wanglab/gogpt-training-data huggingface dataset:
Protein: Euchromatic histone lysine methyltransferase 2 (A0A8J8XWH8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MRGLPRGRGLMRARGRGRAAPTGGRGRGRGGAHRGRGRPRSLLSLPRAQASWAPQLPAGLTGPPVPCLPSQGEAPAEMGALLLEKEPRGAAERVHGSLGDTSHSEETLPKANPDSLEPTGPSSPASVTVTVGDEGADTPVGATPLIGEEPENLEGDGGRILLGHATKSFPSSPSKGGACPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAATAGPEPPPATTAGQEGQPKVHRARKTMSKPSNGQPPVPEKRPPEVQHFRMSDDMHLGKVTSDVAKRRKLTSGSLSEDLGSAGGSGEVILEKGEPRPLEEWETVVGDDFSLYYDAYSVDERVDSDSKSEVEALAEQLSEEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGCNAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGGTPPVGTVAPAPPPLAHDAPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPPGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAVRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMGWGVLHAKAVVGIKSTVCPTPQDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPDLSSLPPINT
Protein: Carbonic anhydrase Nec1 (EC 4.2.1.1) (Nectar protein 1) (NmNec1) (P0DO50)
Organism: Nesocodon mauritianus (Blue Mauritius bellflower) (Wahlenbergia mauritiana)
Function: Involved in the production of blood-red nectar containing the alkaloid nesocodin and that serves as a visual attractant for pollinator visitation, including vertebrates such as Phelsuma geckos. The nectar is initially acidic and pale yellow, but slowly becomes alkaline before turning into red within 24 hours. Together with NEC2 and NEC3, facilitates the condensation of sinapaldehyde ((E)-3,5-dimethoxy-4-hydroxycinnamaldehyde) and proline to form nesocodin, a pigment with a stable imine bond. Mediates the alkalinization (pH increase) of the flower nectar by catalyzing the reversible hydration of carbon dioxide.
Interaction partners:
Sequence:
MKMINSIFTHGSLIILLLLFHSISIKAQEVDDEREFDYLEGSELGPEKWGELRPEWGTCKRGKMQSPIDISNPVQVTSKELLQTKYKAQNAIINNRGHDIMVRWEGDAGSILINEREFDLLQAHWHAPSEHAINGTRYAMELHMLHRSTDPKLTPTMVVVAVFYEIGDVDPFLSRLGPIMSSLIDQTNEHKQAGVINPMEIQLDDECYYKYIGSLTTPSCTEGVTWIINKRINTVSSDQVKLLREAVHDHAKNNARPLQALNHREVQLHCHKDRKD
Protein: nitric-oxide synthase (NADPH) (EC 1.14.13.39) (Q156E2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
FTTHLETTLTEDGHQRTVRVTRPVFPASKSYERCCPLSPLSPGQGGKDPQQLRAIENLSSPSVTPLHREAMLQRGGVQALIAAQDPMLRDRGCGALLLNGVEENNDMLKEIEPVLQLIKNSKREINGEEQRTIQRRDAEVQVDRDLGMGNGMSPQLASDKNSVCEDLWRKDNNMQTVLTNPYSEKDEPPAQGRISPNKALMNGSPSKCPRFMKIKNVETGVTYNDTLHHSSSNYPLCTECLCFGSIMTPSQGSRKPDESRTKEELLPLATDFIDQYYTSIKRFGSKAYVDRLEEVTKEIEASGTYQLKDTELIYGAKHAWRNAARCVGRIQWSKLQVFDARDCTTAHGMYNYICNHIKYATNKGNLRSAITIFPQRTDGKRDFRVWNTQLIRYAGYKQPDGQILGDPANVEFTEICIQQGWKAPKGRFDVLPLLLQSNGNDPELFEIPQDLILEVQITHPKYDWFKDLNLKWYSLPAVFSMLLKVGGLEFTAFTACPFSGWVMGTEIGVRNFGDSSRYNFCEEVATMMGLDTRKTFLLWKDQALVEINIAVLYSFNLSKVTIVDHHSATESFMKHMENEIRVRGGCPGDWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQADPWNNHVRKVNNGTPTKKRAIGFKKLAKAVKFSAKLMGQAMAKRVKATILFATETGKSQDYAKTLCEIFKHAFDAKVMSMDEYDMVDLEHETLVLAVTSTFGNGDPPENGEKFGAALMEMRHPTSNTEDRKSYKVRFKG
Protein: Probable receptor-like protein kinase At5g24010 (EC 2.7.11.-) (Q9FLW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
Interaction partners:
- AT3g15480/MJK13_14
- Cyclase-associated protein 1
- GPI-anchored protein LLG3
- GPI-anchored protein LLG1
- GPI-anchored protein LLG2
Sequence:
MAFPINLTQTLLFFFCPLLHLSFAAFTPTDNYLINSGSNTNTSFFTTRSFLSDSSEPGSSFLSTDRSISISDTNPSPDSPVLYNTARVFPVGGSYKFQVTTKGTHFIRLHFAPFKASRFNLRSAKFRVLINGFSVINSFSTSSVVVKEFILKIDDPVLEISFLPFKASGFGFVNAVEVFSAPKDYIMDQGTKLVIPNSAQIFSNLSSQVLETVHRINVGGSKLTPFNDTLWRTWVVDDNYLLLRAAARRAWTTHSPNYQNGGATREIAPDNVYMTAQEMDRDNQELQARFNISWGFQVDEKRVLHLVRLHFCDIVSSSLNQLYFNVFINEYLAFKDVDLSTLTFHVLASPLYIDFVAESDRSGMLRISVGPSDLSNPARVNALLNGVEIMRILSPVSSEVVSGKRNVVWIVVGSVLGGFVFLSLFFLSVLCLCRRKNNKTRSSESTGWTPLRRFRGSSNSRTTERTVSSSGYHTLRISFAELQSGTNNFDRSLVIGVGGFGMVFRGSLKDNTKVAVKRGSPGSRQGLPEFLSEITILSKIRHRHLVSLVGYCEEQSEMILVYEYMDKGPLKSHLYGSTNPPLSWKQRLEVCIGAARGLHYLHTGSSQGIIHRDIKSTNILLDNNYVAKVADFGLSRSGPCIDETHVSTGVKGSFGYLDPEYFRRQQLTDKSDVYSFGVVLFEVLCARPAVDPLLVREQVNLAEWAIEWQRKGMLDQIVDPNIADEIKPCSLKKFAETAEKCCADYGVDRPTIGDVLWNLEHVLQLQESGPLNIPEEDYGDVTDPRTARQGLSNGSNIERDYGDGTSGIISSTQVFSQLMTNAGR
Protein: Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) (Q5HZM6)
Organism: Xenopus laevis (African clawed frog)
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Stabilizes transcriptional repressor snai1 by inhibiting its ubiquitination which promotes neural crest cell migration.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H9T3}. Nucleus {ECO:0000250|UniProtKB:Q9H9T3}.
Interaction partners:
Sequence:
MKPDRGMRGNMSQAELMMMTVADVIKQLVEAHEQGKDVNLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQYRKILVPKLKAKPIRTASGIAVVAVMCKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHNVDKVEFIVMGGTFMALPEDYRDFFIRNLHDALSGHTSNSVSEAVRYSERSNTKCVGITIETRPDYCLKRHLSDMLCYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLSKDAGFKVVSHMMPDLPNMGLERDIEQFIEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYRSYSPSTLVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTECRDVRTREVGIQEIHHKVRPYQVELIRRDYVANGGWETFLSYEDPEQDILIGLLRLRKCSEESFRPELKGGVSIVRELHVYGSVVPISSRDPSKFQHQGFGMLLMEEAERIARDEHGSWKIAVISGVGTRNYYRKIGYELEGPYMVKRLD
Protein: Insulin-1 [Cleaved into: Insulin-1 B chain; Insulin-1 A chain] (P01322)
Organism: Rattus norvegicus (Rat)
Function: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1
- Insulin receptor
- Insulin-like growth factor 1 receptor
- Insulin receptor substrate 1
- Pro-epidermal growth factor
- Insulin receptor substrate 2
- Insulin receptor-related protein
- Receptor protein-tyrosine kinase
- Cation-independent mannose-6-phosphate receptor
- Insulin receptor substrate 3
Sequence:
MALWMRFLPLLALLVLWEPKPAQAFVKQHLCGPHLVEALYLVCGERGFFYTPKSRREVEDPQVPQLELGGGPEAGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
Protein: 14-3-3-like protein A (14-3-3e protein) (B6RF02)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Flowering locus T-like protein
- Protein HEADING DATE 3A-like
- Protein TIME FOR COFFEE-like
- arsenate reductase
- arsenate reductase
- Protein PXR1-like
- T-complex protein 1 subunit theta-like
- CCT-theta
- CCT-theta
- CCT-theta
Sequence:
MSPTESSREENVYMAKLAEQAERYEEMVEFMEKVAKTVDVEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVAQLKEYRGKIEAELSKICDGILSLLESHLIPLASSAESKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDITDEAGDEIKEASKHESGEGQQ
Protein: Somatotropin (Growth hormone) (P01246)
Organism: Bos taurus (Bovine)
Function: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Subcellular location: Secreted.
Interaction partners:
- Growth hormone receptor
- Somatoliberin
- Appetite-regulating hormone
- Short palate, lung and nasal epithelium carcinoma-associated protein 2A
- Peripherin-2
- Retinal guanylyl cyclase 1
- Amelogenin, X isoform
- Killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 5A
- Gamma-crystallin D
- Thyroglobulin
Sequence:
MMAAGPRTSLLLAFALLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (P62267)
Organism: Mus musculus (Mouse)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays an important role in translational accuracy.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62266}. Cytoplasm {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62266}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}.
Interaction partners:
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL30
Sequence:
MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS
Protein: L-amino-acid oxidase (DrLAO) (LAAO) (EC 1.4.3.2) (G8XQX1)
Organism: Daboia russelii (Russel's viper) (Vipera russelii)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active on L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L-Val, L-Lys, and L-Ala. Inhibits ADP- and collagen-induced platelet aggregation. This inhibition is inhibited by catalase, indicating the importance of generated H(2)O(2) for the inhibitory effect. This effect on platelets among snake L-amino-acid oxidases is however controversial, since some of them induce aggregation, whereas the other inhibit agonist-induced aggregation (By similarity). In vivo, this enzyme induces a rapid, substantial and reversible increase in the paw volume of mice (edema). In addition, myofibrosis, and inflammatory cell infiltration on the paw tissue are also observed.
Subcellular location: Secreted {ECO:0000269|PubMed:21802487}.
Interaction partners:
Sequence:
MNVFFMFSLLFLATLGSCADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVIVGAGMSGLSAAYVLAGAGHKVTVLEASERPGGRVRTHRNVKEGWYANLGPMRVPEKHRIIREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVHFKARVIKIQQNAEKVTVTYQTTQKNLLLETADYVIVCTTSRAARRITFKPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIQGGKSTTDLPSRFIYYPNHNFTTGVGVIIAYGIGDDANFFQALNLNECADIVFNDLSSIHQLPKKDLQTFCYPSIIQKWSLDKYAMGAITTFTPYQFQHFSEALTAPVGRIFFAGEYTANAHGWIDSTIKSGLTAARDVNRASEL
Protein: AP-2 complex subunit mu (E9PFW3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|PIRNR:PIRNR005992}. Membrane, coated pit {ECO:0000256|PIRNR:PIRNR005992}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR005992}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR005992}.
Interaction partners:
Sequence:
MIGGLFIYNHKGEVLISRVYRDDIGSRQAADSAVFSSSGPFPGEWLEANRRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC
Protein: Precursor of CEP9 (PCEP9) [Cleaved into: C-terminally encoded peptide 9.1 (CEP9.1) (CEP9a); C-terminally encoded peptide 9.2 (CEP9.2) (CEP9b); C-terminally encoded peptide 9.3 (CEP9.3) (CEP9c); C-terminally encoded peptide 9.4 (CEP9.4) (CEP9d); C-terminally encoded peptide 9.5 (CEP9.5) (CEP9e)] (A0A1I9LMX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 9.2]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.4]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.5]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.1]: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25324386}. Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}.
Interaction partners:
- Precursor of CEP15
- Precursor of CEP8
- Precursor of CEP4
- Precursor of CEP14
- Precursor of CEP7
- Precursor of CEP13
- Protein IDA-LIKE 5
- Precursor of CEP11
- Precursor of CEP5
- Protein IDA-LIKE 4
Sequence:
MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA
Protein: Centrosomal protein of 55 kDa (Cep55) (Up-regulated in colon cancer 6) (Q53EZ4)
Organism: Homo sapiens (Human)
Function: Plays a role in mitotic exit and cytokinesis. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis. Not required for microtubule nucleation. Plays a role in the development of the brain and kidney.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28264986}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16198290}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16198290}. Cleavage furrow {ECO:0000269|PubMed:16198290}. Midbody, Midbody ring {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:28264986}. Note=Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loses affinity for the centrosome at the onset of prophase and diffuses throughout the cell. This dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis. {ECO:0000269|PubMed:16198290}.
Interaction partners:
- Tumor susceptibility gene 101 protein
- Disks large-associated protein 5
- Kinesin-like protein KIF11
- Programmed cell death 6-interacting protein
- Inactive serine/threonine-protein kinase TEX14
- Kinesin-like protein KIF23
- Kinesin-like protein KIF20A
- Centromere protein F
- Rac GTPase-activating protein 1
- Cyclin-dependent kinase 1
Sequence:
MSSRSTKDLIKSKWGSKPSNSKSETTLEKLKGEIAHLKTSVDEITSGKGKLTDKERHRLLEKIRVLEAEKEKNAYQLTEKDKEIQRLRDQLKARYSTTTLLEQLEETTREGERREQVLKALSEEKDVLKQQLSAATSRIAELESKTNTLRLSQTVAPNCFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLPQQTKKPESEGYLQEEKQKCYNDLLASAKKDLEVERQTITQLSFELSEFRRKYEETQKEVHNLNQLLYSQRRADVQHLEDDRHKTEKIQKLREENDIARGKLEEEKKRSEELLSQVQFLYTSLLKQQEEQTRVALLEQQMQACTLDFENEKLDRQHVQHQLHVILKELRKARNQITQLESLKQLHEFAITEPLVTFQGETENREKVAASPKSPTAALNESLVECPKCNIQYPATEHRDLLVHVEYCSK
Protein: Lutropin-choriogonadotropic hormone receptor (Q7T027)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}.
Interaction partners:
- Glycoprotein hormones alpha chain
- Glycoprotein hormones alpha chain
- Gonadotropin subunit beta-2
- Gonadotropin subunit beta-1
- Glycoprotein hormones alpha chain
- Glycoprotein hormones alpha chain
- Lutropin-choriogonadotropic hormone receptor
- Thyrotropin subunit beta-like
- Thyrotropin subunit beta
Sequence:
MMSISLLFLFYPSVLLFFGFGCRYASSFVCPGICRCSSNTIRCNNITEKSVPMSERGPRLVLKHLTMSTIASHTFDGLRRVQHIEIGQSVALETIETLAFNNLLDLNEIFIKNTRSLVHIARRTFNNLPKLRYLSISNTGITVFPDMTSIHSLEPWNQNFVLDICDNLYLLSIPVNAFVGMTTEYTAMNLFNNGIREIQDYAFNGTKINKLVLKNNRNLRVIHREAFKGAVGPRILDVSSTAIETLPSHGLNSVVELVARTAYGLKRLPPFRGLGNLQKAHLTYNSHCCALLTWDTHRDSPINAAQHNGSRPTYCDDSQSEKFPAGMVDSSDTSLLVEIHGTNKDVEDESYGGVDFQYPELGLYCQTRPTLQCTPEADAFNPCEDIAGFSFLRVAIWFINILAIIGNLTVLLIFFTSRCKLTVPRFLMCHLAFADFCIGVYLLMIAAVDLHTRGHYSEHAIDWQTGAGCSAAGFLSVFGGELSVYTLSTITLERWHTITHALQLEKRLGLAQAAGIMAGGWLICLGMAMLPLVGVSSYSRVSMCLPMDVKTPLAQAFILLLLFFNVGAFLVVCVCYVLIYLAVRNPQFPSRSADAKIAKRMAVLIFTDLLCMAPISFFAISAAFKVPLITVTNSKILLVLFFPINSCANPFLYAIFTKAFRKDVYLLLSNMGCCENKANMYRMKAYCSENLVKSSSGNKGTLICTTQMMDPLPLQSQQLKDDGDLGTI
Protein: Conserved domain protein (Q728D4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Cell division protein ZapA
Sequence:
MELLDLLENRVTSLLAQLESLREENRTLREEVDNGLAALAEENRTLKEALEQERSVKDAVLGRIDSLLTTLKDKTGDA
Protein: Odorant receptor 22b (P81910)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Involved in the behavioral responses to esters. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 85b
Sequence:
MLSQFFPHIKEKPLSERVKSRDAFVYLDRVMWSFGWTVPENKRWDLHYKLWSTFVTLLIFILLPISVSVEYIQRFKTFSAGEFLSSIQIGVNMYGSSFKSYLTMMGYKKRQEAKMSLDELDKRCVCDEERTIVHRHVALGNFCYIFYHIAYTSFLISNFLSFIMKRIHAWRMYFPYVDPEKQFYISSIAEVILRGWAVFMDLCTDVCPLISMVIARCHITLLKQRLRNLRSEPGRTEDEYLKELADCVRDHRLILDYVDALRSVFSGTIFVQFLLIGIVLGLSMINIMFFSTLSTGVAVVLFMSCVSMQTFPFCYLCNMIMDDCQEMADSLFQSDWTSADRRYKSTLVYFLHNLQQPIILTAGGVFPISMQTNLNMVKLAFTVVTIVKQFNLAEKFQ
Protein: ER membrane protein complex subunit 1 (Q9VHY6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 7
- Membrane magnesium transporter
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 8/9 homolog
- ER membrane protein complex subunit 2
- Dynactin subunit 4
Sequence:
MQEKWLLPALSLALLLGTCSALYEDQIKKFDWRGVNVGALKQSRVDLNHFQPRILVTTYEGVVASLCVKTGELVWRQVLEQKPRGDVKLLQVSGFADDSSDTAAAPMGSNMGFDMLTVQGHAPALVRGWNTNMGALEWEWSIMPMNTERAQDAMWIYSKSVLYHVLPAWRSHLEVTAYFASSGHSTGSTSKVIAPWITSESCTLSGTFYVCTDGKQLISLDLVSKSGQVIRTSLEAEPKGKTQALTGLNGVVIVDGKPISVNKDQSICGDLRSSSFAVGSFNYRKVLAYADLSSGILRINALYLDNCAPAAELEQSLPFPEHFGTPSLSNFDCKQKRNGEGKNCLFLFSSTSESIVAVQHGRVRWSREESLANVIDSQFVDLPLADTEGTLENEMKGKAGDFTSFERDIASAFLRRITTQAVQIRSLFLHVIGLGPPPTDTQRAGLVRDSFGLHKMLVLLTRAGKIFGIDNVSGKHHWQLHLPNVIGFANDEQMRLIVQRSAKHFPLQPLCTILGKNAVSGNGVLYRFNPITGKVAEGGLVQLDYRIKQLSLLGETEKDFLKGILLLDASNKVHVYPEHAAPLADGMYLYTADLKTAELAGYFVKYAGGQLSSTHIWNARLGGHNSEQQIIGVAGKNPIEHVHSQGRVLGDRSVLYKYINPNLVAFVTQAPDSTHKSVLNLYLVDVVSGSVVFTMTHRKVRAPLSIVHSENWLAYSYFNEKLRRTEITTIELYEGKSQANSSVWSSLQAPPMPLVERQSYILPTIVEALRETITERGITNKHVLIGTASGSIVEMPWHLLDPRRPIASTTQGREEGAIPYIPELPLPTESHINYNQTVARLRNIYTAPSGLESTCLVVATGLDLFVTRVAPSKTFDLLKEDFDYILISIVLVALTSGSLIVKHLASRKLLKQAWK