Q8TEP8 · CE192_HUMAN
- ProteinCentrosomal protein of 192 kDa
- GeneCEP192
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2537 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for mitotic centrosome maturation and bipolar spindle assembly (PubMed:17980596, PubMed:18207742, PubMed:25042804).
Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication (PubMed:17980596, PubMed:18207742, PubMed:25042804).
Centrosome-specific activating scaffold for AURKA and PLK1 (PubMed:25042804).
Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication (PubMed:17980596, PubMed:18207742, PubMed:25042804).
Centrosome-specific activating scaffold for AURKA and PLK1 (PubMed:25042804).
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 | centriole | |
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | pericentriolar material | |
Cellular Component | procentriole | |
Cellular Component | procentriole replication complex | |
Molecular Function | phosphatase binding | |
Molecular Function | protein kinase binding | |
Biological Process | centriole replication | |
Biological Process | centrosome-templated microtubule nucleation | |
Biological Process | mitotic spindle assembly | |
Biological Process | protein localization to centrosome | |
Biological Process | response to bacterium |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentrosomal protein of 192 kDa
- Short namesCep192; Cep192/SPD-2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TEP8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Pericentriolar location in mitotic centrosomes.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_037514 | 1053 | in dbSNP:rs10048340 | |||
Sequence: T → A | ||||||
Natural variant | VAR_050782 | 1109 | in dbSNP:rs11080623 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_037515 | 1365 | in dbSNP:rs2282542 | |||
Sequence: V → M | ||||||
Natural variant | VAR_050783 | 1544 | in dbSNP:rs7228940 | |||
Sequence: R → H | ||||||
Natural variant | VAR_050784 | 1552 | in dbSNP:rs578208 | |||
Sequence: S → P | ||||||
Natural variant | VAR_050785 | 1701 | in dbSNP:rs6505780 | |||
Sequence: L → F | ||||||
Natural variant | VAR_050786 | 2051 | in dbSNP:rs2027698 | |||
Sequence: S → N | ||||||
Natural variant | VAR_050787 | 2121 | in dbSNP:rs474337 | |||
Sequence: L → P | ||||||
Natural variant | VAR_050788 | 2271 | in dbSNP:rs3737379 | |||
Sequence: K → E | ||||||
Mutagenesis | 2313 | Increased presence on interphasic centrosomes, and decreased presence on mitotic centrosomes; no ubiquitination and unchanged levels in response to hypoxia. | ||||
Sequence: P → A | ||||||
Natural variant | VAR_050789 | 2449 | in dbSNP:rs1786263 | |||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,642 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000312495 | 1-2537 | UniProt | Centrosomal protein of 192 kDa | |||
Sequence: MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKRPSFGYFIRSPEKREPIALIRKSDVSRGNLEKEMAHLNHDLYSGDLNEQSQAQLSEGSITLQVEAVESTSQVDENDVTLTADKGKTEDTFFMSNKPQRYKDKLPDSGDSMLRISTIASAIAEASVNTDPSQLAAMIKALSNKTRDKTFQEDEKQKDYSHVRHFLPNDLEKSNGSNALDMEKYLKKTEVSRYESALENFSRASMSDTWDLSLPKEQTTQDIHPVDLSATSVSVRAPEENTAAIVYVENGESENQESFRTINSSNSVTNRENNSAVVDVKTCSIDNKLQDVGNDEKATSISTPSDSYSSVRNPRITSLCLLKDCEEIRDNRENQRQNECVSEISNSEKHVTFENHRIVSPKNSDLKNTSPEHGGRGSEDEQESFRPSTSPLSHSSPSEISGTSSSGCALESFGSAAQQQQPPCEQELSPLVCSPAGVSRLTYVSEPESSYPTTATDDALEDRKSDITSELSTTIIQGSPAALEERAMEKLREKVPFQNRGKGTLSSIIQNNSDTRKATETTSLSSKPEYVKPDFRWSKDPSSKSGNLLETSEVGWTSNPEELDPIRLALLGKSGLSCQVGSATSHPVSCQEPIDEDQRISPKDKSTAGREFSGQVSHQTTSENQCTPIPSSTVHSSVADMQNMPAAVHALLTQPSLSAAPFAQRYLGTLPSTGSTTLPQCHAGNATVCGFSGGLPYPAVAGEPVQNSVAVGICLGSNIGSGWMGTSSLCNPYSNTLNQNLLSTTKPFPVPSVGTNCGIEPWDSGVTSGLGSVRVPEELKLPHACCVGIASQTLLSVLNPTDRWLQVSIGVLSISVNGEKVDLSTYRCLVFKNKAIIRPHATEEIKVLFIPSSPGVFRCTFSVASWPCSTDAETIVQAEALASTVTLTAIAESPVIEVETEKKDVLDFGDLTYGGWKALPLKLINRTHATVPIRLIINANAVAWRCFTFSKESVRAPVEVAPCADVVTRLAGPSVVNHMMPASYDGQDPEFLMIWVLFHSPKKQISSSDILDSAEEFSAKVDIEVDSPNPTPVLRSVSLRARAGIARIHAPRDLQTMHFLAKVASSRKQHLPLKNAGNIEVYLDIKVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEACEERILKIFVQPFGPQYEVVLKGEVISSGSKPLSPGPCLDIPSILSNKQFLAWGGVPLGRTQLQKLALRNNSASTTQHLRLLIRGQDQDCFQLQNTFGSEQRLTSNCEIRIHPKEDIFISVLFAPTRLSCMLARLEIKQLGNRSQPGIKFTIPLSGYGGTSNLILEGVKKLSDSYMVTVNGLVPGKESKIVFSVRNTGSRAAFVKAVGFKDSQKKVLLDPKVLRIFPDKFVLKERTQENVTLIYNPSDRGINNKTATELSTVYLFGGDEISRQQYRRALLHKPEMIKQILPEHSVLQNINFVEAFQDELLVTEVYDLPQRPNDVQLFYGSMCKIILSVIGEFRDCISSREFLQPSSKASLESTSDLGASGKHGGNVSLDVLPVKGPQGSPLLSRAARPPLDQLASEEPWTVLPEHLILVAPSPCDMAKTGRFQIVNNSVRLLRFELCWPAHCLTVTPQHGCVAPESKLQILVSPNSSLSTKQSMFPWSGLIYIHCDDGQKKIVKVQIREDLTQVELLTRLTSKPFGILSPVSEPSVSHLVKPMTKPPSTKVEIRNKSITFPTTEPGETSESCLELENHGTTDVKWHLSSLAPPYVKGVDESGDVFRATYAAFRCSPISGLLESHGIQKVSITFLPRGRGDYAQFWDVECHPLKEPHMKHTLRFQLSGQSIEAENEPENACLSTDSLIKIDHLVKPRRQAVSEASARIPEQLDVTARGVYAPEDVYRFRPTSVGESRTLKVNLRNNSFITHSLKFLSPREPFYVKHSKYSLRAQHYINMPVQFKPKSAGKFEALLVIQTDEGKSIAIRLIGEALGKN | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 812 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 944 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 946 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1064 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1078 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1749 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1751 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1755 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1755 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2080 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2085 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2090 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2098 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2098 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2313 | UniProt | Hydroxyproline | ||||
Sequence: P |
Post-translational modification
Hydroxylation by PHD1/EGLN2 at Pro-2313 promotes ubiquitination.
Ubiquitinated by a SCF(SKP2) complex following proline hydroxylation.
Isoform 3
Ubiquitinated in a FBXL13-dependent manner, leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with SHBG (PubMed:15862967).
Interacts with PLK4; this interaction mediates the formation of a ternary complex composed by PLK4, TENT5C and CEP192 (PubMed:32433990).
Interacts with PLK4; this interaction mediates the formation of a ternary complex composed by PLK4, TENT5C and CEP192 (PubMed:32433990).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TEP8 | DCTPP1 Q9H773 | 2 | EBI-2339778, EBI-723569 | |
BINARY | Q8TEP8 | NUP50 Q9UKX7 | 4 | EBI-2339778, EBI-2371082 | |
BINARY | Q8TEP8 | PLK4 O00444 | 2 | EBI-2339778, EBI-746202 | |
BINARY | Q8TEP8 | PPP1CA P62136 | 2 | EBI-2339778, EBI-357253 | |
BINARY | Q8TEP8-3 | PLK4 O00444 | 13 | EBI-16111881, EBI-746202 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 69-138 | Disordered | ||||
Sequence: FSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATES | ||||||
Compositional bias | 72-87 | Polar residues | ||||
Sequence: PSGSSPGSQSDAEPRE | ||||||
Compositional bias | 88-104 | Basic and acidic residues | ||||
Sequence: RLQLSFQDDDSISRKKS | ||||||
Compositional bias | 105-123 | Polar residues | ||||
Sequence: YVESQRLSNALSKQSALQM | ||||||
Region | 288-308 | Disordered | ||||
Sequence: HSSETTHKESEESQVICLPGT | ||||||
Region | 950-1021 | Disordered | ||||
Sequence: VTFENHRIVSPKNSDLKNTSPEHGGRGSEDEQESFRPSTSPLSHSSPSEISGTSSSGCALESFGSAAQQQQP | ||||||
Compositional bias | 956-970 | Polar residues | ||||
Sequence: RIVSPKNSDLKNTSP | ||||||
Compositional bias | 983-1021 | Polar residues | ||||
Sequence: SFRPSTSPLSHSSPSEISGTSSSGCALESFGSAAQQQQP | ||||||
Region | 1043-1064 | Disordered | ||||
Sequence: VSEPESSYPTTATDDALEDRKS | ||||||
Compositional bias | 1101-1127 | Polar residues | ||||
Sequence: KGTLSSIIQNNSDTRKATETTSLSSKP | ||||||
Region | 1101-1158 | Disordered | ||||
Sequence: KGTLSSIIQNNSDTRKATETTSLSSKPEYVKPDFRWSKDPSSKSGNLLETSEVGWTSN | ||||||
Compositional bias | 1139-1157 | Polar residues | ||||
Sequence: DPSSKSGNLLETSEVGWTS | ||||||
Region | 1182-1234 | Disordered | ||||
Sequence: ATSHPVSCQEPIDEDQRISPKDKSTAGREFSGQVSHQTTSENQCTPIPSSTVH | ||||||
Compositional bias | 1191-1205 | Basic and acidic residues | ||||
Sequence: EPIDEDQRISPKDKS | ||||||
Compositional bias | 1207-1234 | Polar residues | ||||
Sequence: AGREFSGQVSHQTTSENQCTPIPSSTVH |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8TEP8-3
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.
- Name3
- Length2,537
- Mass (Da)279,111
- Last updated2018-07-18 v3
- ChecksumCA0A92F264280C3B
Q8TEP8-1
- Name1
- Differences from canonical
- 1-603: MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKR → MKTSDLV
Q8TEP8-2
- Name2
- Differences from canonical
- 1-603: MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKR → MKTSDLV
- 1999-2003: ALLHK → QGPAT
- 2004-2537: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_059657 | 1-603 | in isoform 1 and isoform 2 | |||
Sequence: MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKR → MKTSDLV | ||||||
Compositional bias | 72-87 | Polar residues | ||||
Sequence: PSGSSPGSQSDAEPRE | ||||||
Compositional bias | 88-104 | Basic and acidic residues | ||||
Sequence: RLQLSFQDDDSISRKKS | ||||||
Compositional bias | 105-123 | Polar residues | ||||
Sequence: YVESQRLSNALSKQSALQM | ||||||
Sequence conflict | 357 | in Ref. 1; AIA61642 | ||||
Sequence: V → I | ||||||
Compositional bias | 956-970 | Polar residues | ||||
Sequence: RIVSPKNSDLKNTSP | ||||||
Compositional bias | 983-1021 | Polar residues | ||||
Sequence: SFRPSTSPLSHSSPSEISGTSSSGCALESFGSAAQQQQP | ||||||
Compositional bias | 1101-1127 | Polar residues | ||||
Sequence: KGTLSSIIQNNSDTRKATETTSLSSKP | ||||||
Compositional bias | 1139-1157 | Polar residues | ||||
Sequence: DPSSKSGNLLETSEVGWTS | ||||||
Compositional bias | 1191-1205 | Basic and acidic residues | ||||
Sequence: EPIDEDQRISPKDKS | ||||||
Compositional bias | 1207-1234 | Polar residues | ||||
Sequence: AGREFSGQVSHQTTSENQCTPIPSSTVH | ||||||
Sequence conflict | 1402 | in Ref. 4; BAB84900 | ||||
Sequence: R → L | ||||||
Sequence conflict | 1453 | in Ref. 5; AAL55870 | ||||
Sequence: P → A | ||||||
Alternative sequence | VSP_059658 | 1999-2003 | in isoform 2 | |||
Sequence: ALLHK → QGPAT | ||||||
Alternative sequence | VSP_059659 | 2004-2537 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 2115 | in Ref. 3 and 7; AAI44482 | ||||
Sequence: R → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KJ567064 EMBL· GenBank· DDBJ | AIA61642.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001357 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP002449 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136818 EMBL· GenBank· DDBJ | CAB66752.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK074074 EMBL· GenBank· DDBJ | BAB84900.1 EMBL· GenBank· DDBJ | mRNA | ||
AF318363 EMBL· GenBank· DDBJ | AAL55870.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK001214 EMBL· GenBank· DDBJ | BAA91559.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC144481 EMBL· GenBank· DDBJ | AAI44482.1 EMBL· GenBank· DDBJ | mRNA |