wanglab/gogpt-training-data huggingface dataset:
Protein: Coiled-coil and C2 domain-containing protein 1A (Akt kinase-interacting protein 1) (Five prime repressor element under dual repression-binding protein 1) (FRE under dual repression-binding protein 1) (Freud-1) (Putative NF-kappa-B-activating protein 023N) (Q6P1N0)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses (By similarity). Plays distinct roles depending on its localization. When cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway. Repressor of HTR1A when nuclear. In the centrosome, regulates spindle pole localization of the cohesin subunit SCC1/RAD21, thereby mediating centriole cohesion during mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16033914}. Nucleus {ECO:0000250|UniProtKB:Q66HA5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000303|PubMed:20171170}.
Interaction partners:
- Charged multivesicular body protein 4c
- Neurotrypsin
- Charged multivesicular body protein 4a
- Charged multivesicular body protein 6
- Protein cereblon
- Charged multivesicular body protein 4b
- Vacuolar protein sorting-associated protein 4A
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 5
- Charged multivesicular body protein 3
Sequence:
MHKRKGPPGPPGRGAAAARQLGLLVDLSPDGLMIPEDGANDEELEAEFLALVGGQPPALEKLKGKGPLPMEAIEKMASLCMRDPDEDEEEGTDEDDLEADDDLLAELNEVLGEEQKASETPPPVAQPKPEAPHPGLETTLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPVAIGKGPASTPTYSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPGLAKPQMPPGPCSPGPLAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRTLLEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPPGFPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSGSAPTAKAPPKATSTRAQQQLAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAPVNKDDFALVQRPGPGLSQEAARRYGELTKLIRQQHEMCLNHSNQFTQLGNITETTKFEKLAEDCKRSMDILKQAFVRGLPTPTARFEQRTFSVIKIFPDLSSNDMLLFIVKGINLPTPPGLSPGDLDVFVRFDFPYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQTKGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVIDPVPAAVPTQVAGPKGKAPPVPAPARESGNRSARPLHSLSVLAFDQERLERKILALRQARRPVPPEVAQQYQDIMQRSQWQRAQLEQGGVGIRREYAAQLERQLQFYTEAARRLGNDGSRDAAKEALYRRNLVESELQRLRR
Protein: PMS1 homolog 2, mismatch repair system component (A0A2R8Y6S3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKEFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQLGQGKRQPVVCTGGSPSIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYGLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYHMYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDVNKLNVSQQPLLDVEGNLIKMHAADLEKPMVEKQDQSPSLRTGEEKKDVSISRLREAFSLRHTTENKPHSPKTPEPRRSPLGQKRGMLSSSTSGAISDKGVLRPQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTGCKFRVLPQPTNLATPNTKRFKKEEILSSSDICQKLVNTQDMSASQVDVAVKINKKVVPLDFSMSSLAKRIKQLHHEAQQSEGEQNYRKFRAKICPGENQAAEDELRKEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDENAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHIANLGVISQN
Protein: Adenine nucleotide alpha hydrolases-like superfamily protein (At2g03720) (Q9ZPQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQAIDETQRERNSRAHELVHPLKNFCQLKKPNVKTEIVVVETAEEKGKTIVEESKKQGAGVLVLGQRKRTSKWRVIWKWRTKGGMGGGVVEYCIHNSDCMAIAVRKKSNNGGYLITTKRHKDFWLLA
Protein: Zinc finger protein 670 (Q9BS34)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDSVSFEDVAVAFTQEEWALLDPSQKNLYRDVMQEIFRNLASVGNKSEDQNIQDDFKNPGRNLSSHVVERLFEIKEGSQYGETFSQDSNLNLNKKVSTGVKPCECSVCGKVFICHSALHRHILSHIGNKLFECEECPEKLYHCKQCGKAFISLTSVDRHMVTHTSNGPYKGPVYEKPFDFPSVFQMPQSTYTGEKTYKCKHCDKAFNYSSYLREHERTHTGEKPYACKKCGKSFTFSSSLRQHERSHTGEKPYECKECGKAFSRSTYLGIHERTHTGEKPYECIKCGKAFRCSRVLRVHERTHSGEKPYECKQCGKAFKYSSNLCEHERTHTGVKPYGCKECGKSFTSSSALRSHERTHTGEKPYECKKCGKAFSCSSSLRKHERAYMW
Protein: Enoyl-CoA delta isomerase 1, peroxisomal (EC 5.3.3.8) (Delta(3),Delta(2)-enoyl CoA isomerase 1) (AtECI1) (O04469)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Essential for the beta oxidation of unsaturated fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:18657232}.
Interaction partners:
- Enoyl-CoA delta isomerase 2, peroxisomal
- Enoyl-CoA delta isomerase 3
- Transmembrane protein
- Pseudouridine kinase
- ARP protein
- Probable receptor-like protein kinase At3g17420
- Acyl carrier protein 1, mitochondrial
- Peroxisomal adenine nucleotide carrier 1
- Peroxisomal 2,4-dienoyl-CoA reductase [
- Phospholipase A1-IIgamma
Sequence:
MCSLEKRDRLFILKLTGDGEHRLNPTLLDSLRSTINQIRSDPSFSQSVLITTSDGKFFSNGYDLALAESNPSLSVVMDAKLRSLVADLISLPMPTIAAVTGHASAAGCILAMSHDYVLMRRDRGFLYMSELDIELIVPAWFMAVIRGKIGSPAARRDVMLTAAKVTADVGVKMGIVDSAYGSAAETVEAAIKLGEEIVQRGGDGHVYGKMRESLLREVLIHTIGEYESGSSVVRSTGSKL
Protein: Probable zinc protease PqqL (EC 3.4.24.-) (P31828)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YddB
- NADH-quinone oxidoreductase subunit C/D
- Inner membrane ABC transporter ATP-binding protein YddA
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit E
- Acyl carrier protein
- NADH-quinone oxidoreductase subunit B
Sequence:
MEIIMRNLCFLLTLVATLLLPGRLIAAALPQDEKLITGQLDNGLRYMIYPHAHPKDQVNLWLQIHTGSLQEEDNELGVAHFVEHMMFNGTKTWPGNKVIETFESMGLRFGRDVNAYTSYDETVYQVSLPTTQKQNLQQVMAIFSEWSNAATFEKLEVDAERGVITEEWRAHQDAKWRTSQARRPFLLANTRNLDREPIGLMDTVATVTPAQLRQFYQRWYQPNNMTFIVVGDIDSKEALALIKDNLSKLPANKAAENRVWPTKAENHLRFNIINDKENRVNGIALYYRLPMVQVNDEQSFIEQAEWSMLVQLFNQRLQERIQSGELKTISGGTARSVKIAPDYQSLFFRVNARDDNMQDAANALMAELATIDQHGFSAEELDDVKSTRLTWLKNAVDQQAERDLRMLTSRLASSSLNNTPFLSPEETYQLSKRLWQQITVQSLAEKWQQLRKNQDAFWEQMVNNEVAAKKALSPAAILALEKEYANKKLAAYVFPGRNLSLTVDADPQAEISSKETLAENLTSLTLSNGARVILAKSAGEEQKLQIIAVSNKGDLSFPAQQKSLIALANKAVSGSGVGELSSSSLKRWSAENSVTMSSKVSGMNTLLSVSARTNNPEPGFQLINQRITHSTINDNIWASLQNAQIQALKTLDQRPAEKFAQQMYETRYADDRTKLLQENQIAQFTAADALAADRQLFSSPADITFVIVGNVAEDKLVALITRYLGSIKHSDSPLAAGKPLTRATDNASVTVKEQNEPVAQVSQWKRYDSRTPVNLPTRMALDAFNVALAKDLRVNIREQASGAYSVSSRLSVDPQAKDISHLLAFTCQPERHDELLTLANEVMVKRLAKGISEQELNEYQQNVQRSLDIQQRSVQQLANTIVNSLIQYDDPAAWTEQEQLLKQMTVENVNTAVKQYLSHPVNTYTGVLLPK
Protein: Solute carrier family 45 member 3 (Prostate cancer-associated protein 6) (Prostein) (Q8K0H7)
Organism: Mus musculus (Mouse)
Function: Proton-associated sucrose transporter. May be able to transport also glucose and fructose.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ETS domain-containing protein Elk-4
- ETS translocation variant 1
- Prostatic acid phosphatase
- Transmembrane protease serine 2
- ETS translocation variant 5
- ETS translocation variant 4
- High affinity immunoglobulin epsilon receptor subunit beta
Sequence:
MIQRLWASRLLRHRKAQLLLVNLLTFGLEVCLAAGITYVPPLLLEVGVEEKFMTMVLGIGPVLGLVSVPLLGSASDQWRGRYGRRRPFIWALSLGVLLSLFLIPRAGWLAGLLYPDTRPLELALLILGVGLLDFCGQVCFTPLEALLSDLFRDPDHCRQAFSVYAFMISLGGCLGYLLPAIDWDTSVLAPYLGTQEECLFGLLTLIFLICMAATLFVTEEAVLGPPEPAEGLLVSAVSRRCCPCHVGLAFRNLGTLFPRLQQLCCRMPRTLRRLFVAELCSWMALMTFTLFYTDFVGEGLYQGVPRAEPGTEARRHYDEGIRMGSLGLFLQCAISLVFSLVMDRLVQKFGTRSVYLASVMTFPVAAAATCLSHSVVVVTASAALTGFTFSALQILPYTLASLYHREKQVFLPKYRGDAGGSSGEDSQTTSFLPGPKPGALFPNGHVGSGSSGILAPPPALCGASACDVSMRVVVGEPPEARVVTGRGICLDLAILDSAFLLSQVAPSLFMGSIVQLSHSVTAYMVSAAGLGLVAIYFATQVVFDKNDLAKYSV
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-1) (Phospholipase C-delta-1) (PLC-delta-1) (Q8R3B1)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development. Binds phosphatidylinositol 4,5-bisphosphate (By similarity).
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Protein kinase C alpha type
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate multikinase
- Inositol polyphosphate 1-phosphatase
- Myotubularin
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MDSGRDFLTLHGLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADVQHWVQGLRKIIDRSGSMDQRQKLQHWIHSCLRKADKNKDNKMNFKEVKDFLKELNVQVDDSYARKIFRECDHSQTDSLEDEEIETFYRMLTQRAEIDRAFAEAAGSAETLSVEKLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMNQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMAHHLRAILGPMLLDQPLDGVTTSLPSPEQLKEKILLKGKKLGGLLPAGGENGPEATDVSDEDEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMVIYCKSVHFGGFSSPSTSGQAFYEMASFSESRALRLLQESGNSFVRHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPDTTFNSRALTQGPWWAPKKLRVWIISGQQLPKVNKNKNSIVDPKVIVEIHGVGQDVASRQTAVITNNGFNPRWDTEFEFVVAVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDLHPSATLFVKISIQD
Protein: Endothelin receptor type B (Endothelin receptor non-selective type) (Q9DGM2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Endothelin-3
- END domain-containing protein.
- Endothelin 1.
- Endothelin 2
- Endothelin-3a
- Guanine nucleotide-binding protein
- Guanine nucleotide-binding protein G
- Adenylate cyclase-inhibiting G alpha protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MRFQIIMETRCVFCFLFLLTEHIAVMSAQGKDFNQSRLSMGPLSPTQKSTIVIGNQINESMPRRPKVLPPMCTDPTEIRDTFKYINTVVSCLVFVVGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIMIDIPINVYKLLAKDWPFGVGLCKLVPFIQKTSVGITILSLCALSIDRFRAVSSWNRIKGIGVPKWTAIEIILIWVLSIILAVPEAIAFDMITMDYKGEQLRICLLHPKQRIKFMQFYKKAKDWWLFSFYFCMPLTCTAIFYTLMTCEMLRKKNGVQIALSDHIKQRREVAKTVFCLVLVFALCWLPLHLSRILQRTIYDERDPNRCELLSFFLVLDYIGINMASVNSCINPIALYMVSKRFKSCFRSCLCCWCLPPEILAMDDKQSCIKLKVTERGSAITAMSPTSILQIRH
Protein: Swi5-dependent recombination DNA repair protein 1 homolog (Meiosis protein 5 homolog) (Q86XK3)
Organism: Homo sapiens (Human)
Function: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination. Acts as a transcriptional modulator for ESR1.
Subcellular location: Nucleus {ECO:0000269|PubMed:23874500}. Note=Colocalizes with ESR1 in the nucleus. {ECO:0000269|PubMed:23874500}.
Interaction partners:
- DNA repair protein SWI5 homolog
- DNA repair protein RAD51 homolog 4
- DNA repair protein RAD51 homolog 3
- DNA repair protein XRCC3
- DNA repair protein RAD51 homolog 2
- DNA repair protein XRCC2
- DNA repair protein RAD51 homolog 1
Sequence:
MAEGEKNQDFTFKMESPSDSAVVLPSTPQASANPSSPYTNSSRKQPMSATLRERLRKTRFSFNSSYNVVKRLKVESEENDQTFSEKPASSTEENCLEFQESFKHIDSEFEENTNLKNTLKNLNVCESQSLDSGSCSALQNEFVSEKLPKQRLNAEKAKLVKQVQEKEDLLRRLKLVKMYRSKNDLSQLQLLIKKWRSCSQLLLYELQSAVSEENKKLSLTQLIDHYGLDDKLLHYNRSEEEFIDV
Protein: Proliferating cell nuclear antigen (B5X7E7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU000641}.
Interaction partners:
Sequence:
MFEARLVQGSILKKVLEALKDLITEACWDVSSSGISLQSMDSSHVSLVQLTLRSDGFDSYRCDRNLAMGVNLSSMSKILKCAGNEDIITLRAEDNADTLALVFETLNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVRMPSGEFARICRDLSQIGDAVMISCAKDGVKFSATGELGTGNVKLSQSSNVDKEEEAVTIEMNEPVQLIFALNYLNFFTKATPLSKTVILSMSADIPLVVEYKIADMGHIKYFLAPKIDEEAS
Protein: Malonyl-CoA decarboxylase, mitochondrial (MCD) (EC 4.1.1.9) (O95822)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10417274}. Mitochondrion matrix {ECO:0000269|PubMed:10417274}. Peroxisome {ECO:0000269|PubMed:10417274}. Peroxisome matrix {ECO:0000250|UniProtKB:Q920F5}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250|UniProtKB:Q920F5}.
Interaction partners:
- Acetyl-CoA carboxylase 1
- Malonate--CoA ligase ACSF3, mitochondrial
- Acetyl-CoA carboxylase 2
- Acetyl-CoA acetyltransferase, mitochondrial
- 5'-AMP-activated protein kinase subunit gamma-2
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
Sequence:
MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL
Protein: Solute carrier family 22 member 14 (Organic cation transporter-like 4) (ORCTL-4) (Q9Y267)
Organism: Homo sapiens (Human)
Function: Riboflavin transporter localized at the inner mitochondrial membrane of the spermatozoa midpiece, which is required for male fertility (By similarity). SLC22A14-mediated riboflavin transport is essential for spermatozoa energy generation and motility: riboflavin is the precursor of FMN and FAD, which are coenzymes of many enzymes in the TCA cycle (the citric acid cycle) in mitochondria (By similarity). Required for sperm motility and normal sperm flagellar structure (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:33882315}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q497L9}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the principle piece of the sperm tail. {ECO:0000250|UniProtKB:Q497L9}.
Interaction partners:
- Xylulose kinase
- Serine/threonine-protein kinase OSR1
Sequence:
MAGEENFKEELRSQDASRNLNQHEVAGHPHSWSLEMLLRRLRAVHTKQDDKFANLLDAVGEFGTFQQRLVALTFIPSIMSAFFMFADHFVFTAQKPYCNTSWILAVGPHLSKAEQLNLTIPQAPNGSFLTCFMYLPVPWNLDSIIQFGLNDTDTCQDGWIYPDAKKRSLINEFDLVCGMETKKDTAQIMFMAGLPIGSLIFRLITDKMGRYPAILLSLLGLIIFGFGTAFMNSFHLYLFFRFGISQSVVGYAISSISLATEWLVGEHRAHAIILGHCFFAVGAVLLTGIAYSLPHWQLLFLVGGILVIPFISYIWILPESPRWLMMKGKVKEAKQVLCYAASVNKKTIPSNLLDELQLPRKKVTRASVLDFCKNRQLCKVTLVMSCVWFTVSYTYFTLSLRMRELGVSVHFRHVVPSIMEVPARLCCIFLLQQIGRKWSLAVTLLQAIIWCLLLLFLPEGEDGLRLKWPRCPATELKSMTILVLMLREFSLAATVTVFFLYTAELLPTVLRATGLGLVSLASVAGAILSLTIISQTPSLLPIFLCCVLAIVAFSLSSLLPETRDQPLSESLNHSSQIRNKVKDMKTKETSSDDV
Protein: Vesicle transport protein (Q9LT07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363111}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363111}.
Interaction partners:
- Vesicle transport protein GOT1
- Trafficking protein particle complex subunit
- Peroxisome biogenesis protein 3-1
- Pentatricopeptide repeat-containing protein At1g15510, chloroplastic
- WRKY transcription factor-like protein
- Serine carboxypeptidase-like 33
- Peroxisome biogenesis protein 3-2
Sequence:
MDKMNQAIEKMKMLVGMEVEDEQQAADEESSLSFMEDLNRNCALTTKQRFYGFAICLSAGLTCTLLSMLVFFNPVKFGITFTLGNLMALGSTAFLIGPQRQVTMMLDPARIYATALYLASIIIALFCALYVRNKLLTLLAIILEFTGLIWYSLSYIPFARTMVSKIFMTCFDTEF
Protein: DCN1-like protein (Defective in cullin neddylation protein 1-like protein) (C9J0B2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKGSLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAW
Protein: E74 like ETS transcription factor 3 (Q5SR36)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAATCEISNIFSNYFSAMYSSEDSTLASVPPAATFGADDLVLTLSNPQMSLEEKASWLGEQPQFWSKTQVLDWISYQVEKNKYDASAIDFSRCDMDGATLCNCALEELRLVFGPLGDQLHAQLRDLTSSSSDELSWIIELLEKDGMAFQEALDPGPFDQGSPFAQELLDDGQQASPYHPGSCGAGAPSPGSSDVSTAGTGASRSSHSSDSGGSDVDLDPTDGKLFPSDGFRD
Protein: Histone H4 (P09322)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H2B-alpha
- Histone acetyltransferase type B subunit 2
- Histone H3.1/H3.2
- Histone acetyltransferase type B catalytic subunit
- Histone H2A-beta
- Histone chaperone cia1
- Histone H2A-alpha
- Histone acetyltransferase gcn5
- Histone H2A.Z
- Histone H3.3
Sequence:
MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALVYEETRAVLKLFLENVIRDAVTYTEHAKRKTVTSLDVVYSLKRQGRTIYGFGG
Protein: PTTG1 interacting protein b precursor (PTTG1-interacting protein b) (Pituitary tumor-transforming 1 interacting protein) (Pttg1ip protein) (Q5XJ41)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- PDZK1-interacting protein 1.
Sequence:
MIQTRTFLLSFVFFVFTFSVVVAQTAKSPVTNCTIKSNTTCEDCLKIVSCLWCISSQKCIDYPVNSVLPSHSVCPLSDARWGLCWMNFQILIITISVIAGVIVIAIFVCCFCCCKCENIGRSKRSEERMENQASLRKFRHEERKAEMKQRHDEMRLKYGLKKDNQYSRFENS
Protein: Phosphatidate phosphatase PAH2 (EC 3.1.3.4) (Phosphatidic acid phosphohydrolase 2) (AtPAH2) (Q9FMN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Magnesium-dependent phosphatidate phosphatase which catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol. Acts redundantly with PAH1 to repress phospholipid biosynthesis at the endoplasmic reticulum (ER). May function indirectly as repressor of multiple enzymes involved in phospholipid biosynthesis. Is involved in the pathway of galactolipid synthesis in the ER, which is required for the membrane lipid remodeling, an essential adaptation mechanism to cope with phosphate starvation.
Subcellular location: Cytoplasm, cytosol.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 1
- Lipid phosphate phosphatase 1
- Putative lipid phosphate phosphatase 3, chloroplastic
- Probable lipid phosphate phosphatase 4
- Triacylglycerol lipase SDP1L
- Lipid phosphate phosphatase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Diacylglycerol O-acyltransferase 3
- Monogalactosyldiacylglycerol synthase 2, chloroplastic
Sequence:
MNAVGRIGSYIYRGVGTVSGPFHPFGGAIDIIVVEQPDGTFKSSPWYVRFGKFQGVLKNGRNLIRIDVNGVDSGFNMYLAHTGQAYFLREVEDVVGESESGEVYTLSSGDEAETTSRDDVVDKVKIPLKSRSCNYDSPSPRTGNGKIVGKPGILGYVFGGRSVRESQDCGVERAEIAADLLEVKWSTNIDTRKRGKGMSSESLDGKDYGESTSTSGKSCVEGSSEMLVDSDSILETPLVASPTLRFLDEKEQDFRESTNVEDYCEEDGSSGVVVENGLCEASSMVFSVTSEGSGNVEIFVEPRTEALAEDAVSGSDLDSKQELLRAPESVEIATLGSADQADMGSIGTSQEGSSTGSPVQDENKITIKDMHISAGDFEKSQSASGESILQPEIEEEQFSFSDLDECKPGGNSSVGSSSSDTVKVDGKESYDETKTSPEKGVENTMALSEPINIERKKDIFTDEMERLVGSLPIMRLQNNDDMDASPSQPLSQSFDPCFNTSKLDLREDESSSGGLDAESVAESSPKLKAFKHVIANPEVVELSLCKHLLSEGMGAEAASQAFNSEKLDMEKFASLGPSILENDKLVVKIGGCYFPWDAAAPIILGVVSFGTAQVFEPKGMIAVDRNEKPGDVLAQGSGSWKLWPFSLRRSTKEAEASPSGDTAEPEEKQEKSSPRPMKKTVRALTPTSEQLASLDLKDGMNSVTFTFSTNIVGTQQVDARIYLWKWNSRIVVSDVDGTITRSDVLGQFMPLVGIDWSQTGVTHLFSAVKENGYQLIFLSARAISQASVTRQFLVNLKQDGKALPDGPVVISPDGLFPSLFREVIRRAPHEFKIACLEEIRGLFPPEHNPFYAGFGNRDTDEISYLKVGIPRGKIFIINPKGEVAVNRRIDTRSYTNLHTLVNRMFPATSSSEPEDFNTWNFWKLPPPSLM
Protein: Arginine/agmatine antiporter (P60061)
Organism: Escherichia coli (strain K12)
Function: Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (Probable). Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Probably undergoes several conformational states in order to translocate the substrate across the membrane; keeps the substrate accessible to only 1 side of the membrane at a time by opening and closing 3 membrane-internal gates (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:12867448}; Multi-pass membrane protein {ECO:0000269|PubMed:21368142}.
Interaction partners:
- Biodegradative arginine decarboxylase
- HTH-type transcriptional regulator AdiY
- Glutamate decarboxylase alpha
Sequence:
MSSDADAHKVGLIPVTLMVSGNIMGSGVFLLPANLASTGGIAIYGWLVTIIGALGLSMVYAKMSFLDPSPGGSYAYARRCFGPFLGYQTNVLYWLACWIGNIAMVVIGVGYLSYFFPILKDPLVLTITCVVVLWIFVLLNIVGPKMITRVQAVATVLALIPIVGIAVFGWFWFRGETYMAAWNVSGLGTFGAIQSTLNVTLWSFIGVESASVAAGVVKNPKRNVPIATIGGVLIAAVCYVLSTTAIMGMIPNAALRVSASPFGDAARMALGDTAGAIVSFCAAAGCLGSLGGWTLLAGQTAKAAADDGLFPPIFARVNKAGTPVAGLIIVGILMTIFQLSSISPNATKEFGLVSSVSVIFTLVPYLYTCAALLLLGHGHFGKARPAYLAVTTIAFLYCIWAVVGSGAKEVMWSFVTLMVITAMYALNYNRLHKNPYPLDAPISKD
Protein: Ubiquitin-protein ligase, putative (EC 6.3.2.-) (Q580A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
- Ubiquitin-like modifier-activating enzyme 5
- E3 ubiquitin-protein ligase
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- E2 ubiquitin-conjugating enzyme
- Ubiquitin fusion degradation protein 2, putative
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2, putative
Sequence:
MFLSLDVTPSRAPYDLLSDLCTLLIIAGDSTDVPLQPLIRAIDMALTKGSSSGDVMVMAARAIVIILDRLSGSLFSLDTRNGLDTFRKCFSTVVSMVDMQKRESLHFEKSSEGELKEEVLQCLSLSSKCCELAVVVPSTEEQIQFCLAAVDGSKRTSCKVLHHSIGLMRQKELKSATDCRALEQLVHHHLMALFHLDIDHEWDELLRTVVEGILTYRAWCAPRVLSPDRQGGKHRRGSEEGGASSSSTHITSLRNMMVTLLQIGERIAGSGTASSRVQLTLACLASVIETHLLPREACESAMLWLAQLLLRSEVRSASFSNPFNSGSDSVAVNAEQPWIDSTPTLPNLRWVVPSLLWSALVLLAKLCGANFNFQSEYIWAWRGRDDEYHLYIKKVRRRLTTMYFSAERSRIVAPGRHVIDLQTMTDNFAHGDTASRVHFQPIPCAISFDGGLAIPTRGMMLKKKVCAAVQDALRPLSFGHTQVASLARSIRFYIICSGDPTNTMDVITAFCSLPADQKEPTVGEICATLLKRDKRWASVLQEAGVADTPAAECLARDGGKKNRIESSTSEVKRGADCLREVQRSPGNVLAFLRTTSSSELLAFVQGLEKSPYGEEQMMALCEEMKKDDVLASRMRTVAQTYVLRVLHHTASCKPVGEDLAERVRSTSYTVNICSAGDRIKGKGAPRCPNGHALRVHFSVNWRCDSCAFANAFGSLACRDCNYDLCSNCVDEKLSRMETNSSAVVGDVIQSWKALKLKRSPSTSSTSSQKRKSGCSGNAGEVMLFTSSGVVPASRPVSLLEGNDVHIAPVGGECRCCIPCPPFVACSAAHNIAEHSSLRVFLHTFLATRPQRWVDTAVELSIVNALESRGEDIFLSGVSGIPSRVVLILQEVAPYISLAFKRNMAHFLAVGCCRFGLYHLQDVGVNVRGTVTGSIASNGLAFKVTVKRNTESITNTLYKVFLEYPTLRNKVEFNFEGEEGTGEGPTQELYAELSRRYRSMSELWHHRDDGVCIAFPSMQQVHPKRFFVLGASCGRAFADGYTMDISLLPVVWPLIRSQTPSVEVLWHLLEEVEPALANSYKCVLQATDAELEQMGLEDEETGEALTVSTAKFYVEKCVERRLTNAVSNLHWFARGLASVVDLDAFWFFTDDEMSAIICGFSAEDSEEKLFSEEALRAAVMEAHGYSTGSQEVETFISLVGDEFTREQQQLFIEFLTGCPQLPLNGLDGLGRKITVVRKELEGRGEQTLPSCNTCFLYFKLPPYSTRKIMKERLLVAITEGRRNFSLS