Q13753 · LAMC2_HUMAN
- ProteinLaminin subunit gamma-2
- GeneLAMC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1193 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.
Miscellaneous
Binds heparin.
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 | cell cortex | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | laminin-2 complex | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | heparin binding | |
Biological Process | cell adhesion | |
Biological Process | epidermis development | |
Biological Process | positive regulation of cell migration | |
Biological Process | positive regulation of cell population proliferation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLaminin subunit gamma-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13753
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Major component.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epidermolysis bullosa, junctional 3A, intermediate (JEB3A)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB3A is an autosomal recessive, intermediate form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. In intermediate forms of junctional epidermolysis bullosa, blistering does not lead to the formation of chronic granulation tissue and does not affect the lifespan of affected individuals. Nail dystrophy and dental enamel defects are present. Scarring or non-scarring alopecia and diffuse hair loss may occur.
- See alsoMIM:619785
Epidermolysis bullosa, junctional 3B, severe (JEB3B)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB3B is an autosomal recessive form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. It belongs to the severe spectrum of junctional epidermolysis bullosa (previously known as generalized severe or Herlitz type), characterized by onset of blistering over large regions of the body at birth or in early infancy. Blistering also affects the mucous membranes, such as the moist lining of the mouth and digestive tract, which can make it difficult to eat and digest food. The extensive blistering leads to scarring and the formation of red, bumpy patches called granulation tissue. Other complications can include fusion of the fingers and toes, abnormalities of the fingernails and toenails, joint deformities, dental enamel defects, and alopecia. Severe, junctional forms are associated with death in the first 6 to 24 months of life.
- See alsoMIM:619786
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050081 | 111 | in dbSNP:rs12065473 | |||
Sequence: A → P | ||||||
Natural variant | VAR_050082 | 115 | in dbSNP:rs17481405 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_050083 | 124 | in dbSNP:rs11586699 | |||
Sequence: T → M | ||||||
Natural variant | VAR_050084 | 136 | in dbSNP:rs12037099 | |||
Sequence: D → V | ||||||
Natural variant | VAR_022017 | 247 | in dbSNP:rs2296306 | |||
Sequence: D → E | ||||||
Natural variant | VAR_050085 | 608 | in dbSNP:rs4373715 | |||
Sequence: S → I | ||||||
Natural variant | VAR_020304 | 733 | in dbSNP:rs2296303 | |||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,436 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
Protein family/group databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MPALWLGCCLCFSLLLPAARA | ||||||
Chain | PRO_0000017077 | 22-1193 | Laminin subunit gamma-2 | |||
Sequence: TSRREVCDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLPCNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQDQRLLDSKCDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQCFCYGHSASCRSSAEYSVHKITSTFHQDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQCICPVGYKGQFCQDCASGYKRDSARLGPFGTCIPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSDGTCVCKPGFGGPNCEHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ | ||||||
Disulfide bond | 28↔37 | |||||
Sequence: CDCNGKSRQC | ||||||
Disulfide bond | 30↔53 | |||||
Sequence: CNGKSRQCIFDRELHRQTGNGFRC | ||||||
Disulfide bond | 56↔65 | |||||
Sequence: CNDNTDGIHC | ||||||
Disulfide bond | 68↔81 | |||||
Sequence: CKNGFYRHRERDRC | ||||||
Disulfide bond | 84↔96 | |||||
Sequence: CNCNSKGSLSARC | ||||||
Disulfide bond | 86↔102 | |||||
Sequence: CNSKGSLSARCDNSGRC | ||||||
Disulfide bond | 104↔113 | |||||
Sequence: CKPGVTGARC | ||||||
Disulfide bond | 116↔128 | |||||
Sequence: CLPGFHMLTDAGC | ||||||
Disulfide bond | 139↔150 | |||||
Sequence: CDCDPAGIAGPC | ||||||
Disulfide bond | 141↔155 | |||||
Sequence: CDPAGIAGPCDAGRC | ||||||
Disulfide bond | 157↔166 | |||||
Sequence: CKPAVTGERC | ||||||
Disulfide bond | 169↔184 | |||||
Sequence: CRSGYYNLDGGNPEGC | ||||||
Glycosylation | 342 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 462↔470 | |||||
Sequence: CPCHNGFSC | ||||||
Disulfide bond | 464↔481 | |||||
Sequence: CHNGFSCSVMPETEEVVC | ||||||
Disulfide bond | 484↔493 | |||||
Sequence: CPPGVTGARC | ||||||
Disulfide bond | 496↔514 | |||||
Sequence: CADGYFGDPFGEHGPVRPC | ||||||
Disulfide bond | 517↔531 | |||||
Sequence: CQCNNNVDPSASGNC | ||||||
Disulfide bond | 519↔538 | |||||
Sequence: CNNNVDPSASGNCDRLTGRC | ||||||
Disulfide bond | 541↔550 | |||||
Sequence: CIHNTAGIYC | ||||||
Disulfide bond | 553↔570 | |||||
Sequence: CKAGYFGDPLAPNPADKC | ||||||
Disulfide bond | 573↔585 | |||||
Sequence: CNCNPMGSEPVGC | ||||||
Disulfide bond | 575↔591 | |||||
Sequence: CNPMGSEPVGCRSDGTC | ||||||
Disulfide bond | 593↔602 | |||||
Sequence: CKPGFGGPNC | ||||||
Disulfide bond | 609 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 612 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 803 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Glycosylation | 805 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Glycosylation | 942 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1033 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1184 | Interchain | ||||
Sequence: C |
Post-translational modification
O-glycosylated; contains chondroitin sulfate (CS). CS attachment is on either Ser-803 or Ser-805.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-83 | Laminin EGF-like 1 | ||||
Sequence: CDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLP | ||||||
Domain | 84-130 | Laminin EGF-like 2 | ||||
Sequence: CNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQ | ||||||
Domain | 139-186 | Laminin EGF-like 3 | ||||
Sequence: CDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQ | ||||||
Domain | 187-196 | Laminin EGF-like 4; first part | ||||
Sequence: CFCYGHSASC | ||||||
Domain | 213-381 | Laminin IV type A | ||||
Sequence: QDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQ | ||||||
Domain | 382-415 | Laminin EGF-like 4; second part | ||||
Sequence: CICPVGYKGQFCQDCASGYKRDSARLGPFGTCIP | ||||||
Domain | 416-461 | Laminin EGF-like 5 | ||||
Sequence: CNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKP | ||||||
Domain | 462-516 | Laminin EGF-like 6 | ||||
Sequence: CPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQP | ||||||
Domain | 517-572 | Laminin EGF-like 7 | ||||
Sequence: CQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRA | ||||||
Domain | 573-602 | Laminin EGF-like 8; truncated | ||||
Sequence: CNCNPMGSEPVGCRSDGTCVCKPGFGGPNC | ||||||
Region | 603-1193 | Domain II and I | ||||
Sequence: EHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ | ||||||
Coiled coil | 611-718 | |||||
Sequence: ACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRD | ||||||
Coiled coil | 811-1076 | |||||
Sequence: AVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQM | ||||||
Coiled coil | 1117-1193 | |||||
Sequence: EEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ |
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain IV is globular.
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.
Q13753-1
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.
- NameLong
- Length1,193
- Mass (Da)130,976
- Last updated2006-03-07 v2
- Checksum0BBE1A56516C5C9A
Q13753-2
- NameShort
- Differences from canonical
- 1110-1193: DQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ → GM
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 2; CAA52108 | ||||
Sequence: F → L | ||||||
Sequence conflict | 473 | in Ref. 1; CAA78728/CAA78729 | ||||
Sequence: M → I | ||||||
Sequence conflict | 521 | in Ref. 1; CAA78728/CAA78729 | ||||
Sequence: N → S | ||||||
Sequence conflict | 857 | in Ref. 1; CAA78728/CAA78729 | ||||
Sequence: R → P | ||||||
Sequence conflict | 883 | in Ref. 3; AAC50457/AAC50456 | ||||
Sequence: S → T | ||||||
Alternative sequence | VSP_003040 | 1110-1193 | in isoform Short | |||
Sequence: DQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ → GM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z15008 EMBL· GenBank· DDBJ | CAA78728.1 EMBL· GenBank· DDBJ | mRNA | ||
Z15009 EMBL· GenBank· DDBJ | CAA78729.1 EMBL· GenBank· DDBJ | mRNA | ||
X73902 EMBL· GenBank· DDBJ | CAA52108.1 EMBL· GenBank· DDBJ | mRNA | ||
U31201 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31178 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31179 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31180 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31181 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31182 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31183 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31184 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31186 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31187 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31188 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31189 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31190 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31191 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31192 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31193 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31194 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31195 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31196 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31197 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31198 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31199 EMBL· GenBank· DDBJ | AAC50457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31200 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31178 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31179 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31180 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31181 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31182 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31183 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31184 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31186 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31187 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31188 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31189 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31190 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31191 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31192 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31193 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31194 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31195 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31196 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31197 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U31198 EMBL· GenBank· DDBJ | AAC50456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL354953 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471067 EMBL· GenBank· DDBJ | EAW91146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC112286 EMBL· GenBank· DDBJ | AAI12287.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113378 EMBL· GenBank· DDBJ | AAI13379.1 EMBL· GenBank· DDBJ | mRNA |