O94813 · SLIT2_HUMAN
- ProteinSlit homolog 2 protein
- GeneSLIT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1529 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal cord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal cord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 1121-1122 | Cleavage | ||||
Sequence: RT |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSlit homolog 2 protein
- Short namesSlit-2
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94813
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_018098 | 636 | ||||
Sequence: S → P | ||||||
Natural variant | VAR_018099 | 1277 | in dbSNP:rs771375896 | |||
Sequence: S → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,759 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MRGVGWQMLSLSLGLVLAILNKVAPQACPA | ||||||
Chain | PRO_0000007726 | 31-1121 | Slit homolog 2 protein N-product | |||
Sequence: QCSCSGSTVDCHGLALRSVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRVLQLMENKISTIERGAFQDLKELERLRLNRNHLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSGHQSFMAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNTIKVIPPGAFSPYKKLRRIDLSNNQISELAPDAFQGLRSLNSLVLYGNKITELPKSLFEGLFSLQLLLLNANKINCLRVDAFQDLHNLNLLSLYDNKLQTIAKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYRSKLSGDCFADLACPEKCRCEGTTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPTECTCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNSDPVDFYRCTCPYGFKGQDCDVPIHACISNPCKHGGTCHLKEGEEDGFWCICADGFEGENCEVNVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQDLNPCQHDSKCILTPKGFKCDCTPGYVGEHCDIDFDDCQDNKCKNGAHCTDAVNGYTCICPEGYSGLFCEFSPPMVLPR | ||||||
Chain | PRO_0000007725 | 31-1529 | Slit homolog 2 protein | |||
Sequence: QCSCSGSTVDCHGLALRSVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRVLQLMENKISTIERGAFQDLKELERLRLNRNHLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSGHQSFMAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNTIKVIPPGAFSPYKKLRRIDLSNNQISELAPDAFQGLRSLNSLVLYGNKITELPKSLFEGLFSLQLLLLNANKINCLRVDAFQDLHNLNLLSLYDNKLQTIAKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYRSKLSGDCFADLACPEKCRCEGTTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPTECTCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNSDPVDFYRCTCPYGFKGQDCDVPIHACISNPCKHGGTCHLKEGEEDGFWCICADGFEGENCEVNVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQDLNPCQHDSKCILTPKGFKCDCTPGYVGEHCDIDFDDCQDNKCKNGAHCTDAVNGYTCICPEGYSGLFCEFSPPMVLPRTSPCDNFDCQNGAQCIVRINEPICQCLPGYQGEKCEKLVSVNFINKESYLQIPSAKVRPQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPGKSNVASLRQAPGQNGTSFHGCIRNLYINSELQDFQKVPMQTGILPGCEPCHKKVCAHGTCQPSSQAGFTCECQEGWMGPLCDQRTNDPCLGNKCVHGTCLPINAFSYSCKCLEGHGGVLCDEEEDLFNPCQAIKCKHGKCRLSGLGQPYCECSSGYTGDSCDREISCRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGCTRCVS | ||||||
Glycosylation | 66 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 277↔286 | |||||
Sequence: CTCSNNIVDC | ||||||
Disulfide bond | 434↔457 | |||||
Sequence: CDCHLKWLADYLHTNPIETSGARC | ||||||
Disulfide bond | 436↔478 | |||||
Sequence: CHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRC | ||||||
Disulfide bond | 506↔512 | |||||
Sequence: CPEKCRC | ||||||
Disulfide bond | 510↔519 | |||||
Sequence: CRCEGTTVDC | ||||||
Glycosylation | 564 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 623 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 668↔691 | |||||
Sequence: CNCYLAWLGEWLRKKRIVTGNPRC | ||||||
Disulfide bond | 670↔712 | |||||
Sequence: CYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTC | ||||||
Disulfide bond | 727↔733 | |||||
Sequence: CPTECTC | ||||||
Disulfide bond | 731↔740 | |||||
Sequence: CTCLDTVVRC | ||||||
Glycosylation | 794 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 799 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 863↔886 | |||||
Sequence: CDCNMQWLSDWVKSEYKEPGIARC | ||||||
Disulfide bond | 865↔907 | |||||
Sequence: CNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTC | ||||||
Disulfide bond | 922↔933 | |||||
Sequence: CLSNPCKNDGTC | ||||||
Disulfide bond | 927↔943 | |||||
Sequence: CKNDGTCNSDPVDFYRC | ||||||
Disulfide bond | 945↔954 | |||||
Sequence: CPYGFKGQDC | ||||||
Disulfide bond | 961↔972 | |||||
Sequence: CISNPCKHGGTC | ||||||
Disulfide bond | 966↔984 | |||||
Sequence: CKHGGTCHLKEGEEDGFWC | ||||||
Disulfide bond | 986↔995 | |||||
Sequence: CADGFEGENC | ||||||
Disulfide bond | 1002↔1013 | |||||
Sequence: CEDNDCENNSTC | ||||||
Disulfide bond | 1007↔1022 | |||||
Sequence: CENNSTCVDGINNYTC | ||||||
Glycosylation | 1009 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1010 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1019 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1024↔1033 | |||||
Sequence: CPPEYTGELC | ||||||
Disulfide bond | 1040↔1053 | |||||
Sequence: CAQDLNPCQHDSKC | ||||||
Disulfide bond | 1047↔1062 | |||||
Sequence: CQHDSKCILTPKGFKC | ||||||
Disulfide bond | 1064↔1073 | |||||
Sequence: CTPGYVGEHC | ||||||
Disulfide bond | 1080↔1091 | |||||
Sequence: CQDNKCKNGAHC | ||||||
Disulfide bond | 1085↔1100 | |||||
Sequence: CKNGAHCTDAVNGYTC | ||||||
Disulfide bond | 1102↔1111 | |||||
Sequence: CPEGYSGLFC | ||||||
Chain | PRO_0000007727 | 1122-1529 | Slit homolog 2 protein C-product | |||
Sequence: TSPCDNFDCQNGAQCIVRINEPICQCLPGYQGEKCEKLVSVNFINKESYLQIPSAKVRPQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPGKSNVASLRQAPGQNGTSFHGCIRNLYINSELQDFQKVPMQTGILPGCEPCHKKVCAHGTCQPSSQAGFTCECQEGWMGPLCDQRTNDPCLGNKCVHGTCLPINAFSYSCKCLEGHGGVLCDEEEDLFNPCQAIKCKHGKCRLSGLGQPYCECSSGYTGDSCDREISCRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGCTRCVS | ||||||
Disulfide bond | 1125↔1136 | |||||
Sequence: CDNFDCQNGAQC | ||||||
Disulfide bond | 1130↔1145 | |||||
Sequence: CQNGAQCIVRINEPIC | ||||||
Disulfide bond | 1147↔1156 | |||||
Sequence: CLPGYQGEKC | ||||||
Glycosylation | 1183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1300 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1307↔1333 | |||||
Sequence: CIRNLYINSELQDFQKVPMQTGILPGC | ||||||
Disulfide bond | 1336↔1346 | |||||
Sequence: CHKKVCAHGTC | ||||||
Disulfide bond | 1341↔1356 | |||||
Sequence: CAHGTCQPSSQAGFTC | ||||||
Disulfide bond | 1358↔1367 | |||||
Sequence: CQEGWMGPLC | ||||||
Disulfide bond | 1375↔1385 | |||||
Sequence: CLGNKCVHGTC | ||||||
Disulfide bond | 1380↔1395 | |||||
Sequence: CVHGTCLPINAFSYSC | ||||||
Disulfide bond | 1397↔1406 | |||||
Sequence: CLEGHGGVLC | ||||||
Disulfide bond | 1416↔1426 | |||||
Sequence: CQAIKCKHGKC | ||||||
Disulfide bond | 1421↔1436 | |||||
Sequence: CKHGKCRLSGLGQPYC | ||||||
Disulfide bond | 1438↔1447 | |||||
Sequence: CSSGYTGDSC | ||||||
Disulfide bond | 1453↔1492 | |||||
Sequence: CRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCC | ||||||
Disulfide bond | 1471↔1506 | |||||
Sequence: CQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFEC | ||||||
Disulfide bond | 1482↔1522 | |||||
Sequence: CRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKC | ||||||
Disulfide bond | 1486↔1524 | |||||
Sequence: CAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GREM1 (By similarity).
Homodimer. Binds ROBO1 and ROBO2 with high affinity
Homodimer. Binds ROBO1 and ROBO2 with high affinity
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94813 | ROBO1 Q9Y6N7 | 2 | EBI-1236865, EBI-399762 | |
BINARY | O94813 | SLIT2 O94813 | 2 | EBI-1236865, EBI-1236865 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-55 | LRRNT | ||||
Sequence: QCSCSGSTVDCHGLALRSVPRNIPR | ||||||
Repeat | 56-77 | LRR 1 | ||||
Sequence: NTERLDLNGNNITRITKTDFAG | ||||||
Repeat | 80-101 | LRR 2 | ||||
Sequence: HLRVLQLMENKISTIERGAFQD | ||||||
Repeat | 104-125 | LRR 3 | ||||
Sequence: ELERLRLNRNHLQLFPELLFLG | ||||||
Repeat | 128-149 | LRR 4 | ||||
Sequence: KLYRLDLSENQIQAIPRKAFRG | ||||||
Repeat | 152-173 | LRR 5 | ||||
Sequence: DIKNLQLDYNQISCIEDGAFRA | ||||||
Repeat | 176-197 | LRR 6 | ||||
Sequence: DLEVLTLNNNNITRLSVASFNH | ||||||
Domain | 209-259 | LRRCT 1 | ||||
Sequence: NNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSG | ||||||
Domain | 264-300 | LRRNT 2 | ||||
Sequence: MAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPE | ||||||
Repeat | 301-322 | LRR 7 | ||||
Sequence: TITEIRLEQNTIKVIPPGAFSP | ||||||
Repeat | 325-346 | LRR 8 | ||||
Sequence: KLRRIDLSNNQISELAPDAFQG | ||||||
Repeat | 349-370 | LRR 9 | ||||
Sequence: SLNSLVLYGNKITELPKSLFEG | ||||||
Repeat | 373-394 | LRR 10 | ||||
Sequence: SLQLLLLNANKINCLRVDAFQD | ||||||
Repeat | 397-418 | LRR 11 | ||||
Sequence: NLNLLSLYDNKLQTIAKGTFSP | ||||||
Domain | 430-480 | LRRCT 2 | ||||
Sequence: NPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSA | ||||||
Domain | 497-533 | LRRNT 3 | ||||
Sequence: SGDCFADLACPEKCRCEGTTVDCSNQKLNKIPEHIPQ | ||||||
Repeat | 534-555 | LRR 12 | ||||
Sequence: YTAELRLNNNEFTVLEATGIFK | ||||||
Repeat | 559-580 | LRR 13 | ||||
Sequence: QLRKINFSNNKITDIEEGAFEG | ||||||
Repeat | 583-604 | LRR 14 | ||||
Sequence: GVNEILLTSNRLENVQHKMFKG | ||||||
Repeat | 607-628 | LRR 15 | ||||
Sequence: SLKTLMLRSNRITCVGNDSFIG | ||||||
Repeat | 631-652 | LRR 16 | ||||
Sequence: SVRLLSLYDNQITTVAPGAFDT | ||||||
Domain | 664-714 | LRRCT 3 | ||||
Sequence: NPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDD | ||||||
Domain | 718-754 | LRRNT 4 | ||||
Sequence: DNSCSPLSRCPTECTCLDTVVRCSNKGLKVLPKGIPR | ||||||
Repeat | 755-777 | LRR 17 | ||||
Sequence: DVTELYLDGNQFTLVPKELSNYK | ||||||
Repeat | 778-799 | LRR 18 | ||||
Sequence: HLTLIDLSNNRISTLSNQSFSN | ||||||
Repeat | 802-823 | LRR 19 | ||||
Sequence: QLLTLILSYNRLRCIPPRTFDG | ||||||
Repeat | 826-847 | LRR 20 | ||||
Sequence: SLRLLSLHGNDISVVPEGAFND | ||||||
Domain | 859-909 | LRRCT 4 | ||||
Sequence: NPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQG | ||||||
Domain | 918-955 | EGF-like 1 | ||||
Sequence: KCNPCLSNPCKNDGTCNSDPVDFYRCTCPYGFKGQDCD | ||||||
Domain | 957-996 | EGF-like 2 | ||||
Sequence: PIHACISNPCKHGGTCHLKEGEEDGFWCICADGFEGENCE | ||||||
Domain | 998-1034 | EGF-like 3; calcium-binding | ||||
Sequence: NVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCE | ||||||
Domain | 1036-1074 | EGF-like 4 | ||||
Sequence: KLDFCAQDLNPCQHDSKCILTPKGFKCDCTPGYVGEHCD | ||||||
Domain | 1076-1112 | EGF-like 5; calcium-binding | ||||
Sequence: DFDDCQDNKCKNGAHCTDAVNGYTCICPEGYSGLFCE | ||||||
Domain | 1121-1157 | EGF-like 6 | ||||
Sequence: RTSPCDNFDCQNGAQCIVRINEPICQCLPGYQGEKCE | ||||||
Domain | 1160-1333 | Laminin G-like | ||||
Sequence: VSVNFINKESYLQIPSAKVRPQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPGKSNVASLRQAPGQNGTSFHGCIRNLYINSELQDFQKVPMQTGILPGC | ||||||
Domain | 1332-1368 | EGF-like 7 | ||||
Sequence: GCEPCHKKVCAHGTCQPSSQAGFTCECQEGWMGPLCD | ||||||
Domain | 1453-1528 | CTCK | ||||
Sequence: CRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGCTRCV |
Domain
The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro.
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 3 isoforms produced by Alternative splicing.
O94813-1
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
- Length1,529
- Mass (Da)169,870
- Last updated1999-05-01 v1
- Checksum5D19CC5E7FD461BA
O94813-2
- Name2
O94813-3
- Name3
- Differences from canonical
- 480-487: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 226 | in Ref. 2; AAD25539 | ||||
Sequence: Q → K | ||||||
Alternative sequence | VSP_050035 | 258 | in isoform 2 | |||
Sequence: S → SDEEE | ||||||
Alternative sequence | VSP_050036 | 480-487 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 607-610 | in Ref. 3; AAD04309 | ||||
Sequence: SLKT → KPQN | ||||||
Sequence conflict | 634 | in Ref. 3; AAD04309 | ||||
Sequence: L → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB017168 EMBL· GenBank· DDBJ | BAA35185.1 EMBL· GenBank· DDBJ | mRNA | ||
AF055585 EMBL· GenBank· DDBJ | AAD04309.1 EMBL· GenBank· DDBJ | mRNA | ||
AF133270 EMBL· GenBank· DDBJ | AAD25539.1 EMBL· GenBank· DDBJ | mRNA | ||
AC021118 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092577 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC096718 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108011 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471069 EMBL· GenBank· DDBJ | EAW92793.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC117190 EMBL· GenBank· DDBJ | AAI17191.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143978 EMBL· GenBank· DDBJ | AAI43979.1 EMBL· GenBank· DDBJ | mRNA |