P13942 · COBA2_HUMAN
- ProteinCollagen alpha-2(XI) chain
- GeneCOL11A2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for binding site.
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 | collagen trimer | |
Cellular Component | collagen type XI trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | heparin binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Biological Process | cartilage development | |
Biological Process | collagen fibril organization | |
Biological Process | roof of mouth development | |
Biological Process | sensory perception of sound | |
Biological Process | skeletal system development | |
Biological Process | soft palate development |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-2(XI) chain
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP13942
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Otospondylomegaepiphyseal dysplasia, autosomal dominant (OSMEDA)
- Note
- DescriptionAn autosomal dominant form of otospondylomegaepiphyseal dysplasia, a disorder characterized by sensorineural deafness, enlarged epiphyses, mild platyspondyly, and disproportionate shortness of the limbs. Total body length is normal. Typical facial features are mid-face hypoplasia, short upturned nose and depressed nasal bridge. Most patients have Pierre Robin sequence including an opening in the roof of the mouth (cleft palate) and a small lower jaw (micrognathia). Ocular symptoms are absent. Some patients have early-onset osteoarthritis.
- See alsoMIM:184840
Natural variants in OSMEDA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_013594 | 940-948 | missing | in OSMEDA | |
VAR_013595 | 1441 | G>E | in OSMEDA; dbSNP:rs121912946 |
Otospondylomegaepiphyseal dysplasia, autosomal recessive (OSMEDB)
- Note
- DescriptionAn autosomal recessive form of otospondylomegaepiphyseal dysplasia, a disorder characterized by sensorineural deafness, enlarged epiphyses, mild platyspondyly, and disproportionate shortness of the limbs. Total body length is normal. Typical facial features are mid-face hypoplasia, short upturned nose and depressed nasal bridge. Most patients have Pierre Robin sequence including an opening in the roof of the mouth (cleft palate) and a small lower jaw (micrognathia). Ocular symptoms are absent. Some patients have early-onset osteoarthritis.
- See alsoMIM:215150
Natural variants in OSMEDB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001907 | 661 | G>R | in OSMEDB; dbSNP:rs121912945 |
Deafness, autosomal dominant, 13 (DFNA13)
- Note
- DescriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
- See alsoMIM:601868
Natural variants in DFNA13
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_010655 | 808 | G>E | in DFNA13; dbSNP:rs121912948 | |
VAR_010656 | 1034 | R>C | in DFNA13; dbSNP:rs121912947 |
Deafness, autosomal recessive, 53 (DFNB53)
- Note
- DescriptionA form of non-syndromic sensorineural deafness characterized by prelingual, profound, non-progressive hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
- See alsoMIM:609706
Natural variants in DFNB53
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072731 | 37 | A>S | in DFNB53; dbSNP:rs606231410 | |
VAR_025276 | 621 | P>T | in DFNB53; dbSNP:rs121912952 | |
VAR_072732 | 888 | P>T | in DFNB53; dbSNP:rs864309523 |
Fibrochondrogenesis 2 (FBCG2)
- Note
- DescriptionA severe skeletal dysplasia characterized by a flat midface, short long bones, short ribs with broad metaphyses, and vertebral bodies that show distinctive hypoplastic posterior ends and rounded anterior ends, giving the vertebral bodies a pinched appearance on lateral radiographic views. The chest is small, causing perinatal respiratory problems which usually, but not always, result in lethality. Affected individuals who survive the neonatal period have high myopia, mild to moderate hearing loss, and severe skeletal dysplasia.
- See alsoMIM:614524
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_072731 | 37 | in DFNB53; dbSNP:rs606231410 | |||
Sequence: A → S | ||||||
Natural variant | VAR_048804 | 236 | in dbSNP:rs35116188 | |||
Sequence: P → S | ||||||
Natural variant | VAR_048805 | 276 | in dbSNP:rs9277934 | |||
Sequence: E → K | ||||||
Natural variant | VAR_013591 | 593 | ||||
Sequence: D → G | ||||||
Natural variant | VAR_025276 | 621 | in DFNB53; dbSNP:rs121912952 | |||
Sequence: P → T | ||||||
Natural variant | VAR_001907 | 661 | in OSMEDB; dbSNP:rs121912945 | |||
Sequence: G → R | ||||||
Natural variant | VAR_010655 | 808 | in DFNA13; dbSNP:rs121912948 | |||
Sequence: G → E | ||||||
Natural variant | VAR_013592 | 824 | in dbSNP:rs1799909 | |||
Sequence: E → K | ||||||
Natural variant | VAR_013593 | 879 | in dbSNP:rs747883362 | |||
Sequence: P → L | ||||||
Natural variant | VAR_072732 | 888 | in DFNB53; dbSNP:rs864309523 | |||
Sequence: P → T | ||||||
Natural variant | VAR_048806 | 894 | in dbSNP:rs2855430 | |||
Sequence: L → P | ||||||
Natural variant | VAR_013594 | 940-948 | in OSMEDA | |||
Sequence: Missing | ||||||
Natural variant | VAR_010656 | 1034 | in DFNA13; dbSNP:rs121912947 | |||
Sequence: R → C | ||||||
Natural variant | VAR_013596 | 1316 | in dbSNP:rs2229784 | |||
Sequence: P → T | ||||||
Natural variant | VAR_079875 | 1422 | in dbSNP:rs555936333 | |||
Sequence: P → L | ||||||
Natural variant | VAR_013595 | 1441 | in OSMEDA; dbSNP:rs121912946 | |||
Sequence: G → E | ||||||
Natural variant | VAR_013597 | 1600 | in dbSNP:rs1799912 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_033797 | 1628 | in dbSNP:rs2229790 | |||
Sequence: E → D | ||||||
Natural variant | VAR_048807 | 1722 | in dbSNP:rs2229792 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,487 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, propeptide, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MERCSRCHRLLLLLPLVLGLSAAPGWA | ||||||
Chain | PRO_0000005840 | 28-1736 | Collagen alpha-2(XI) chain | |||
Sequence: GAPPVDVLRALRFPSLPDGVRRAKGICPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQVPPTADRFQAEEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGDPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPQGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPQGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPLGPPGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLPGTAGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPSGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGIQGEPGVKGPRGERGEKGESGQPGEPGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEGGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGSPGSEGRQGGKGAKGDPGAIGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSPGQKGEMGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPGGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSRLMQEDEAIPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFMG | ||||||
Propeptide | PRO_0000005841 | 1501-1736 | C-terminal propeptide | |||
Sequence: IQPLPIQMPKKTRRSVDGSRLMQEDEAIPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFMG | ||||||
Disulfide bond | 1571↔1603 | |||||
Sequence: CQDLKLCHPELPDGEYWVDPNQGCARDAFRVFC | ||||||
Disulfide bond | 1577 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1594 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1604 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1612↔1733 | |||||
Sequence: CVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVC | ||||||
Disulfide bond | 1655↔1689 | |||||
Sequence: CSGAARDGPLRLRGANEDELSPETSPYVKEFRDGC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P13942 | DDR2 Q16832 | 2 | EBI-2515504, EBI-1381484 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 57-228 | Laminin G-like | ||||
Sequence: DVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELEC | ||||||
Region | 215-486 | Nonhelical region | ||||
Sequence: QAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQVPPTADRFQAEEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARLALR | ||||||
Region | 227-303 | Disordered | ||||
Sequence: ECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEIL | ||||||
Compositional bias | 233-271 | Polar residues | ||||
Sequence: RERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESL | ||||||
Region | 330-465 | Disordered | ||||
Sequence: EEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGP | ||||||
Domain | 399-447 | Collagen-like 1 | ||||
Sequence: GPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPG | ||||||
Region | 485-1538 | Disordered | ||||
Sequence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| ||||||
Domain | 487-545 | Collagen-like 2 | ||||
Sequence: GPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGA | ||||||
Region | 487-1500 | Triple-helical region | ||||
Sequence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| ||||||
Domain | 546-590 | Collagen-like 3 | ||||
Sequence: RGMPGDPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGE | ||||||
Compositional bias | 727-744 | Basic and acidic residues | ||||
Sequence: GIRGLKGHKGEKGEDGFP | ||||||
Domain | 805-862 | Collagen-like 4 | ||||
Sequence: GRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKG | ||||||
Domain | 863-899 | Collagen-like 5 | ||||
Sequence: TSGGDGPHGPPGERGLPGPQGPNGFPGPKGPLGPPGK | ||||||
Compositional bias | 874-900 | Pro residues | ||||
Sequence: GERGLPGPQGPNGFPGPKGPLGPPGKD | ||||||
Domain | 1099-1156 | Collagen-like 6 | ||||
Sequence: GNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIG | ||||||
Domain | 1157-1172 | Collagen-like 7 | ||||
Sequence: LQGLPGPSGEKGETGD | ||||||
Compositional bias | 1175-1189 | Pro residues | ||||
Sequence: PMGPPGPPGPRGPAG | ||||||
Domain | 1441-1499 | Collagen-like 8 | ||||
Sequence: GQKGEMGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPGGPKGEKGVQGPPGHPGPPGE | ||||||
Domain | 1541-1735 | Fibrillar collagen NC1 | ||||
Sequence: EEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFM |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 9 isoforms produced by Alternative splicing. Isoforms lack exons 6, 7 or 8 or a combination of these exons. Experimental confirmation may be lacking for some isoforms.
P13942-1
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
- Length1,736
- Mass (Da)171,791
- Last updated2012-01-25 v5
- ChecksumD687B7AAD6A7774C
P13942-2
- Name2
- Differences from canonical
- 267-292: Missing
P13942-3
- Name3
- Differences from canonical
- 293-313: Missing
P13942-4
- Name4
- Differences from canonical
- 314-373: Missing
P13942-5
- Name5
P13942-6
- Name6
P13942-7
- Name7
P13942-8
- Name8
P13942-9
- Name9
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2AAS7 | A2AAS7_HUMAN | COL11A2 | 624 | ||
H0YIS1 | H0YIS1_HUMAN | COL11A2 | 435 | ||
A0A140T9X7 | A0A140T9X7_HUMAN | COL11A2 | 624 | ||
A0A140T9W8 | A0A140T9W8_HUMAN | COL11A2 | 597 | ||
A0A140T9N0 | A0A140T9N0_HUMAN | COL11A2 | 263 | ||
A0A140T9N1 | A0A140T9N1_HUMAN | COL11A2 | 1650 | ||
A0A140T9I7 | A0A140T9I7_HUMAN | COL11A2 | 1623 | ||
A0A140T9A1 | A0A140T9A1_HUMAN | COL11A2 | 290 | ||
Q4VXY6 | Q4VXY6_HUMAN | COL11A2 | 1650 | ||
A0A140TA54 | A0A140TA54_HUMAN | COL11A2 | 1629 | ||
A0A140TA43 | A0A140TA43_HUMAN | COL11A2 | 1736 | ||
A0A0G2JL35 | A0A0G2JL35_HUMAN | COL11A2 | 1736 | ||
A0A0G2JL78 | A0A0G2JL78_HUMAN | COL11A2 | 1629 | ||
A0A0G2JI07 | A0A0G2JI07_HUMAN | COL11A2 | 624 | ||
A0A0C4DFS1 | A0A0C4DFS1_HUMAN | COL11A2 | 1736 | ||
A0A0G2JHD9 | A0A0G2JHD9_HUMAN | COL11A2 | 333 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 1; AAC50213/AAC50214/AAC50215 | ||||
Sequence: C → G | ||||||
Sequence conflict | 85 | in Ref. 5; AAC17464 and 6; AAA35498 | ||||
Sequence: S → P | ||||||
Sequence conflict | 97 | in Ref. 5; AAC17464 and 6; AAA35498 | ||||
Sequence: Q → R | ||||||
Compositional bias | 233-271 | Polar residues | ||||
Sequence: RERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESL | ||||||
Alternative sequence | VSP_043432 | 267-290 | in isoform 9 | |||
Sequence: PTESLYYDYEPPYYDVMTTGTTPD → VRELGEPPSAAHPREGRHPGISPP | ||||||
Alternative sequence | VSP_001167 | 267-292 | in isoform 2, isoform 5, isoform 6 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043433 | 291-1736 | in isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001168 | 293-313 | in isoform 3, isoform 5, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001169 | 314-373 | in isoform 4, isoform 6, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 530-531 | in Ref. 1; AAC50213/AAC50214/AAC50215, 5; AAC17464 and 6; AAA35498 | ||||
Sequence: PP → SL | ||||||
Sequence conflict | 542 | in Ref. 6; AAA35498 | ||||
Sequence: A → P | ||||||
Sequence conflict | 548-549 | in Ref. 6; AAA35498 | ||||
Sequence: MP → TL | ||||||
Sequence conflict | 578-579 | in Ref. 6; AAA35498 | ||||
Sequence: AQ → PR | ||||||
Sequence conflict | 704-705 | in Ref. 6; AAA35498 | ||||
Sequence: NQ → KP | ||||||
Sequence conflict | 720 | in Ref. 6; AAA35498 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 726 | in Ref. 6; AAA35498 | ||||
Sequence: D → N | ||||||
Compositional bias | 727-744 | Basic and acidic residues | ||||
Sequence: GIRGLKGHKGEKGEDGFP | ||||||
Sequence conflict | 843-846 | in Ref. 7; AAA52034 | ||||
Sequence: TGPR → HGST | ||||||
Compositional bias | 874-900 | Pro residues | ||||
Sequence: GERGLPGPQGPNGFPGPKGPLGPPGKD | ||||||
Sequence conflict | 882-884 | in Ref. 7; AAA52034 | ||||
Sequence: QGP → SGS | ||||||
Sequence conflict | 1031-1032 | in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034 | ||||
Sequence: PP → RQ | ||||||
Sequence conflict | 1091 | in Ref. 7; AAA52034 | ||||
Sequence: D → V | ||||||
Sequence conflict | 1124 | in Ref. 7; AAA52034 | ||||
Sequence: A → R | ||||||
Sequence conflict | 1127-1133 | in Ref. 7; AAA52034 | ||||
Sequence: EPGARGP → GAGGLGT | ||||||
Compositional bias | 1175-1189 | Pro residues | ||||
Sequence: PMGPPGPPGPRGPAG | ||||||
Sequence conflict | 1253 | in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034 | ||||
Sequence: P → A | ||||||
Sequence conflict | 1257 | in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034 | ||||
Sequence: T → Q | ||||||
Sequence conflict | 1552 | in Ref. 7; AAA52034 | ||||
Sequence: E → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U32169 EMBL· GenBank· DDBJ | AAC50213.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U32169 EMBL· GenBank· DDBJ | AAC50214.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U32169 EMBL· GenBank· DDBJ | AAC50215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL031228 EMBL· GenBank· DDBJ | CAA20240.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL645940 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL662824 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL844527 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL845446 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR759733 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR936877 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX03676.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC053886 EMBL· GenBank· DDBJ | AAH53886.1 EMBL· GenBank· DDBJ | mRNA | ||
U41069 EMBL· GenBank· DDBJ | AAC17464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U41065 EMBL· GenBank· DDBJ | AAC17464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U41066 EMBL· GenBank· DDBJ | AAC17464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U41067 EMBL· GenBank· DDBJ | AAC17464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L18987 EMBL· GenBank· DDBJ | AAA35498.1 EMBL· GenBank· DDBJ | mRNA | ||
J04974 EMBL· GenBank· DDBJ | AAA52034.1 EMBL· GenBank· DDBJ | mRNA |