Q6WKZ8 · UBR2_MOUSE
- ProteinE3 ubiquitin-protein ligase UBR2
- GeneUbr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1755 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed:14585983, PubMed:19008229, PubMed:30872531, PubMed:31268597).
Recognizes and binds to proteins bearing specific N-terminal residues (N-degrons) that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:14585983, PubMed:19008229, PubMed:30872531, PubMed:31268597).
Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:19008229).
Does not ubiquitinate proteins that are acetylated at the N-terminus (By similarity).
In contrast, it strongly binds methylated N-degrons (By similarity).
Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A (PubMed:14585983, PubMed:20080676).
Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity).
Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (PubMed:28708824).
Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization (PubMed:28806172).
Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1B following NLRP1B activation by pathogens and other damage-associated signals: ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1B, which polymerizes and forms the NLRP1B inflammasome followed by host cell pyroptosis (PubMed:30872531, PubMed:31268597).
Plays a role in T-cell receptor signaling by inducing 'Lys-63'-linked ubiquitination of lymphocyte cell-specific kinase LCK (PubMed:38225265).
This activity is regulated by DUSP22, which induces 'Lys-48'-linked ubiquitination of UBR2, leading to its proteasomal degradation by SCF E3 ubiquitin-protein ligase complex (By similarity).
Recognizes and binds to proteins bearing specific N-terminal residues (N-degrons) that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:14585983, PubMed:19008229, PubMed:30872531, PubMed:31268597).
Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:19008229).
Does not ubiquitinate proteins that are acetylated at the N-terminus (By similarity).
In contrast, it strongly binds methylated N-degrons (By similarity).
Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A (PubMed:14585983, PubMed:20080676).
Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity).
Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (PubMed:28708824).
Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization (PubMed:28806172).
Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1B following NLRP1B activation by pathogens and other damage-associated signals: ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1B, which polymerizes and forms the NLRP1B inflammasome followed by host cell pyroptosis (PubMed:30872531, PubMed:31268597).
Plays a role in T-cell receptor signaling by inducing 'Lys-63'-linked ubiquitination of lymphocyte cell-specific kinase LCK (PubMed:38225265).
This activity is regulated by DUSP22, which induces 'Lys-48'-linked ubiquitination of UBR2, leading to its proteasomal degradation by SCF E3 ubiquitin-protein ligase complex (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 99 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 112 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 115 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 127 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 127 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 133 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 136 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 148 | L-arginine residue (UniProtKB | ChEBI) of a peptide (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 149 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 150 | L-arginine residue (UniProtKB | ChEBI) of a peptide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 151 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 153 | L-arginine residue (UniProtKB | ChEBI) of a peptide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 163 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 166 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1108 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1111 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1168 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1170 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1173 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1176 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1210 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1213 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | histone H2A ubiquitin ligase activity | |
Molecular Function | L-leucine binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to L-leucine | |
Biological Process | heterochromatin formation | |
Biological Process | male meiosis I | |
Biological Process | male meiotic nuclear division | |
Biological Process | negative regulation of TOR signaling | |
Biological Process | protein ubiquitination | |
Biological Process | reciprocal meiotic recombination | |
Biological Process | retrotransposon silencing | |
Biological Process | spermatogenesis | |
Biological Process | ubiquitin-dependent protein catabolic process | |
Biological Process | ubiquitin-dependent protein catabolic process via the N-end rule pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase UBR2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6WKZ8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with chromatin during meiosis.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Male mice are viable but not fertile, due to massive apoptosis of spermatocytes (PubMed:38225265).
They have a reduction of testis weight of 68% and no detectable sperm in their epididymis. The seminiferous tubules contain reduced numbers of post-meiotic round, elongated spermatids and accumulation of pyknotic and zygotene-like nuclei. Female mice show severe prenatal lethality, but the rare survivors are fertile. Fibroblast cells display spontaneous chromosome instability and fragility (PubMed:14585983, PubMed:16488448, PubMed:28708824).
UBR1 and UBR2 double knockout embryos die at mid-gestation, with defects in neurogenesis and cardiovascular development. These defects include reduced proliferation as well as precocious migration and differentiation of neural progenitor cells (PubMed:16606826).
Decrease in T-cell receptor-stimulated cytokines production and Th1 and Th17 differentiation in T-cells (PubMed:38225265).
'Lys-63'-linked ubiquitination and phosphorylation of Lck are obliterated (PubMed:38225265).
They have a reduction of testis weight of 68% and no detectable sperm in their epididymis. The seminiferous tubules contain reduced numbers of post-meiotic round, elongated spermatids and accumulation of pyknotic and zygotene-like nuclei. Female mice show severe prenatal lethality, but the rare survivors are fertile. Fibroblast cells display spontaneous chromosome instability and fragility (PubMed:14585983, PubMed:16488448, PubMed:28708824).
UBR1 and UBR2 double knockout embryos die at mid-gestation, with defects in neurogenesis and cardiovascular development. These defects include reduced proliferation as well as precocious migration and differentiation of neural progenitor cells (PubMed:16606826).
Decrease in T-cell receptor-stimulated cytokines production and Th1 and Th17 differentiation in T-cells (PubMed:38225265).
'Lys-63'-linked ubiquitination and phosphorylation of Lck are obliterated (PubMed:38225265).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 81 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000056141 | 2-1755 | E3 ubiquitin-protein ligase UBR2 | |||
Sequence: ASEMEPEVQAIDRSLLECSAEEIAGRWLQATDLNREVYQHLAHCVPKIYCRGPNPFPQKEDTLAQHILLGPMEWYICAEDPALGFPKLEQANKPSHLCGRVFKVGEPTYSCRDCAVDPTCVLCMECFLGSIHRDHRYRMTTSGGGGFCDCGDTEAWKEGPYCQKHKLSSSEVVEEEDPLVHLSEDVIARTYNIFAIMFRYAVDILTWEKESELPEDLEVAEKSDTYYCMLFNDEVHTYEQVIYTLQKAVNCTQKEAIGFATTVDRDGRRSVRYGDFQYCDQAKTVIVRNTSRQTKPLKVQVMHSSVAAHQNFGLKALSWLGSVIGYSDGLRRILCQVGLQEGPDGENSSLVDRLMLNDSKLWKGARSVYHQLFMSSLLMDLKYKKLFALRFAKNYRQLQRDFMEDDHERAVSVTALSVQFFTAPTLARMLLTEENLMTVIIKAFMDHLKHRDAQGRFQFERYTALQAFKFRRVQSLILDLKYVLISKPTEWSDELRQKFLQGFDAFLELLKCMQGMDPITRQVGQHIEMEPEWEAAFTLQMKLTHVISMVQDWCALDEKVLIEAYKKCLAVLTQCHGGFTDGEQPITLSICGHSVETIRYCVSQEKVSIHLPISRLLAGLHVLLSKSEVAYKFPELLPLSELSPPMLIEHPLRCLVLCAQVHAGMWRRNGFSLVNQIYYYHNVKCRREMFDKDIVMLQTGVSMMDPNHFLMIMLSRFELYQLFSTPDYGKRFSSEVTHKDVVQQNNTLIEEMLYLIIMLVGERFNPGVGQVAATDEIKREIIHQLSIKPMAHSELVKSLPEDENKETGMESVIESVAHFKKPGLTGRGMYELKPECAKEFNLYFYHFSRAEQSKAEEAQRKLKRENKEDTALPPPALPPFCPLFASLVNILQCDVMLYIMGTILQWAVEHHGSAWSESMLQRVLHLIGMALQEEKHHLENAVEGHVQTFTFTQKISKPGDAPHNSPSILAMLETLQNAPSLEAHKDMIRWLLKMFNAIKKIRECSSSSPVAEAEGTIMEESSRDKDKAERKRKAEIARLRREKIMAQMSEMQRHFIDENKELFQQTLELDTSASATLDSSPPVSDAALTALGPAQTQVPEPRQFVTCILCQEEQEVTVGSRAMVLAAFVQRSTVLSKDRTKTIADPEKYDPLFMHPDLSCGTHTGSCGHVMHAHCWQRYFDSVQAKEQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIPLLLPPRSILSRRLNFSDQPDLAQWTRAVTQQIKVVQMLRRKHNAADTSSSEDTEAMNIIPIPEGFRPDFYPRNPYSDSIKEMLTTFGTAAYKVGLKVHPNEGDPRVPILCWGTCAYTIQSIERILSDEEKPVFGPLPCRLDDCLRSLTRFAAAHWTVALLPVVQGHFCKLFASLVPSDSYEDLPCILDIDMFHLLVGLVLAFPALQCQDFSGSSLATGDLHIFHLVTMAHIVQILLTSCTEENGMDQENPTGEEELAILSLHKTLHQYTGSALKEAPSGWHLWRSVRAAIMPFLKCSALFFHYLNGVPAPPDLQVSGTSHFEHLCNYLSLPTNLIHLFQENSDIMNSLIESWCQNSEVKRYLNGERGAISYPRGANKLIDLPEDYSSLINQASNFSCPKSGGDKSRAPTLCLVCGSLLCSQSYCCQAELEGEDVGACTAHTYSCGSGAGIFLRVRECQVLFLAGKTKGCFYSPPYLDDYGETDQGLRRGNPLHLCQERFRKIQKLWQQHSITEEIGHAQEANQTLVGIDWQHL | ||||||
Cross-link | 94 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 158 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 165 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 248 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 255 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 470 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 476 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 488 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 568 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 779 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 789 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1496 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1599 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1689 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 1694 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1697 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Dephosphorylated by DUSP22 at Ser-1694 and Tyr-1697, leading to subsequent ubiquitination and proteasomal degradation.
'Lys-48'-linked ubiquitinated at Lys-94, Lys-779 and Lys-1599 following DUSP22-mediated dephosphorylation of Ser-1694 and Tyr-1697 which promotes UBR2 interaction with the SCF(FBW1A) E3 ubiquitin-protein ligase complex.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in skeletal muscle. Also expressed in heart, kidney and testis. Expressed in acinar cells of the pancreas. In testes, expressed primarily in spermatocytes. Expressed in cerebellum (PubMed:28806172).
Induction
In models of cancer cachexia, induced specifically at the onset and during the progression of muscle wasting.
Gene expression databases
Interaction
Subunit
Interacts with UBE2B; promotes the UBE2B-H2A interaction and the ubiquitination of histone H2A by UBE2B and UBR2 (PubMed:14585983, PubMed:20080676).
Interacts with RECQL4 (By similarity).
Interacts with Tex19.1 and Tex19.2; does not lead to Tex19.1 degradation and stabilizes it (PubMed:21103378).
Interacts with L1RE1 (PubMed:28806172).
Interacts with CASP8 (By similarity).
Interacts with ATXN3 (By similarity).
Interacts with UBE2O (PubMed:31268597).
Interacts with RECQL4 (By similarity).
Interacts with Tex19.1 and Tex19.2; does not lead to Tex19.1 degradation and stabilizes it (PubMed:21103378).
Interacts with L1RE1 (PubMed:28806172).
Interacts with CASP8 (By similarity).
Interacts with ATXN3 (By similarity).
Interacts with UBE2O (PubMed:31268597).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 97-168 | UBR-type | ||||
Sequence: HLCGRVFKVGEPTYSCRDCAVDPTCVLCMECFLGSIHRDHRYRMTTSGGGGFCDCGDTEAWKEGPYCQKHKL | ||||||
Region | 1012-1033 | Disordered | ||||
Sequence: AEAEGTIMEESSRDKDKAERKR | ||||||
Compositional bias | 1018-1033 | Basic and acidic residues | ||||
Sequence: IMEESSRDKDKAERKR | ||||||
Coiled coil | 1019-1054 | |||||
Sequence: MEESSRDKDKAERKRKAEIARLRREKIMAQMSEMQR | ||||||
Zinc finger | 1108-1214 | RING-type; atypical | ||||
Sequence: CILCQEEQEVTVGSRAMVLAAFVQRSTVLSKDRTKTIADPEKYDPLFMHPDLSCGTHTGSCGHVMHAHCWQRYFDSVQAKEQRRQQRLRLHTSYDVENGEFLCPLCE |
Domain
The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif (By similarity).
The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons (By similarity).
It exhibits preference for arginine in the first position, and a lower preference for lysine and histidine (By similarity).
It binds N-degrons with a methylated arginine or lysine in the first position (By similarity).
The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons (By similarity).
It exhibits preference for arginine in the first position, and a lower preference for lysine and histidine (By similarity).
It binds N-degrons with a methylated arginine or lysine in the first position (By similarity).
Sequence similarities
Belongs to the E3 ubiquitin-protein ligase UBR1-like family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6WKZ8-1
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
- Length1,755
- Mass (Da)199,155
- Last updated2005-08-16 v2
- ChecksumE6D413D674FBBFDA
Q6WKZ8-2
- Name2
- Differences from canonical
- 397-426: RQLQRDFMEDDHERAVSVTALSVQFFTAPT → ERLQRDYVTDDHDREFSVADLSVQIFTVPS
Q6WKZ8-3
- Name3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A286YCB2 | A0A286YCB2_MOUSE | Ubr2 | 178 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_015172 | 1-197 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 59 | in Ref. 1; AAQ17202 | ||||
Sequence: Q → L | ||||||
Sequence conflict | 137 | in Ref. 1; AAQ17202 and 3; BAC65536 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 143 | in Ref. 1; AAQ17202 | ||||
Sequence: S → W | ||||||
Sequence conflict | 271 | in Ref. 2; AAL32102 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_015173 | 397-426 | in isoform 2 and isoform 3 | |||
Sequence: RQLQRDFMEDDHERAVSVTALSVQFFTAPT → ERLQRDYVTDDHDREFSVADLSVQIFTVPS | ||||||
Sequence conflict | 429-435 | in Ref. 1; AAQ17202 | ||||
Sequence: RMLLTEE → PNAPHRKK | ||||||
Sequence conflict | 656 | in Ref. 1; AAQ17202 | ||||
Sequence: L → P | ||||||
Sequence conflict | 979 | in Ref. 1; AAQ17202 | ||||
Sequence: A → S | ||||||
Compositional bias | 1018-1033 | Basic and acidic residues | ||||
Sequence: IMEESSRDKDKAERKR | ||||||
Sequence conflict | 1050 | in Ref. 5; BAC38864 | ||||
Sequence: S → F | ||||||
Sequence conflict | 1332 | in Ref. 1; AAQ17202 | ||||
Sequence: C → W | ||||||
Sequence conflict | 1619 | in Ref. 4; AAH26391 | ||||
Sequence: C → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY280958 EMBL· GenBank· DDBJ | AAQ17202.1 EMBL· GenBank· DDBJ | mRNA | ||
AY061885 EMBL· GenBank· DDBJ | AAL32102.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122254 EMBL· GenBank· DDBJ | BAC65536.3 EMBL· GenBank· DDBJ | Unassigned DNA | Sequence problems. | |
BC025617 EMBL· GenBank· DDBJ | AAH25617.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC026391 EMBL· GenBank· DDBJ | AAH26391.1 EMBL· GenBank· DDBJ | mRNA | ||
BC031403 EMBL· GenBank· DDBJ | AAH31403.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC075642 EMBL· GenBank· DDBJ | AAH75642.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083320 EMBL· GenBank· DDBJ | BAC38864.1 EMBL· GenBank· DDBJ | mRNA |