wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich single-pass membrane protein 1 (Q8N8F7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTHSSQDTGSCGIQEDGKLYVVDSINDLNKLNLCPAGSQHLFPLEDKIPVLGTNSGNGSRSLFFVGLLIVLIVSLALVFFVIFLIVQTGNKMDDVSRRLTAEGKDIDDLKRINNMIVKRLNQLNQLDSEQN
Protein: Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3 homolog) (Q9W3U1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-74'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30526847}. Nucleus {ECO:0000269|PubMed:30526847}. Note=Localizes mainly in the cytoplasm. {ECO:0000269|PubMed:30526847}.
Interaction partners:
- RE54550p
- Exonuclease mut-7 homolog
- EG:BACR7C10.4 protein
- U3 small nucleolar RNA-associated protein 15 homolog
Sequence:
MGKNTKRNKKTKQQQQQPQQNGVTASASGTAVEDFEDQQAASSLPSLNGKKRSQLNKLVEELLDLVEKQPANPNEEWKQYGQLQELLKQIMILEEPLSQAVCPQISDSPDDQTRLAKVEAFSAWAKDGGVHSEGLEIAIFPGYQLGLRATRPLAKDELVLSVPRKLILSEENNSDCRLFGKMTQATHLNLAYDLVIEKIRGEFSEWRPYIDVLPAKYNTVLYFTTKQMELLRGTAAAALAMRQCRVIAKQYAFLYKYAHTMTEPSTGNRSHPGERGLFFTQHGLCYKLYRWAVSTVMTRQNLVPSEKQESEDGPKLISALIPYWDMANHRPGKITSFYATVSRQLECTAQEAVNTGEQFFIYYGDRSNTDLLVHNGFVDPNNTKDYVNIRVGLSLTDALAAKRASILDKLNIRHTAELRVLPAPDFISKELLAFVRVFKMSAEQLDHWCSDLDRAGDLLHIDCALETDHETRTWQFLEDRLKLLLAVFNKEMHEADEVKELELKDGQEIELMLFLYRRLERSILAGALQYAQEHRKV
Protein: Uncharacterized protein YjfN (P0AF82)
Organism: Escherichia coli (strain K12)
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Lipoprotein BsmA
- Uncharacterized protein YjfY
Sequence:
MKQLLASPSLQLVTYPASATAQSAEFASADCVTGLNEIGQISVSNISGDPQDVERIVALKADEQGASWYRIITMYEDQQPDNWRVQAILYA
Protein: SURF1-like protein (Q385U9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363076}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363076}.
Interaction partners:
- Cytochrome oxidase assembly protein, putative
- Cytochrome C oxidase assembly protein, putative
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c
Sequence:
MRPDYMGFMFLTSGVMSFNAGIWQLHRRRQKRRLMENHKNIRKPPVYELPPGDATIDEFEFLPAAFEGTFDNEGSMLVGPRALPTYKGASSNEESNGGFLVVTPFEIAHTGQFIMVNRGWVPIDAGKHRTLLMQYVGEGFTPGSVRGIFRREEYMSASLIWGPNKDNEGPVAADLSWLVMRPWNMAVHYYKRRWGPDRAEESVEKHGARHYYLEMIEDYSGDDQRMVRGHPWPWRRSVDEITYVHLPPSVHTMYIFFWFSVTLGSLYGMGKCYKRQKELFALRRQMTAQTTLLERKRQEEAKMYMEAMKEVERLKKLGTVAAPRIGSQPTEQQKSDEKSPASGEKS
Protein: Norsolorinic acid reductase stcV (EC 1.1.1.-) (Sterigmatocystin biosynthesis cluster protein V) (Q00727)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Norsolorinic acid reductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
Sequence:
MAAPPAPQPPSLLGYHRVLSPLAGIRVSPLCLGTMHFGGQWTRAMGDVTKETAFALLDRFYEAGGNFIDTANFYQGEGSEKWLGEWVASRGNRDELVLATKYTMSYRLTGPEKIKSNFQGSHSKSLRLSVEASLAKLRTDYIDLLYVHMWDFSTSVEEVMQSLHHLVAAGKVLNIGISDAPAWVVAKCNEYARFHGLTRFCVYQGRWACSYRDFEREILPMCQSEGLALAPWGALGRGQYKSAEEFQQEGTRNMGPQEEKHRLMGAKLTEVGERKGVAAAAIALAYLLHKSPYVFPVIGCRTVEQLEANITSLGVELSDEEIYEIEDTIPFDVGFPMAFLFESPQQKYRSDMTTRHIWQVTCNARIESVPKPRPIEPKQGYKQMDRK
Protein: RE15579p (Trynity, isoform A) (Trynity, isoform B) (Trynity, isoform C) (Trynity, isoform D) (Trynity, isoform E) (Trynity, isoform F) (Q8MS37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE59626p
- Hexosyltransferase
Sequence:
MQSTQSKSDRSSMHRGPLLLCAVMVVLVTLPEQINARMAFEKLTDFDFPGNTYYSVKNLSLYECQGWCREEADCQAAAFSFVVNPLSPSQETHCQLQNDSSAANPSAAPQRSANMYYMIKLQLRSENVCHRPWSFERVPNKVIRGLDNALIYTSTKEACLSACLNERRFVCRSVEYDYNNMKCVLSDSDRRSSGQFVQLVDAQGTDYFENLCLKPAQACKNNRSFGNSQKMGVSEEKVAQYVGLHYYTDKELQVTSESACRLACEIESEFLCRSFLYLGQPQGSQYNCRLYHLDHKTLPDGPSTYLNHERPLIDHGEPIGQYFENQCEKAAGLGAGSPPGTLDKIDTLPVSLDTIEDPNLTNLTRNDVNCDKTGTCYDVSVHCKDTRIAVQVRTNKPFNGRIYALGRSETCNIDVINSDAFRLDLTMAGQDCNTQSVTGVYSNTVVLQHHSVVMTKADKIYKVKCTYDMSSKNITFGMMPIRDPEMIHINSSPEAPPPRIRILDTRQREVETVRIGDRLNFRIEIPEDTPYGIFARSCVAMAKDARTSFKIIDDDGCPTDPTIFPGFTADGNALQSTYEAFRFTESYGVIFQCNVKYCLGPCEPAVCEWNMDSFESLGRRRRRSIESNDTKSEDDMNISQEILVLDFGDEKREFFKADPSTDFAKDKTVTIIEPCPTKTSVLALAVTCALMILLYISTLFCYYMKKWMQPHKIVA
Protein: Lytic chitin monooxygenase (EC 1.14.99.53) (EfCBM33A) (Lytic polysaccharide monooxygenase) (LPMO) (Q838S1)
Organism: Enterococcus faecalis (strain ATCC 700802 / V583)
Function: Involved in chitin degradation. Catalyzes the oxidative cleavage of glycosidic bonds in both alpha- and beta-chitin via a copper-dependent mechanism, leading to oxidized chitooligosaccharides with a dominance of even-numbered products. Acts synergistically with the chitinase EfChi18A, and combining the two enzymes leads to rapid and complete depolymerization of crystalline chitin, especially with beta-chitin as a substrate. Is likely involved in a chitin degradation pathway that allows E.faecalis V583 to grow on chitin as a carbon source.
Subcellular location: Secreted {ECO:0000305|PubMed:22210154}.
Interaction partners:
- Chitinase
- Carbohydrate deacetylase
Sequence:
MKKSLLTIVLAFSFVLGGAALAPTVSEAHGYVASPGSRAFFGSSAGGNLNTNVGRAQWEPQSIEAPKNTFITGKLASAGVSGFEPLDEQTATRWHKTNITTGPLDITWNLTAQHRTASWDYYITKNGWNPNQPLDIKNFDKIASIDGKQEVPNKVVKQTINIPTDRKGYHVIYAVWGIGDTVNAFYQAIDVNIQ
Protein: Nicotinamide nucleotide adenylyltransferase 3 (D6RHV4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEG
Protein: Putative uncharacterized protein RUSC1-AS1 (RUSC1 antisense RNA 1) (RUSC1 antisense gene protein 1) (Q66K80)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPGGSENAAALWISEGGRGPGRGPGPEWTSRSLLPQSGPALQPTPYSQRKGPRETHPDALKGGGGWGWGNTQSLSGECRKGVGAGEEKDGAAVSLSTPHLLAASAGLQPAPSPLGTAVCPFSPHSSPSFSHHRTLSLFISPAPLSCPAPRAQVHRSTPMGRALLTRVLLEPLRPWACPRLPRSPPGGAQSGRGGALAQPTLRCAAAPLRAWAWRSSDPPPAFSVFCHPPRGFDIS
Protein: Chromatin modifying protein 2B (cDNA FLJ11303 fis, clone PLACE1009995, highly similar to Charged multivesicular body protein 2b) (cDNA FLJ11318 fis, clone PLACE1010274, highly similar to Charged multivesicular body protein 2b) (cDNA, FLJ95104) (B2RE76)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (P38697)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:14562095}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase 3
- Inosine-5'-monophosphate dehydrogenase 4
- Hypoxanthine-guanine phosphoribosyltransferase
- Bifunctional purine biosynthesis protein ADE17
- Bifunctional purine biosynthesis protein ADE16
- AMP deaminase
- IMP-specific 5'-nucleotidase 1
- Purine-cytosine permease FCY2
Sequence:
MAAIRDYKTALDFTKSLPRPDGLSVQELMDSKIRGGLTYNDFLILPGLVDFASSEVSLQTKLTRNITLNIPLVSSPMDTVTESEMATFMALLGGIGFIHHNCTPEDQADMVRRVKNYENGFINNPIVISPTTTVGEAKSMKEKYGFAGFPVTTDGKRNAKLVGVITSRDIQFVEDNSLLVQDVMTKNPVTGAQGITLSEGNEILKKIKKGRLLVVDEKGNLVSMLSRTDLMKNQNYPLASKSANTKQLLCGASIGTMDADKERLRLLVKAGLDVVILDSSQGNSIFELNMLKWVKESFPGLEVIAGNVVTREQAANLIAAGADGLRIGMGTGSICITQEVMACGRPQGTAVYNVCEFANQFGVPCMADGGVQNIGHITKALALGSSTVMMGGMLAGTTESPGEYFYQDGKRLKAYRGMGSIDAMQKTGTKGNASTSRYFSESDSVLVAQGVSGAVVDKGSIKKFIPYLYNGLQHSCQDIGCRSLTLLKNNVQRGKVRFEFRTASAQLEGGVHNLHSYEKRLHN
Protein: Ubiquitin 3 binding protein But2 C-terminal domain-containing protein (Q5B5Y9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MFGFKLFLALAVLATTSQTAQINRPSVRDSTILRSTVSCPDCPESNCYKCRYGSEKTLRANTGGLAWIQSLVGFRLDLPDDIYPDDITKCTVQFPAFTTLPNSAFNMTVTPAVSSDWDEVTVNGENAPASTDNIALYHVPALTNPPLLDVTEACWLADDDGQFSIYLGAEFGSYEIWSKDSGNPAVLHVYYDD
Protein: Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (Complexed with cdc5 protein 9) (snRNP core protein D2) (O14036)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62316}.
Interaction partners:
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 19
- LSM complex subunit lsm2
- Pre-mRNA-splicing factor prp5
- Pre-mRNA-splicing factor cwf2
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein E
Sequence:
MADLVDKPRSELSEIELARLEEYEFSAGPLSVLQQAVKNHDQVLINCRNNKKLLARVKAFDRHSNMVLENVKEMWTEKKRTASGKKGKAINKDRFISKMFLRGDGVVLVVRIPSA
Protein: Double C2-like domain-containing protein alpha isoform X2 (Double C2-like domains, alpha) (F1R9U1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- Aspartate beta-hydroxylase domain-containing protein 2
- Kinesin-like protein KIF22
- Seizure-related 6 homolog
- Protein yippee-like 3
- Serine/threonine-protein phosphatase 4 catalytic subunit A
- Proline-rich transmembrane protein 2
- PAXIP1-associated glutamate-rich protein 1
- Rabphilin 3A-like
- TLC domain-containing 3Ba.
Sequence:
MTVRKGKKLTISIQEHMAIDVCPGPIRPIRQISAYFPRLSPTAEPVSPNPASPLSLSPGLGASGGASGGLLSPLQAGARGGGGTLSAASSIETSVDICSSDSDDSTALGTLEFELRYEKATSSLNCTIIRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTVRNSLNPVWNETLTYVGITEEDMHRKTLRLSVCDEDKLTHNEFIGESRVALRRVKPDQTKRFYTCLEHPPPLPSPTAMGAALRGISCYLREWENEQMTSLEERGRLLLSLQFLPPPAEGEGESRRGGLCVGVLRCAHLAAMDVNGFSDPYVKIYLKPDVKKKSKHKTSVIKKTLNPEFNEEFFYEISLSELVHKTLEVTVWDYDLGRSNDFIGGVCLSCHVQGDALRHWMDCLRNKGQRVERWHILANELPQTTCHD
Protein: Cell division control protein 24 (O75004)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the progression of DNA replication and in the maintenance of genomic integrity. Acts during S phase, after initiation, where it is essential for completion.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA replication ATP-dependent helicase/nuclease dna2
- Cell division control protein 42 homolog
- ATP-dependent DNA helicase pfh1
- DNA polymerase delta subunit 3
- Uncharacterized protein C1322.02
- Rho guanine nucleotide exchange factor scd1
- Protein scd2/ral3
Sequence:
MDFPGLIKKIKEDLENRLVEKSKQPAFTDYWLINKTISLLKEYPSGFSYPILINEIELACSERNKLDNVFSSLEWLTKSDAVIYLEDQFHFHCYDYYYTPIPSLKLKDSEENTCEMILHSSFYLLFHEPFNILKGSTLRFSQSRIHQKWYLRKQIRFLPTTSFVPVLQYAASKSFVKSMVESTEHEFFQIRDITISKSDQGVKRITVELGRIISLDKKGAFLIDNNTNFIHFSGTYHDFPKLLDKQQYLLIPFWSTVWEGSTNWQDGMIGILVILSENDFEEKKCDSWQVGRLAAVNSNFLVLDNNGQRVKILYSNSQKHYFKDTYIGDLLCISPINHSSDNLSDYSCVSDTTTEILSNLENPLSSNFLRNDLCKFSNLFSGVSGHLKIQPLTLVITGFVANLTRQSDLNTSLVLPEVNPLTAKMEVIDCLRNSFWAALRPNCVSYFASMISGFKELFQKEMEFPIYLDLKSYKLGFHWCDIYVDSEHNCHIQKINSLPCE
Protein: Uncharacterized protein (Q382I9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDENTTSFALNVSGWLIPDIRRHVFVLVWCCGVPVHVRYIIQLLRMSSVPLEMMMSSSDEGSVEKVEKYDSKNHGAPHSPSESELRSVALDIAFTQVGSDCCKANSHVVEACLSEERWAEVRSLSCVATSDTDGGGTATRIVSSDPTVNGEVLVLLPPGEVPQAELVSAYFTALDQARFFERQYKMHVTCPLDGFEWGKTERNEVKKHPSLGSANRKAGVEVIVIGSSDDDDEGDQKMAEVVVLDDSDDETP
Protein: Selenoprotein S (SelS) (VCP-interacting membrane protein) (Q9BQE4)
Organism: Homo sapiens (Human)
Function: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm {ECO:0000250}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Derlin-1
- Selenoprotein K
- Derlin-2
- E3 ubiquitin-protein ligase synoviolin
- Protein sel-1 homolog 1
- E3 ubiquitin-protein ligase AMFR
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein F
- FAS-associated factor 2
Sequence:
MERQEESLSARPALETEGLRFLHTTVGSLLATYGWYIVFSCILLYVVFQKLSARLRALRQRQLDRAAAAVEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLKQLEEEKRRQKIEMWDSMQEGKSYKGNAKKPQEEDSPGPSTSSVLKRKSDRKPLRGGGYNPLSGEGGGACSWRPGRRGPSSGGUG
Protein: Magnetosome protein Mms5 (Q2W8J4)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Might be involved in magnetite crystal growth.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:16303747}; Single-pass membrane protein {ECO:0000255}. Note=Tightly associated with magnetite crystals. {ECO:0000269|PubMed:12496282}.
Interaction partners:
- Magnetosome protein MamF
Sequence:
MLSAKGVSLGLGLGLGAWGPVLLGVVGVAGAIALYGYYKNRNAEPAAAEAV
Protein: Protein SMAX1-LIKE 6 (AtSMXL6) (Protein D53-like 2) (AtD53-like 2) (Protein D53-like SMXL 6) (Q9LML2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of a transcriptional corepressor complex involved in branching control. Regulates cotyledon expansion and lateral root growth, but not germination or hypocotyl elongation. Promotes auxin transport and PIN1 accumulation in the stem and represses BRC1/TCP18 expression in axillary buds.
Subcellular location: Nucleus {ECO:0000269|PubMed:26546446}.
Interaction partners:
- F-box protein MAX2
- Probable esterase KAI2
- Strigolactone esterase D14
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Carotenoid cleavage dioxygenase 7, chloroplastic
- Cytochrome P450 711A1
- Carotenoid cleavage dioxygenase 8, chloroplastic
- ATP-dependent Clp protease adapter protein CLPS1
- Squamosa promoter-binding-like protein 15
- Protein RADIALIS-like 5
Sequence:
MPTPVTTARECLTEEAARALDDAVVVARRRSHAQTTSLHAVSALLAMPSSILREVCVSRAARSVPYSSRLQFRALELCVGVSLDRLPSSKSPATEEDPPVSNSLMAAIKRSQANQRRHPESYHLQQIHASNNGGGGCQTTVLKVELKYFILSILDDPIVNRVFGEAGFRSSEIKLDVLHPPVTQLSSRFSRGRCPPLFLCNLPNSDPNREFPFSGSSGFDENSRRIGEVLGRKDKKNPLLIGNCANEALKTFTDSINSGKLGFLQMDISGLSLISIEKEISEILADGSKNEEEIRMKVDDLGRTVEQSGSKSGIVLNLGELKVLTSEANAALEILVSKLSDLLKHESKQLSFIGCVSSNETYTKLIDRFPTIEKDWDLHVLPITASTKPSTQGVYPKSSLMGSFVPFGGFFSSTSNFRVPLSSTVNQTLSRCHLCNEKYLQEVAAVLKAGSSLSLADKCSEKLAPWLRAIETKEDKGITGSSKALDDANTSASQTAALQKKWDNICQSIHHTPAFPKLGFQSVSPQFPVQTEKSVRTPTSYLETPKLLNPPISKPKPMEDLTASVTNRTVSLPLSCVTTDFGLGVIYASKNQESKTTREKPMLVTLNSSLEHTYQKDFKSLREILSRKVAWQTEAVNAISQIICGCKTDSTRRNQASGIWLALLGPDKVGKKKVAMTLSEVFFGGKVNYICVDFGAEHCSLDDKFRGKTVVDYVTGELSRKPHSVVLLENVEKAEFPDQMRLSEAVSTGKIRDLHGRVISMKNVIVVVTSGIAKDNATDHVIKPVKFPEEQVLSARSWKLQIKLGDATKFGVNKRKYELETAQRAVKVQRSYLDLNLPVNETEFSPDHEAEDRDAWFDEFIEKVDGKVTFKPVDFDELAKNIQEKIGSHFERCFGSETHLELDKEVILQILAASWSSLSSGEEEGRTIVDQWMQTVLARSFAEAKQKYGSNPMLGVKLVASSSGLASGVELPAKVDVIW
Protein: Invasin (Q4ACI6)
Organism: Edwardsiella tarda
Interaction partners:
Sequence:
SGIRQIAEIPYNLVDRNNDLVLEYKKQEVIKLALSHHAINDLAGAVYTVSANLKSKYALDQVSWQDGGLVAAGGQLTVIDKNHFSLMLPPYRPAQAKSDAHQTSTAEIAANTYQLIAVAFDNQGNQSNSETLRVVVQPPQVTAQGTFVISGDGARANGSDKIGVDFIIKDTNGNPLANREVVFHTNNGAQPGTITVTTDDNGIAHFDVTNTSAGTTHVSATFDDQTQGVDITFANAVNSVIVTGLVNGYPLVGTPFHAQVTCATGECPAS
Protein: Gamma-aminobutyric acid receptor subunit alpha-1 (GABA(A) receptor subunit alpha-1) (GABAAR subunit alpha-1) (P14867)
Organism: Homo sapiens (Human)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity. GABRA1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P08219}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cell membrane {ECO:0000269|PubMed:2465923, ECO:0000269|PubMed:25489750}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P62813}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Note=Mainly located in GABAergic synapses in granule cells, and also in the extrasynaptic membrane at a lower concentration. {ECO:0000250|UniProtKB:P62813}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit beta-1
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Chloride channel protein 2
Sequence:
MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ
Protein: Toll-like receptor 4 (B3U3W0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
Sequence:
MLNVFYLNFRCHIRQIENDAFYNVKNLTTLFLTGNPIIYFAPGCLNTLYNLQRLVLVDIGLESLQLNINNLTKLQELNVGTNYIQSMTLPPFMTTFKDFSLLDLHANNISIIRTDHTVVLREIGRNMTLILTWNPLLHIEPGAFKDVYLRQLDIRSAFVSFSAQKAALKALHGLNVKRLIFGKYREDNGFHFVDNDVLDGLCCFNFQEVSYYVLESAKTTIAIFRCMINATRITVKGGNIFKMETVHFHKTKELYLINNGLGTLPTKQLSHLHTLEKLEITHNSEPIFAEPFTDLPKLQYVDLSDNQLKIKHCCSTLLSGTPQINYLNLSLNSEISVDVGGFEGLDSLEILDFSYTRVVRIGYLSVLSNLKNLRYLDVSYSSVTFSNIFCFLGLSSLNVLKMAGNNFQGDVAKYIFNNLTLLEHLDMSFCHLVELHTSSFKYLQRLRHLNVKGNYLIKIDFLTHPNLKQLTSFYVEKNSITAIPLHVLKNLPMNLSEFDLSFNPIDCSCSQTDFMLWIINNQKVLKQPENILCKTISPNSDFRVTDFDIDHCVYKKKLIIVLPVFCVVFIVVLSILVYRFQFYLRYCWILLRGYRSPGQQECSYDAFVIFSSYDEAWVMNELMENLENGVPPIQLCLHMRDFQAGKSIASNIIDEGIMGSRKIIVVVSQHFIASAWCRFEFELAQSRFLMERNANIIIIILEDVAERKTKKILGLHKHLKKNTYLKWSRDPLSNMRFWIRLRKAIVATKQ
Protein: Pituitary vasotocin receptor (Q90YN1)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}.
Interaction partners:
Sequence:
MEPGWSWNSTHSSQTTHSTELQSSQPPAGTPNRTLLQGRDEQLARAEVGVLAAILLVATTGNLAVLLAVCRRGRKLSRMHLFVLHLALSDLGVALFQVLPQMLWEVTYRFAGPDLLCRAVKYLQVLSMFASTYMLMAMTLDRYVAVCHPLRTLRRPGRQPCAMVGAAWLLSCLLSTPQIFIFSLREVQPGSGVLDCWADFGYPWGARAYITWTTLCIFLLPVGILTACYSLICREICKNLKGKTQSCTPVAGGLLAASPSAPCCSQKGSQCPSGQPSRVSSVRTISRAKIRTVKMTFVIVVAYVACWAPFFSMQMWSVWDEDAPDDESADAAFTITMLLASLSSCCNPCIYMFFSGRPLQDTARCLALWGCPPSAPRRQGSAGSLCSRRTTILSHGLSAGIPLHRGSGTDLSPPEEEAVTESGTL
Protein: Nitrogen fixation nifHD region glnB-like protein 1 (P0CW44)
Organism: Methanococcus maripaludis (Methanococcus deltae)
Function: Could be involved in the regulation of nitrogen fixation.
Interaction partners:
Sequence:
MKMIRAVVRPSKAEEVVDALAESGCLALTKMDVIGRGKQKGIKIDQIYYDELPKTMLMLVVEDDTAENVIELITKTAYTGSFGYGKIFVSPVDEAYTVRTRSCGL
Protein: Immunoglobulin J chain (Joining chain of multimeric IgA and IgM) (P01591)
Organism: Homo sapiens (Human)
Function: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01592}.
Interaction partners:
- Polymeric immunoglobulin receptor
- Marginal zone B- and B1-cell-specific protein
- Immunoglobulin lambda-like polypeptide 5
- Something about silencing protein 10
- Interleukin-2
- B-cell antigen receptor complex-associated protein alpha chain
- Immunoglobulin lambda-like polypeptide 1
- Immunoglobulin heavy variable 4-38-2
- POU domain class 2-associating factor 1
- Tumor necrosis factor receptor superfamily member 17
Sequence:
MKNHLLFWGVLAVFIKAVHVKAQEDERIVLVDNKCKCARITSRIIRSSEDPNEDIVERNIRIIVPLNNRENISDPTSPLRTRFVYHLSDLCKKCDPTEVELDNQIVTATQSNICDEDSATETCYTYDRNKCYTAVVPLVYGGETKMVETALTPDACYPD