wanglab/gogpt-training-data huggingface dataset:
Protein: Toxin co-regulated pilus biosynthesis protein P (Toxin-coregulated pilus biosynthesis protein P) (Q93TT6)
Organism: Vibrio cholerae
Interaction partners:
Sequence:
MGYVRVIYQFPDNLWWNECSNQVYYAQDPMKPERLIGTPSIMQAKLLKILCEYHPSPCPNDQIIKALWPHGFISSESLTQAIKRTRDFLNDEHKTLIENVKLQGYRINIIQVIVSENIVDEADCSQKKSVKERIKIEWGKINVVPYLVFSALYVALLPVIWWSYGQWYQHELAGITHDLRDLARLPGITIQKLSEQKLMFAIDQHQCSVNYEQKTLECTKN
Protein: Homeobox protein cut-like 1 (CCAAT displacement protein) (CDP) (CDP/Cux p200) (Homeobox protein cux-1) [Cleaved into: CDP/Cux p110] (P39880)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in the control of neuronal differentiation in the brain. Regulates dendrite development and branching, and dendritic spine formation in cortical layers II-III. Also involved in the control of synaptogenesis. In addition, it has probably a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator.
Subcellular location: Nucleus {ECO:0000269|PubMed:15099520}.
Interaction partners:
- Golgin subfamily A member 5
- T-box brain protein 1
- RNA-binding protein EWS
- Cyclin-A1
- B-cell lymphoma/leukemia 11B
- Transcription factor SOX-2
- Eomesodermin homolog
- Secreted phosphoprotein 24
- Cyclin-A2
- Signal transducer and activator of transcription 3
Sequence:
MLCVAGARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQDFFSSSLASPSLPLASTGKFALNSLLQRQLMQSFYSKAMQEAGSTSMIFSTGPYSTNSISSQSPLQQSPDVNGMAPSPSQSESAGSVSEGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEPFHKMKQFLSDEQNILALRSIQGRQRENPGQSLNRLFQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKRELQVQKTAEPAQPSSASGSGNSDDAIRSILQQARREMEAQQAALDPALKQAPLSQSDITILTPKLLSTSPMPTVSSYPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAADCAQGVLRQVKNEVGRSGAWKDHWWSAVQPERRNAASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSKPTKPSVPPLTPEQYEVYMYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLNGELGQGVLPVQGQQQGPVLHSVTSLQDPLQQGCVSSESTPKTSASCSPAPESPMSSSESVKSLTELVQQPCPPIEASKDSKPPEPSDPPASDSQPTTPLPLSGHSALSIQELVAMSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREPFVRMQLWLNDPNNVEKLMDMKRMEKKAYMKRRHSSVSDSQPCEPPSVGTEYSQGASPQPQHQLKKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRELFIEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEPKSQGEAEREEVPRPAEQTEPPPSGTPGPDDARDDDHEGGPVEGPGPLPSPASATATAAPAAPEDAATSAAAAPGEGPAAPSSAPPPSNSSSSSAPRRPSSLQSLFGLPEAAGARDSRDNPLRKKKAANLNSIIHRLEKAASREEPIEWEF
Protein: Type 1 fimbrin D-mannose specific adhesin (Protein FimH) (P08191)
Organism: Escherichia coli (strain K12)
Function: Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
Subcellular location: Fimbrium {ECO:0000269|PubMed:1971261}.
Interaction partners:
- Chaperone protein FimC
- Outer membrane usher protein FimD
- Protein FimG
- Protein FimF
- Probable fimbrial chaperone SfmC
- Type-1 fimbrial protein, A chain
- Uncharacterized fimbrial-like protein SfmF
- Uncharacterized fimbrial-like protein SfmA
- Probable autotransporter YfaL
- Fimbrin-like protein FimI
Sequence:
MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ
Protein: Uncharacterized protein, isoform F (A0A0B4KEU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNSGRNHHRFDQTFLGATELDDELIKQLPKEVLLRVFSYLDVVSLCRCAQVCKYWNVLALDGSSWQKINLFDFQRDIEGPVIENISQRCRGFLKSLSLRGCQSVGDQSVRTLANHCHNIEHLDLSDCKKITDISTQSISRYCSKLTAINLHSCSNITDNSLKYLSDGCPNLMEINVSWCHLISENGVEALARGCVKLRKFSSKGCKQINDNAIMCLAKYCPDLMVLNLHSCETITDSSIRQLAANCHKLQKLCVSKCADLTDLTLLSLSQHNHLLNTLEVSGCRNFTDIGFQALGRNCKYLERMDLEECSQITDLTLAHLATGCPSLEKLTLSHCELITDDGIRHLTTGSCAAEILSVLELDNCPLITDRTLEHLVSCHNLQRIELFDCQLITRTAIRKLKNHLPNIKVHAYFAPGTPPAVTSGHRPRYCRCCEILXDTAIGFARKIMRKTATDXCWPVCIVMFAMVFSLTLVSMICMYLLGLLDAAMTTWPPDSN
Protein: Protein YIF1B (YIP1-interacting factor homolog B) (Q6PEC3)
Organism: Rattus norvegicus (Rat)
Function: Functions in endoplasmic reticulum to Golgi vesicle-mediated transport and regulates the proper organization of the endoplasmic reticulum and the Golgi (By similarity). Plays a key role in targeting to neuronal dendrites receptors such as HTR1A. Plays also a role in primary cilium and sperm flagellum assembly probably through protein transport to these compartments (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:18685031, ECO:0000269|PubMed:26077767}; Multi-pass membrane protein {ECO:0000255}. Note=Shuttles between the endoplasmic reticulum, the intermediate compartment and the Golgi apparatus. {ECO:0000269|PubMed:26077767}.
Interaction partners:
Sequence:
MHATGLAAPAGTPRLRKWPSKRRVPVSQPGMADPHQFFDDTSSAPSRGYGGQPSPGSLGYPTSSSEAAFLAAPMSNMAMAYGSSLAAQGKELVDKNIDRFIPVSKLKYYFAVDTVYVGKKLGLLVFPYLHQDWEVQYQQDTPVAPRFDINAPDLYIPAMAFITYILVAGLALGTQDRMIGGVLTGLLFGKIGYYLVLAWCCVSIFVFMIRTLRLKILAQAAAEGVPVRGARNQLRMYLTMAVAAAQPVLMYWLTFHLVR
Protein: Grf10p (A0A1D8PP44)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Bas1p
- Uncharacterized protein
Sequence:
MSPDSISSSVNQDLSTPTPPTSLSSTSTNSNTNASSGQKRIRATGEALEFLISEFETNPNPSPERRKFISDKAQMNEKAVRIWFQNRRAKQRKFERQMLRKETDSPGNYAGIYNTYTPNPPTVTTDMTNFNVNGSAGGATADFNDKLKNISSIPVEVNEKYCFIDCRSLSVGSWQRIKTGFHQSNLLTNNLINLAPVTLNQVMSNADLLIILSKKNLELNYFFSAISNNSRILFRIFYPLNAVVKCSLFDNNYYQNNNTNGTNSSDDNNISEIRLNLCQKPKFSVYFFNGSNTNNQWSICDDFSEGQQVSCAFAANDNSLPSNGKNQSFSNTIPHVLVGSTLSLQYLSQFILQHQQRQRQQQRQAQPQPQPQPHNQFDFNSQPFETIPTSAINNNFNTTKTVNSSSMQGFVPGDFQDLPAIYESISNSNHTTTTDLKDTNATTTTTNKHTPSSTTFTPQNLNGSNQSQTNVTYTNNYNESPFSIASTTNNNNTNSNRSNSQSHNPIFSDQLFYESSESASTNSPQFAMKKMNSETKLYINGNVSSNSSTNGPPLDDDNNLFDGVTRFTTTETSPEDDIIGMFTSQAHEPSAFELANGVTSSGSSYTHINNGSLTKSDKTFTGLSETSNNNNNTNGINFVDDFHVGNEFGDIDFEHHYSQDHHQQQQKNDNNNGNTNLDSFIDFEN
Protein: Long chain fatty acid elongase 2 (ELO-2) (EC 2.3.1.-) (Elongation of long chain fatty acids protein 2) (F11E6.5/ELO-2) (Long-chain 3-oxoacyl-CoA synthase 2) (CEELO2) (Q9XVQ9)
Organism: Caenorhabditis elegans
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. Uses malonyl-CoA to add 2 carbons per cycle to the chain of long-chain fatty acids. Condensing enzyme responsible for the elongation of palmitate (hexadecanoate, 16:0), also involved in polyunsaturated fatty acid (PUFA) biosynthesis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain 3-oxooacyl-coA reductase let-767
- Delta
- Delta
- Delta
- Delta
- Delta
- Omega-3 fatty acid desaturase fat-1
- Acetyl-CoA carboxylase
- Delta
- Long chain fatty acid elongase 6
Sequence:
MAAAQTSPAATLVDVLTKPWSLDQTDSYMSTFVPLSYKIMIGYLVTIYFGQKLMAHRKPFDLQNTLALWNFGFSLFSGIAAYKLIPELFGVFMKDGFVASYCQNENYYTDASTGFWGWAFVMSKAPELGDTMFLVLRKKPVIFMHWYHHALTFVYAVVTYSEHQAWARWSLALNLAVHTVMYFYFAVRALNIQTPRPVAKFITTIQIVQFVISCYIFGHLVFIKSADSVPGCAVSWNVLSIGGLMYISYLFLFAKFFYKAYIQKRSPTKTSKQE
Protein: Innexin (Q9N3R4)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
- Innexin-14
- Innexin-17
- Innexin
- Innexin-7
Sequence:
MTKAAVTSFTDPLKRIRGLESGTEKLLHNTTIAILVFLFILLASKPMFGSPIVCQVPKDWPSSSVDYFTDICYYGQREKVDIQHRISRAGGRGTVTVNLTTGTSEFYMWVPLVPILLVALCLLPAFFWKFVGLDCFNGMDIVSFLEFYEQTDDPGERLVEMEGWRRRKLAAQLNKWIMAKRNFFCGLSQTMIIYVLMKWFRTILFIAQFWIIADVFGDGNFFWGYADLARIANGDSINPLKGSFTLISGCRVQRLAMSIGFYRSYTNAHSAVARCMLSANFLNAKAFLVLYWWFLLVSFISLCSAIHYTIILLVPQYRRHEFKSMIRTEDHFIERYGEPHPNLHLGKEAPLEYLVEHLGNDGFLVVEMVYDMLHHYECDRFTEHIWMHIIVHNGEEDFEDDEIENKKIKIVDEMEMDGAGDRNSGGIDKKETNDWSSSAGTSKNKDSTSKVSLSASQPSMMMSESDEEPMISPAVFTSLSS
Protein: AT4G01090 protein (AT4g01090/F2N1_13) (Q9M155)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g01410 hydroxyproline-rich glycoprotein family)
- MATH domain and coiled-coil domain-containing protein At3g58220
- Protein PAL OF QUIRKY
- Protein kinase superfamily protein
- PRA1 family protein F1
- F19P19.6 protein
- Probable E3 ubiquitin-protein ligase RHY1A
- PRA1 family protein D
- Protein KINESIN LIGHT CHAIN-RELATED 2
- Potassium transporter 13
Sequence:
MRSRGDVSEAEGTRSDAGSSRSEEETSLKEKHSNSRAGSQRSGKSLRNDEPNYGSDSSSKNTSSSNNPIEYTEHERAELLRRLDSIKDHLLRGGGGGNNVVDKPKEPDQNQPFLRPVHLHGHANHNPGPSYYHQYPEPIQYPGPVHGMYPQAYQDPYGYQRRPPPVPNPNWYPPGHYPNQMARQYPGGQYVELGPDIVEPHSYYPATPGRYGDLPPYSPVSSHHREEKLATQYSDMPPYSPVSSHHRGEKLTTPYSPRVNNGSSFPSSMGTPGPRGGYARWPSEHDSEMGGAFARGYVKKAVSDTGVRRCHPLAGGAPFIACHSCFELLYLPKKKLLSQERLHKLQCGACSEVISFTIVDRKLVFSSGNEETKPVSLEVEDRNTTNTVVIEEEVSSVDFNSSGRDIPRKDEEEPVQELRNHQDTITTQSVRSESQHSDDEERSSNSSEQQQKEVKSVRRRGKGSKAPEPAAPDNASLLELFEYSNVNRAALAYGMAQLGYEKPDKQKSFMTQDSLKPESVATETEVSYNGYSNTEISEDSRYSNRKGSEYGSTEITTRSSTDQNEDQMKSLEVWVNGHLIPEDLVSSAEKLAGPIQAGKYWYDYRAGFWGVMGKPCLGIIPPFIEEFSHPMLDNCAAGNTDVFVNGRELHKRDFELLVGRGLPRDKNRSYIVDISGRILDQDSGEELHSLGKLAPTIEKVKHGFGMRVPRSLAS
Protein: KRAB-A domain-containing protein 2 (Q6ZNG9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSFLVPSLVSSPVLLKLLFSPGPKTIWSLWQQPMLFQEATAFENMTKDWNYLEGSQKDCYRDTMLDSYENTVPQGSFLQLSMMPQRAGNDPPGVSNASEMEMEISNMREKFLMSVTKLVESKSYNSKVFSKEKYFQTIKEVKEAKEKGKKSSRDYRRAAKYDVISVQGTEKLIEATHGERDRIRYYVHKEELFDILHDTHLSIGHGGRTRMLKELQGKYGNVTKEVIVLYLTLCKQCHQKNPVPKRGLAPKPMTFKDIDSTCQVEILDMQSSADGEFKFILYYQDHSTKFIILRPLRTKQAHEVVSVLLDIFTILGTPSVLDSDSGVEFTNQVVHELNELWPDLKIVSGKYHPGQSQGSLEGASRDVKNMISTWMQSNHSCHWAKGLRFMQMVRNQAFDVSLQQSPFEAMFGYKAKFGLYSSNLPRETVATLQTEEELEIAEEQLENSLWIRQEERAEIGADRSDMDDDMDPTPEASEPSTSQGTSGLLCW
Protein: Vascular endothelial zinc finger 1 (Q9Z162)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEANWTAFLFQAHEASHHQQQAAQNSLLPLLSSAVEPPDQKPLLPIPITQKPQAAPETLKDAIGIKKEKPKTSFVCTYCSKAFRDSYHLRRHQSCHTGIKLVSRAKKTPTTVVPLISTIAGDSSRTSLVSTIAGILSTVTTSSSGTNPSSSASTTAMPVPQSVKKPSKPVKKNHACEMCGKAFRDVYHLNRHKLSHSDEKPFECPICNQRFKRKDRMTYHVRSHEGGITKPYTCSVCGKGFSRPDHLSCHVKHVHSTERPFKCQTCTAAFATKDRLRTHMVRHEGKVSCNICGKLLSAAYITSHLKTHGQSQSINCNTCKQGISKTCMSEETSNQKQQQQQQQQQQQQQQQHVTSWPGKQVETLRLWEEAVKARKKEAANLCQTSTAATTPVTLTTPFNITSSVSSGTMSNPVTVAAAMSMRSPVNVSSAVNITSPMNIGHPVTITSPLAMTSPLTLTTPVNLPTPVTAPVNIAHPVTITSPMNLPTPMTLAAPLNIAMRPVESMPFLPQALPTSPPW
Protein: Large ribosomal subunit protein uL29m (39S ribosomal protein L47, mitochondrial) (L47mt) (MRP-L47) (Q08DT6)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9HD33}.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Uncharacterized protein.
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL19m
- Ribosomal protein
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL40
Sequence:
MAAASLAVFCRRVSAALKASTSLISSQTLASTGCRFSLSLLTKNTPNVTSFHQCRLLQTTLSRRGLEEFFDDPKNWGEEKVKSGASWTCQQLRNKSNEDLHKLWYVLLKERNMLLTLEQEAKRQRLPMPSPERLEKVVDSMDALDKVVQEREDALRLLQTGQEKPRPGAWRRDIFGRIIWHKFKQWPIPWYLNKRYNRKRFFAMPYVERFVRLRIEKQARIKARKISLTQKKEKFLQKKFPHLSEAQKSSAA
Protein: Protein LUC7 (Q07508)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Protein NAM8
- Nuclear cap-binding protein subunit 2
- Pre-mRNA-processing protein PRP40
- Small nuclear ribonucleoprotein-associated protein B
- U1 small nuclear ribonucleoprotein component PRP42
- U1 small nuclear ribonucleoprotein C
- 56 kDa U1 small nuclear ribonucleoprotein component
- U1 small nuclear ribonucleoprotein component SNU71
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MSTMSTPAAEQRKLVEQLMGRDFSFRHNRYSHQKRDLGLHDPKICKSYLVGECPYDLFQGTKQSLGKCPQMHLTKHKIQYEREVKQGKTFPEFEREYLAILSRFVNECNGQISVALQNLKHTAEERMKIQQVTEELDVLDVRIGLMGQEIDSLIRADEVSMGMLQSVKLQELISKRKEVAKRVRNITENVGQSAQQKLQVCEVCGAYLSRLDTDRRLADHFLGKIHLGYVKMREDYDRLMKNNRTTNASKTATTLPGRRFV
Protein: RxLR effector protein 54 (D0NBE6)
Organism: Phytophthora infestans (strain T30-4) (Potato late blight agent)
Function: Effector that specifically binds host autophagy protein ATG8CL of the ATG8 family to stimulate autophagosome formation and subsequent autophagy rather than blocking autophagic flux. The pathogen remodels host-microbe interface by co-opting the host autophagy machinery which plays a key role in plant immunity. PexRD54 competes with the autophagy cargo receptor Joka2 to deplete it out of ATG8CL complexes and interferes with Joka2's positive effect on pathogen defense.
Subcellular location: Secreted {ECO:0000269|PubMed:26765567}. Host nucleus {ECO:0000269|PubMed:26765567}. Host cytoplasm {ECO:0000269|PubMed:26765567}. Note=Localizes to host autophagosomes across the perimicrobial membrane. {ECO:0000269|PubMed:29932422}.
Interaction partners:
- Autophagy-related protein
- Seipin
- Seipin
- RxLR effector protein 24
- RxLR effector protein PexRD2
Sequence:
MRFQSIMMLTITCAGTCLAEGLAPSDQAYRPTMTGLKSRLNDPRPLSTATIATSSERFLRFDTVARDTAGNDEERVGPSWLAKVDGLMHKMVTSSLSAEEAQLKVWIQSQIHPRELFGVLSLGKRAAKLDDNPDFVQWLRLVKDFRANNGNQAFSDLDIYYLLLKTNSPEQLKLLFETLRHTPGMTKIGASMEKSLSGNWIRKALEQDTYPTIVYNTLRLKDAGTKLDDTPMFRQWLEYVEKYWNKNAGAFFGDTQMLTLFQKTMTEEEDIIKLVHMLRNNPGMKSHADKLERYLLLTSESSHKTMADVWLKARETPEEVFRILRLAEKQTAAADDNRMLNLWLRYTQTYRDKIDKNAFSDAEALQFFRKAKPLDFDWEIV
Protein: C->U-editing enzyme APOBEC-2 (EC 3.5.4.36) (mRNA(cytosine(6666)) deaminase 2) (Q9WV35)
Organism: Mus musculus (Mouse)
Function: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Interaction partners:
- Putative C->U-editing enzyme APOBEC-4
- Apolipoprotein B-100
- APOBEC1 complementation factor
Sequence:
MAQKEEAAEAAAPASQNGDDLENLEDPEKLKELIDLPPFEIVTGVRLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQAQATQGYLEDEHAGAHAEEAFFNTILPAFDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEGESKAFEPWEDIQENFLYYEEKLADILK
Protein: Indian hedgehog protein (IHH) (EC 3.1.-.-) [Cleaved into: Indian hedgehog protein N-product] (Q98938)
Organism: Gallus gallus (Chicken)
Function: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Both activities occur in the reticulum endoplasmic (By similarity).
Subcellular location: [Indian hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q14623}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=The N-product remains associated with the cell surface. {ECO:0000250|UniProtKB:Q15465}.; SUBCELLULAR LOCATION: [Indian hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15465}. Secreted {ECO:0000250|UniProtKB:Q14623}. Note=Co-localizes with HHAT in the ER and Golgi membrane. {ECO:0000250|UniProtKB:Q15465}.
Interaction partners:
- Protein patched homolog 1
- Patched 2.
- Hedgehog-interacting protein
- Cell adhesion associated, oncogene regulated.
- BOC cell adhesion associated, oncogene regulated.
- Growth arrest specific 1.
- Parathyroid hormone-related protein
- Protein smoothened
- LDL receptor related protein 2.
- Sonic hedgehog protein
Sequence:
MKPARLLLLLSGCALLLAPAVRCCGPGRVVGSRRRPPRKLIPLAYKQFSPNVPEKTLGASGRYEGKIARNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGMLARLAVEAGFDWVYYESKAHIHCSVKSEHSAAAKTGGCFPGRALATLENGARTPLWALRPGQRVLAMDGAGRPTYSDFLAFLDKEPRALTAFHVIETRQPPRRLALTPTHLLFVADNASAPAAQFRPTFASHVQPGHFVLVAVGSGGLQPAEVVGVRGRTDVGAYAPLTRHGTLVVDDVVASCFALVREQQLAQMAFWPLRLYHSLLGGPGVQGDGVHWYSGLLYRLGRMLLPPDSFHPLGAPRAES
Protein: PHD finger protein PERSISTENT TAPETAL CELL 1 (Q67V61)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcriptional activator required for tapetal programmed cell death (PCD) and degeneration, and pollen development in anthers.
Interaction partners:
- Os05g0214400 protein
- Os07g0190900 protein
- FHA domain containing protein, expressed
- Os02g0708600 protein
- Os02g0708500 protein
- Putative MYST-like histone acetyltransferase 1
- Os05g0469825 protein
- Os09g0530600 protein
- Os03g0607800 protein
- Os07g0405100 protein
Sequence:
MAPKMVISLGSSRRRKRGEMLFRFEAFCQPGYPANFAGAGGFRDNVRTLLGFAHLEAGVHGETKCWSFQLELHRHPPTVVRLFVVEEEVAASPHRQCHLCRHIGWGRHLICSKRYHFLLPRRESAAEADGLCFAINHGGGGGAEKASSKGTTTTASSRGHLLHGVVHLNGYGHLVALHGLEGGSDFVSGHQIMDLWDRICSALHVRTVSLVDTARKGHMELRLLHGVAYGETWFGRWGYRYGRPSYGVALPSYRQSLHVLGSMPLCVLVPHLSCFSQELPMVVTKYQAISGHKLLSLGDLLRFMLELRARLPATSVTAMDYRGIMSEASCRWSAKRVDMAARAVVDALRRAEPAARWVTRQEVRDAARAYIGDTGLLDFVLKSLGNHIVGNYVVRRTMNPVTKVLEYCLEDVSSVLPAVAAGGGVPAQGKMRVRFQLTRAQLMRDLVHLYRHVLKEPSQALTGGAFGAIPVAVRMVLDIKHFVKDYHEGQAAASSNGGGGFGHPHINLCCTLLVSNGSPELAPPYETVTLPAHATVGELKWEAQRVFSEMYLGLRSFAADSVVGVGADQEGLPVLGLVDVGSAVVVQGSVGEQINGEDHERKEEAAAAAVCEGSGGGERVVDCACGAVDDDGERMACCDICEAWQHTRCAGIADTEDAPHVFLCSRCDNDVVSFPSFNC
Protein: Serpin A12 (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin) (Q8R4Z1)
Organism: Rattus norvegicus (Rat)
Function: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q7TMF5}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Leptin
- Nicotinamide phosphoribosyltransferase
- Resistin-like gamma
- Resistin
- 30 kDa adipocyte complement-related protein
Sequence:
MNLVLGLGLFLAGLLTVKGLLQDRDAPDTYESPVRVQEWRGKKDARELTRHNMEFGFKLLQRLASNSRQGNIFLSPLSISTAFSMLSLGAQNSTLEEIREGFNFKEMSDRDMHMGFHYLLQKLNRETQDVKMSIGNALFMDQRLRPQQRFLKLAKNLYDADMILTNFQDLENTQKNINKYISRKTHNRIENMVKNIDPGTVMLLTNYIYFQGRWQYEFDPKQTKEEDFFIEEGKTVKVPMMFQRGMYDMAYDSQLSCTILEMPYRGNITATFVLPDSGKLRLLEQGLQADIFAKWKSLLSKRVVDVWVPRLHISATYNMKKVLSRLGISKIFEEHGDLTRISSHRSLKVGEAVHKAELRMNEKGTEGAAGSGAQTLPMETPRRMKLNAPFLMMIYENLMPSMIFLARIYNP
Protein: Nuclear membrane organization protein APQ12 (P40532)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport.
Subcellular location: Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Nucleus export protein BRR6
- Uncharacterized protein YJL049W
- Inner nuclear membrane protein SRC1
- Nucleoporin POM152
- Inner nuclear membrane protein HEH2
- Nucleoporin NUP188
- Nucleoporin POM34
- Nucleoporin NUP85
- Protein YOP1
- Nucleoporin NUP2
Sequence:
MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGIYMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK
Protein: Renal cancer differentiation gene 1 protein (Q504U0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25059753}.
Interaction partners:
Sequence:
MADPEELQVSSPPPPPPSSPSSSDASAASSPGGPVSLGWPVPSRSSGPTVDQLEEVELQIGDAAFSLTKLLEATSAVSAQVEELAFKCTENARFLKTWRDLLKEGYDSLKPDD
Protein: Uncharacterized protein, isoform E (Uncharacterized protein, isoform F) (Uncharacterized protein, isoform H) (Q9V4C1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDSTLNIEEKEIATKNETQIDYADEIKTTPQDNDNLNEKLLVSYIDSGFDKPVTSRDNKDDDDLKIEESESEDCNSEKKNTTDLEVNPAALIDKPSLDISSSDMERTVEIEDSESNNPIIIDASIKTDPLISVENLSTVSENNFELDLIDGSTNGENSSNAENESPVQDTSNILIKGEDDKAIENCKSQDTTKSSSEKNVNDPTSIASDLSAENTKADLVSLNEPNVNDQTSSASDLTAENTKADHDSLNKPKDFNNQILNIISDIDINIKAQEKITQLKEQELKLIQKQNDLANEIHKQQILAKQLSAQNQLKQNECQSGELDLHSQYQNERGGPTSTLYQEKNIASKESANVSKTVDLRKIFTPATDAAEILPKNRKLYASSAFYSPTLHPTVEDQVELARRISHSLSDISNQTSKGQSMYVNRKKRSDKWVHEGGSQGNDAINPFKENSETKSTMEVAKLEKIPLKLIMNPNGKVRDYNSLKDLINVEAGLLSPDNCAELITALQLHQGRGAELFAKRRRKADNWVVDESHSGTQYHPSGIPDFQQYQQRPVLSPNILPAYSDAGKHRVQLNIHQNQLIEKYSKPGLQVVQSPWKAALQTGSASSAFLEDTKSFSPPALTPIPSSQAGSKDWTDANEPMPHGSSRRNTNAVASSPRSVIVPSNPQRDLAYTPCVAQGWGGRSVELPKGLYVPKEISLSSYAAPSQQCEIHSKHFERPYEDTFPRTFPRNNYSANNNFPGNDGIGEFPLSKPTGLTTGTLHQQPYSPTSYKKTVPGLEKVENFARYEQPDRKRLTSGSPQYLNALQNSQVRNASPIPFGTSLNEQTSWPPRSVLLQGGSPSPLPNHVQTFNKCAKGWGSIPVKQQSYSSQYNLPGNLPYSDF
Protein: LD15107p (Q8T0A7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}.
Interaction partners:
Sequence:
MYNFLNADPKSVVIVQTGDSGGCTAATVICALLMYADLLREPEDAVQVFAVKRHTINLRPSEFRYLYYFGDILRPTPLLPHYKNTTLVSLSCQPVPRMTKARDGCRIYMEVYCNGNLLLSTLQDYEKMRLYQAGPGKIVLPINLTACGDVTVVLFHARKGMVRPQGLKICQFQFNTGFIPEPETLITFTNQDLDDLPDPEQVTPRFCVSLSLAVTDSESPPSHKPPWMPAKPKRSPAALFSSDLEYAEMLDNFVTKPSTRSSPPPGARKSDRVSSPLVLPDVTETAHELPSPMPEPSPPIDLLNLNQQPSDVPAADPLTSAKPSTDASFDLLGAFGDDDSTGIGSAPIPDILPPPPLQQPQPKINNDPFDIFGSVDQGGVPSMKPSGFPPFVGSLPTFVAQPAATTNPSPTHPARASADPFANIADLATGLNLNFNRSTLSGKSPVNTSPQPTQFSSPTHKPSPSSQPQATFMHTPPTPQTLPSTSSIRTPTQPQAVPAQSRPDYSRLHFDSQKAAQQPGTGGSKNSDIFADILGQQGYSFGSKMNQCPRSINEMRKEDLFKDMDPKKVRIMEWTDGKKNNIRALLCSMHTVLWDNAKWQRCEMSTMVTPTEVKKAYRRACLAVHPDKHNGTENEEIAKLIFMELNNAWTDFENDATQQNMFNA