | ||||||
Disulfide bond | 808↔859 | |||||
Sequence: CRATGRPPPIVTWRRGDGQALEPGRGSRTGQRDSGVLVFERVSLEDQAPYVC | ||||||
Disulfide bond | 903↔952 | |||||
Sequence: CVILAGRPLPERRWLKAGSPLPPGNRHAVRADGSLHLDRALQEDAGRYSC | ||||||
Modified residue | 909 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 914 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 915 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Disulfide bond | 994↔1042 | |||||
Sequence: CIASGVPTPKITWTKETNALTTSGHYSVSRNGTLVIVQPSPQDAGAYVC | ||||||
Glycosylation | 1024 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1068 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1091↔1140 | |||||
Sequence: CEAQGSPTPLLTWTKDANPLLPVTNRYELLPSGSLRLAQAQVGDNGLYGC | ||||||
Disulfide bond | 1182↔1225 | |||||
Sequence: CVAEGNPQPQLNWFKDGMALMGEGAQGSVHFAAVKTSDAGLYRC | ||||||
Glycosylation | 1264 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1269↔1319 | |||||
Sequence: CPAQGTPKPRITWRRGPSSEPLNGRPDVAVLDEGSLFLSSVSLADSGEYEC | ||||||
Glycosylation | 1350 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1363↔1421 | |||||
Sequence: CDINGFPAPEVAWLKDGQLVGDSGGGWDGEEASGHRLLDGSRSLHFPRIQESHSGLYSC | ||||||
Disulfide bond | 1465↔1515 | |||||
Sequence: CQTSGVPTPQVEWTKDGQPILPGDPHILLQEDGQVLRIISSHLGDEGQYQC | ||||||
Glycosylation | 1542 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1559↔1608 | |||||
Sequence: CEARGMPSPAITWYKDGTLLAPSSEVVYSKGGRQLQLVKAQPSDAGLYTC | ||||||
Disulfide bond | 1653↔1701 | |||||
Sequence: CVARGHPPPTISWQHEGLPVVDSNGTWLEAGGALQLENPGEASGGLYSC | ||||||
Glycosylation | 1676 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1745↔1794 | |||||
Sequence: CQASGSPVPTIQWLQNGRPAEELAGVQLASQGTILHISHVELNHSGLFAC | ||||||
Glycosylation | 1787 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1846↔1899 | |||||
Sequence: CRHWSAYPKPSLVERWRGRGNLRGQPSGTVREPGLTLLSQIEKADLRDEGVYTC | ||||||
Glycosylation | 1934 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1941↔1990 | |||||
Sequence: CLASGVPPPDVSWFKGRQPISTQRRVIVSADGRVLHIERVQLSDAGSYRC | ||||||
Disulfide bond | 2033↔2084 | |||||
Sequence: CNATGTPRPTLIWLKDGNPVSPEGIPGLKVFPGGQVLTVASARASDSGSYSC | ||||||
Glycosylation | 2034 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2119 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2126↔2175 | |||||
Sequence: CQSHAVPPPVLRWQKDGRPLEPHPGIRLSADKALLEVDRAAVWDAGHYTC | ||||||
Disulfide bond | 2218↔2269 | |||||
Sequence: CDCQGIPFPKISWRKDGQPLPGEGDSLEQVLAVGRLLYLGQAQSAQEGTYTC | ||||||
Glycosylation | 2309 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2314↔2363 | |||||
Sequence: CNATGKPLPVVTWQRDGQPVSVEPGLRLQNQNHSLHVERAQASHAGGYSC | ||||||
Glycosylation | 2315 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2395 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2408↔2457 | |||||
Sequence: CEAAGVPAPTVQWFQEGQPISPREGTYLLAGGWMLKMTQAQEQDRGLYSC | ||||||
Glycosylation | 2469 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2501↔2550 | |||||
Sequence: CNATGHPPPKVTWFKDGQSLTVEDPYEMSPDGAFLWIPQANLSNAGHYSC | ||||||
Glycosylation | 2502 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2541 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2597↔2646 | |||||
Sequence: CEALAFPSPNITWMKDGSPFEASKNIQLLPGTHGLQILNAQKEDAGQYTC | ||||||
Glycosylation | 2606 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2688 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2695↔2744 | |||||
Sequence: CECWATPPPSISWYKDGRPVTPSHRLSVLGEGRLLQIQPTQVSDSGRYLC | ||||||
Disulfide bond | 2806↔2855 | |||||
Sequence: CDTNAIPPPELTWYREGQPLSAADGVSVLQGGRILQLPLVQAEDAGRYSC | ||||||
Glycosylation | 2892 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2901↔2950 | |||||
Sequence: CPALGNPAPAVSWFQNGLPVSPSPRLQVLEEGQVLKVATAEVADAASYMC | ||||||
Glycosylation | 2986 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2993↔3042 | |||||
Sequence: CEVYAHPNPEVTWYKDGQPLSLGQEAFLLPGTHTLRLARAQPADSGTYLC | ||||||
Disulfide bond | 3088↔3137 | |||||
Sequence: CETDSLPEPAVTWFKDQQPLALGQRIQGLQGGQTLEILDSQASDKGVYSC | ||||||
Disulfide bond | 3180↔3229 | |||||
Sequence: CDVSGIPAPTVTWLKDRLPVESSVVHGVVSRGGRLQLSHLQPAQAGTYTC | ||||||
Disulfide bond | 3273↔3324 | |||||
Sequence: CEAEGQPPPDITWLKDGGLLDQHVGPHLRFYLDGSTLVLKGLRTADSGAYTC | ||||||
Disulfide bond | 3369↔3418 | |||||
Sequence: CPVQGSPPIHVSWLKDGLPLPLSQRTLLHSSGRTLRISQVQLADSGVFTC | ||||||
Glycosylation | 3430 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3462↔3507 | |||||
Sequence: CEARGSPLPLVSWMKDGEPLLPQSLEQGPGLKLESVSVGDAGTYSC | ||||||
Disulfide bond | 3551↔3593 | |||||
Sequence: CEARGIPPPNITWHKDGQALRRTENDSQAGRVLRVDNAGLYTC | ||||||
Glycosylation | 3560 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3575 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3637↔3686 | |||||
Sequence: CSVEAEPAPEIEWHRGGVLLQADAHTHFPEQGRFLKLQALSTADGGDYSC | ||||||
Glycosylation | 3717 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3721 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3728↔3777 | |||||
Sequence: CQTHGVPTPLVSWRKDGIPLHPGSPRLEFLPEGSLRIHPVLAQDAGHYLC | ||||||
Glycosylation | 3806 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3819↔3870 | |||||
Sequence: CEARGSPKPLVTWWKDGQKLDLRLQQGAYRLLPSNALFLTAPSPQDSAQFEC | ||||||
Disulfide bond | 3912↔3961 | |||||
Sequence: CHSTGSPTPAVSWSKAGTQLGARGSGYRILPSGALEIERALPLHAGRYTC | ||||||
Disulfide bond | 4003↔4051 | |||||
Sequence: CEASGIPQPMVIWQKEGLSIPEGAHMQVLPSGQLRIMHASPEDAGNYFC | ||||||
Disulfide bond | 4093↔4142 | |||||
Sequence: CTAKGSPEPAITWEKDGHLVSGAEGKFTLQPSGELLVKNSEGQDAGTYIC | ||||||
Disulfide bond | 4184↔4231 | |||||
Sequence: CVARGSPTPRIGWTINDQPVTEGVSEQDGGSTLQRAAVTREDSGTYTC | ||||||
Disulfide bond | 4274↔4322 | |||||
Sequence: CVVRGDPAPDIHWTKDGLPLPISRLHFQLQNGSLTILRTKMDDAGRYQC | ||||||
Glycosylation | 4304 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4364↔4412 | |||||
Sequence: CRATGEPVPTIEWLRAGRPLQAGRKLRALPDGSLWLEHVEAGDAGVYEC | ||||||
Glycosylation | 4455 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4601 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4672↔4683 | |||||
Sequence: CSGGPSPCSHTC | ||||||
Disulfide bond | 4679↔4692 | |||||
Sequence: CSHTCRNAPGHFSC | ||||||
Disulfide bond | 4694↔4707 | |||||
Sequence: CPTGFSLAWDHRNC | ||||||
Disulfide bond | 4713↔4726 | |||||
Sequence: CAGNTHLCQEEQRC | ||||||
Disulfide bond | 4720↔4735 | |||||
Sequence: CQEEQRCVNLLGSYNC | ||||||
Disulfide bond | 4739↔4752 | |||||
Sequence: CRPGFRVTADGSNC | ||||||
Disulfide bond | 4758↔4771 | |||||
Sequence: CLEQLDECHYNQLC | ||||||
Disulfide bond | 4765↔4780 | |||||
Sequence: CHYNQLCENTPGGHHC | ||||||
Disulfide bond | 4801↔4812 | |||||
Sequence: CLQLPTPCVYQC | ||||||
Disulfide bond | 4808↔4821 | |||||
Sequence: CVYQCQNLQGSYRC | ||||||
Disulfide bond | 4823↔4836 | |||||
Sequence: CPPGQTLLRDGRTC | ||||||
Glycosylation | 4845 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4908↔4918 | |||||
Sequence: CRVRSLCQHAC | ||||||
Disulfide bond | 4914↔4927 | |||||
Sequence: CQHACQNTEGSYYC | ||||||
Disulfide bond | 4929↔4942 | |||||
Sequence: CPSGYRLLPSGKNC | ||||||
Glycosylation | 5035 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Reported to be phosphorylated; however as this position is extracellular, the in vivo relevance is unsure.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In neonatal skin, localized in the pericellular space of basal epidermal keratinocytes (at protein level) (PubMed:34504132).
In adult skin, restricted to basal keratinocytes of hair follicles and the interfollicular epidermis (PubMed:34504132).
Absent from the myotendinous junction but present in skeletal muscle (at protein level) (PubMed:34504132).
Expressed in the pericellular extracellular matrix of epithelial cells in a number of tissues including embryonic trophectoderm and adult skin and tongue (PubMed:17015624).
Also present in the extracellular matrix of some, but not all, blood vessels (PubMed:17015624).
Expressed primarily in epithelial cells in the embryonic epidermis, lung, intestine, skeletal hindlimb muscle, tongue and the muscular layers of the esophagus (PubMed:34504132).
In adult skin, restricted to basal keratinocytes of hair follicles and the interfollicular epidermis (PubMed:34504132).
Absent from the myotendinous junction but present in skeletal muscle (at protein level) (PubMed:34504132).
Expressed in the pericellular extracellular matrix of epithelial cells in a number of tissues including embryonic trophectoderm and adult skin and tongue (PubMed:17015624).
Also present in the extracellular matrix of some, but not all, blood vessels (PubMed:17015624).
Expressed primarily in epithelial cells in the embryonic epidermis, lung, intestine, skeletal hindlimb muscle, tongue and the muscular layers of the esophagus (PubMed:34504132).
Induction
Following wounding, up-regulated in the basal keratinocytes within the epidermal tongues of closing wounds.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-211 | VWFA | ||||
Sequence: DATLAFVFDVTGSMWDDLMQVIDGASRILERSLSSRSRVIANYALVPFHDPDIGPVTLTADPVVFQRELRELYVQGGGDCPEMSVGAIKAAVEVANPGSFIYVFSDARAKDYHKKKELLQLLQLKQSQVVFVLTGDCGDRTHPGYLVFEEIASTSSGQVFQLDKQQVSEVLKWVE | ||||||
Domain | 426-515 | Ig-like C2-type 1 | ||||
Sequence: PGVPLVSMAPKIHGYLQQPLLVSCSVYSTLPFQLQLQRDGERLGEERYFQESGNSSWEIPRASKAEEGTYQCIAVSRAGSGRASAQIVIT | ||||||
Domain | 517-601 | Ig-like C2-type 2 | ||||
Sequence: PPPQLVPGPNVTVSPGETAILSCQVLGETPYNLTWVRDWRALPATTGRISQLSDLSLEVRSIIPTDGGQYQCVASNPNGVTRATT | ||||||
Domain | 609-692 | Ig-like C2-type 3 | ||||
Sequence: PQVSINARSQRFSQGVEVRVSCSASGYPTPHISWSREGLALPEDSRIHVDAQGTLIIQGLAPEDAGNYSCQATNEVGTDEETVT | ||||||
Domain | 699-782 | Ig-like C2-type 4 | ||||
Sequence: PSVSAVNAVVLTAVGEEAVLLCAASGVPPPRVIWYRGGLEVILAPGDSRSGTLRIPEAQERDAGLYTCKAVNELGDASAEIQLV | ||||||
Domain | 787-877 | Ig-like C2-type 5 | ||||
Sequence: PRLTDPPQDVTVELGKSVFLTCRATGRPPPIVTWRRGDGQALEPGRGSRTGQRDSGVLVFERVSLEDQAPYVCEARNVFGKAQAEARLVVT | ||||||
Domain | 882-968 | Ig-like C2-type 6 | ||||
Sequence: PQIANSASVVRVLEGQPVSLTCVILAGRPLPERRWLKAGSPLPPGNRHAVRADGSLHLDRALQEDAGRYSCVATNVAGSQHRDVELV | ||||||
Domain | 973-1058 | Ig-like C2-type 7 | ||||
Sequence: PRIHPTSTHHVTNEGVPASLPCIASGVPTPKITWTKETNALTTSGHYSVSRNGTLVIVQPSPQDAGAYVCTATNSVGFSSQEMWLS | ||||||
Domain | 1063-1156 | Ig-like C2-type 8 | ||||
Sequence: PMIKMNGSQAVDVPLRVTVKAGEEVTLDCEAQGSPTPLLTWTKDANPLLPVTNRYELLPSGSLRLAQAQVGDNGLYGCTASNPAGATSRRYVLR | ||||||
Domain | 1161-1239 | Ig-like C2-type 9 | ||||
Sequence: PQVQPGPRVLKVLAGEALDLNCVAEGNPQPQLNWFKDGMALMGEGAQGSVHFAAVKTSDAGLYRCEASNSAGTDTWKLE | ||||||
Domain | 1246-1335 | Ig-like C2-type 10 | ||||
Sequence: PHWGTDETKSLLERVAGENASLPCPAQGTPKPRITWRRGPSSEPLNGRPDVAVLDEGSLFLSSVSLADSGEYECQATNEVGSASRRAKLV | ||||||
Region | 1265-1293 | Disordered | ||||
Sequence: ASLPCPAQGTPKPRITWRRGPSSEPLNGR | ||||||
Domain | 1340-1437 | Ig-like C2-type 11 | ||||
Sequence: PSIREEGHITNVSGLAGQPLTLECDINGFPAPEVAWLKDGQLVGDSGGGWDGEEASGHRLLDGSRSLHFPRIQESHSGLYSCQAENQAGSAQRDFNLA | ||||||
Domain | 1442-1531 | Ig-like C2-type 12 | ||||
Sequence: PSLLGAGAAQEVLGLAGADVTLECQTSGVPTPQVEWTKDGQPILPGDPHILLQEDGQVLRIISSHLGDEGQYQCVAFSPAGQQAKDFQLS | ||||||
Domain | 1536-1624 | Ig-like C2-type 13 | ||||
Sequence: PTIWGSNETGEVTVLEGHTAQLLCEARGMPSPAITWYKDGTLLAPSSEVVYSKGGRQLQLVKAQPSDAGLYTCQASNPAGITKKSTSLE | ||||||
Domain | 1629-1717 | Ig-like C2-type 14 | ||||
Sequence: PTIEGADGGPYLVQAVAGRPVALECVARGHPPPTISWQHEGLPVVDSNGTWLEAGGALQLENPGEASGGLYSCVASSPAGEAVLQYSVE | ||||||
Domain | 1722-1810 | Ig-like C2-type 15 | ||||
Sequence: PQLLVAEGMGQVTATVGQSLDLPCQASGSPVPTIQWLQNGRPAEELAGVQLASQGTILHISHVELNHSGLFACQATNEAGTAGAEVEVS | ||||||
Domain | 1825-1913 | Ig-like C2-type 16 | ||||
Sequence: SAHHWWGEPHSPFPATCNPPVCRHWSAYPKPSLVERWRGRGNLRGQPSGTVREPGLTLLSQIEKADLRDEGVYTCSATNLAGESKKDVT | ||||||
Domain | 1920-2008 | Ig-like C2-type 17 | ||||
Sequence: PNIEPGPVNKVVLENASVTLECLASGVPPPDVSWFKGRQPISTQRRVIVSADGRVLHIERVQLSDAGSYRCVATNVAGSAGLKYGLRVN | ||||||
Domain | 2011-2100 | Ig-like C2-type 18 | ||||
Sequence: PRITLPPNLPGPVLLGTPFRLTCNATGTPRPTLIWLKDGNPVSPEGIPGLKVFPGGQVLTVASARASDSGSYSCVAVSAVGEDRRDVILQ | ||||||
Domain | 2105-2189 | Ig-like C2-type 19 | ||||
Sequence: PSILGEELNMSVVVNESVTLECQSHAVPPPVLRWQKDGRPLEPHPGIRLSADKALLEVDRAAVWDAGHYTCEAINQAGRSEKHFN | ||||||
Domain | 2196-2285 | Ig-like C2-type 20 | ||||
Sequence: PAFPSKEPYTLTVTEGQTARLSCDCQGIPFPKISWRKDGQPLPGEGDSLEQVLAVGRLLYLGQAQSAQEGTYTCECSNAAGTSSQEQSLE | ||||||
Domain | 2290-2379 | Ig-like C2-type 21 | ||||
Sequence: PQVTGLWEPLTTVSVIQDGNTTLACNATGKPLPVVTWQRDGQPVSVEPGLRLQNQNHSLHVERAQASHAGGYSCVAENTAGRAERRFALS | ||||||
Domain | 2384-2473 | Ig-like C2-type 22 | ||||
Sequence: PHLTGDSDSLTNVTATLHGSFTLLCEAAGVPAPTVQWFQEGQPISPREGTYLLAGGWMLKMTQAQEQDRGLYSCLASNEAGEARRNFSVE | ||||||
Domain | 2478-2566 | Ig-like C2-type 23 | ||||
Sequence: PSIENEDLEEVIKVPEGQTAQLECNATGHPPPKVTWFKDGQSLTVEDPYEMSPDGAFLWIPQANLSNAGHYSCIASNAVGEKTKHTQLS | ||||||
Domain | 2571-2662 | Ig-like C2-type 24 | ||||
Sequence: PTILGVPEKNANEEVTVTINNPISLICEALAFPSPNITWMKDGSPFEASKNIQLLPGTHGLQILNAQKEDAGQYTCVVTNELGEATKNYHVE | ||||||
Domain | 2667-2758 | Ig-like C2-type 25 | ||||
Sequence: PSISKDDPLGEVSVKEVKTKVNSSLTLECECWATPPPSISWYKDGRPVTPSHRLSVLGEGRLLQIQPTQVSDSGRYLCVATNVAGEDDQDFN | ||||||
Domain | 2781-2871 | Ig-like C2-type 26 | ||||
Sequence: PHEEEAQGRVTEYREIVENNPAYLYCDTNAIPPPELTWYREGQPLSAADGVSVLQGGRILQLPLVQAEDAGRYSCKAANEVGEDWLHYELL | ||||||
Domain | 2875-2964 | Ig-like C2-type 27 | ||||
Sequence: PPVIPGDTQELVEEVTVNASSAVSLECPALGNPAPAVSWFQNGLPVSPSPRLQVLEEGQVLKVATAEVADAASYMCVAENQAGSAEKLFT | ||||||
Domain | 2971-3058 | Ig-like C2-type 28 | ||||
Sequence: PQISDWTTSQLTATLNSSVSLPCEVYAHPNPEVTWYKDGQPLSLGQEAFLLPGTHTLRLARAQPADSGTYLCEALNAAGRDQKMVQLN | ||||||
Domain | 3063-3153 | Ig-like C2-type 29 | ||||
Sequence: PSFKQAPGGPQEAIQVRAGDKAILSCETDSLPEPAVTWFKDQQPLALGQRIQGLQGGQTLEILDSQASDKGVYSCKVSNTAGEAIRTFVLA | ||||||
Domain | 3157-3245 | Ig-like C2-type 30 | ||||
Sequence: PPTFEKPERETVNQVAGRTLVLACDVSGIPAPTVTWLKDRLPVESSVVHGVVSRGGRLQLSHLQPAQAGTYTCVAENAQAEARKDFVVS | ||||||
Domain | 3250-3340 | Ig-like C2-type 31 | ||||
Sequence: PQIQDSGMAQEHNVLEKQEIRLHCEAEGQPPPDITWLKDGGLLDQHVGPHLRFYLDGSTLVLKGLRTADSGAYTCVAHNPAGEDARLHTVN | ||||||
Domain | 3345-3432 | Ig-like C2-type 32 | ||||
Sequence: PTIKQQAGDTGTLVSRTGELVTMVCPVQGSPPIHVSWLKDGLPLPLSQRTLLHSSGRTLRISQVQLADSGVFTCVAASPAGVADRNFT | ||||||
Domain | 3438-3523 | Ig-like C2-type 33 | ||||
Sequence: PPILEPVEFQNNVMAAQGSEVVLPCEARGSPLPLVSWMKDGEPLLPQSLEQGPGLKLESVSVGDAGTYSCTAASEAGEARRHFQLT | ||||||
Domain | 3528-3609 | Ig-like C2-type 34 | ||||
Sequence: PHIEESGETSELSLTPGAHLELLCEARGIPPPNITWHKDGQALRRTENDSQAGRVLRVDNAGLYTCLAESPAGEVEKSFRVR | ||||||
Domain | 3614-3702 | Ig-like C2-type 35 | ||||
Sequence: PNVVGPRGPRSVVGLAPGQLILECSVEAEPAPEIEWHRGGVLLQADAHTHFPEQGRFLKLQALSTADGGDYSCTARNRAGSTSVAFRVE | ||||||
Domain | 3707-3793 | Ig-like C2-type 36 | ||||
Sequence: PTIQSGPNTVNVSVNRTTLLPCQTHGVPTPLVSWRKDGIPLHPGSPRLEFLPEGSLRIHPVLAQDAGHYLCLASNSAGSDRKGLDLR | ||||||
Domain | 3798-3886 | Ig-like C2-type 37 | ||||
Sequence: PAIAPGPSNLTLTAYSPASLPCEARGSPKPLVTWWKDGQKLDLRLQQGAYRLLPSNALFLTAPSPQDSAQFECVVSNEVGESRRRYQVT | ||||||
Domain | 3891-3977 | Ig-like C2-type 38 | ||||
Sequence: PTIADDQTHFTVTRMAPVILTCHSTGSPTPAVSWSKAGTQLGARGSGYRILPSGALEIERALPLHAGRYTCTARNSAGVARKHMVLT | ||||||
Domain | 3982-4067 | Ig-like C2-type 39 | ||||
Sequence: PVVKPLPSVVQVVASEEVLLPCEASGIPQPMVIWQKEGLSIPEGAHMQVLPSGQLRIMHASPEDAGNYFCIAQNSVGSAMAKTRLV | ||||||
Domain | 4071-4158 | Ig-like C2-type 40 | ||||
Sequence: PPVIENGLPDLSTIEGSHALLPCTAKGSPEPAITWEKDGHLVSGAEGKFTLQPSGELLVKNSEGQDAGTYICTAENAVGRARRRVHLT | ||||||
Domain | 4163-4244 | Ig-like C2-type 41 | ||||
Sequence: PVLTTLPGDRSLRLGDRLWLRCVARGSPTPRIGWTINDQPVTEGVSEQDGGSTLQRAAVTREDSGTYTCWAENRVGRVQAVS | ||||||
Domain | 4252-4336 | Ig-like C2-type 42 | ||||
Sequence: PVLQGEAFSYLVEPVGGSIQLHCVVRGDPAPDIHWTKDGLPLPISRLHFQLQNGSLTILRTKMDDAGRYQCLAVNEMGTVKKVVT | ||||||
Domain | 4343-4428 | Ig-like C2-type 43 | ||||
Sequence: PVFQVEPQDVTVRSGVDVELRCRATGEPVPTIEWLRAGRPLQAGRKLRALPDGSLWLEHVEAGDAGVYECVAHNHLGSVTAKALLA | ||||||
Domain | 4432-4654 | Nidogen G2 beta-barrel | ||||
Sequence: EPRGSRGSMTGVINGQEFGMATLNISVLQQGSSEAPTIWSSISQVPASVGPLMRVLVVTIAPIYWALARESGEALNGYSLTGGSFQQESQMEFSTGELLTMTQVARGLDPDGLLLVDMKINGMIPESLADGDLRVQDFQEHYVQTGPGQLFAGSTQRFLHDSLPASLRCNHSIQYDETRGLQPQLVQHLRASSISSAFDPEAEALNFQLTTALQTEENEVGCP | ||||||
Domain | 4668-4708 | EGF-like 1; calcium-binding | ||||
Sequence: DKDECSGGPSPCSHTCRNAPGHFSCSCPTGFSLAWDHRNCR | ||||||
Domain | 4709-4753 | EGF-like 2; calcium-binding | ||||
Sequence: DVDECAGNTHLCQEEQRCVNLLGSYNCLASCRPGFRVTADGSNCE | ||||||
Domain | 4754-4789 | EGF-like 3; calcium-binding | ||||
Sequence: DVDECLEQLDECHYNQLCENTPGGHHCGCPRGYRQQ | ||||||
Domain | 4797-4837 | EGF-like 4; calcium-binding | ||||
Sequence: DINECLQLPTPCVYQCQNLQGSYRCLCPPGQTLLRDGRTCI | ||||||
Domain | 4904-4943 | EGF-like 5; calcium-binding | ||||
Sequence: DLDECRVRSLCQHACQNTEGSYYCLCPSGYRLLPSGKNCQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
A2AJ76-1
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
- Length5,100
- Mass (Da)547,198
- Last updated2007-02-20 v1
- Checksum74EAFA906677B3DF
A2AJ76-2
- Name2
- Differences from canonical
- 1-4439: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BRN3 | A0A2I3BRN3_MOUSE | Hmcn2 | 1449 | ||
F6VSY0 | F6VSY0_MOUSE | Hmcn2 | 236 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039372 | 1-4439 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 5026 | in Ref. 1; BAC38997 | ||||
Sequence: A → V | ||||||
Sequence conflict | 5068 | in Ref. 1; BAC38997 | ||||
Sequence: L → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK083701 EMBL· GenBank· DDBJ | BAC38997.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AL732564 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL732572 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL928861 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |