wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium/calmodulin-dependent protein kinase type II subunit gamma (CaM kinase II subunit gamma) (CaMK-II subunit gamma) (EC 2.7.11.17) (P11730)
Organism: Rattus norvegicus (Rat)
Function: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (By similarity). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin (By similarity). In the central nervous system, it is involved in the regulation of neurite formation and arborization. It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity).
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQSSAPASPAASAAGLAGQAAKSLLNKKSDGGVKKRKSSSSVHLMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ
Protein: Expressed protein (Q8GWC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Gb|AAF32477.1
- TRAF-like family protein
- Uncharacterized protein At1g23150
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Nuclear envelope-associated protein 2
- RING-type E3 ubiquitin transferase
- Cyclin-dependent protein kinase inhibitor SMR16
- Forkhead box protein G1
- At1g53545
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
Sequence:
MAPSAAMLILSHPLVSHKAKNQSLSSPSSVKSTRVFGFLWPWKALDNEDHSAVVLGRLFGDPATIEKRFQEALEQSCW
Protein: Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3) (G3V6U9)
Organism: Rattus norvegicus (Rat)
Function: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery (By similarity). Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}. Nucleus {ECO:0000250|UniProtKB:Q91WC0}. Note=Localizes mainly in the cytoplasm. {ECO:0000250|UniProtKB:Q86TU7}.
Interaction partners:
- Histone-lysine N-methyltransferase SETD7
Sequence:
MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYTQIRALVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSILGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEEEVRCLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFQAGDQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKTVLKNPDLSVRATMAIKLRLGEKEILEKAVKSAAMNREYYRKHMEERAPLPRYEESDLGLLEGGVGDSRLPLVLRKLEEEAGVQESLSLTETVSKVKAAENGLVNGESLIPNGTRSENESLSPEESENTTGDTEESSGSMDAVKERL
Protein: Mitogen-activated protein kinase pmk-2 (EC 2.7.11.24) (Stress-activated protein kinase pmk-2) (p38 MAP kinase 2) (Q8MXI4)
Organism: Caenorhabditis elegans
Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11703092}.
Interaction partners:
- MAP kinase-activated protein kinase mak-2
- Dual specificity mitogen-activated protein kinase kinase sek-1
- Tyrosine-protein phosphatase vhp-1
- Forkhead box protein O
- Dual specificity protein phosphatase lip-1
- Protein skinhead-1
- Putative ribosomal protein S6 kinase alpha-2
- ETS domain-containing protein
- Dual specificity mitogen-activated protein kinase kinase mek-1
- Mitogen-activated protein kinase pmk-3
Sequence:
MGMSATMGDSASIPGVFFADFGPAPPEITPEGYHEVELNKTKWVLPQWYNSLKPLGEGAYGVVCTAEYEPTGDRVAIKKFFRPFQSTIHAKRTYRELKLLRTLQHDNVLEMIDVFTPDPDASSLNNVYFVSVLMGSDLQNIMKIQRLTDEQIQLLIYQVLRGLKYIHSAGIIHRDLKPSNIAVNERCEVKVFLSFSQLSFLILSFFKILDFGLARAQDAEMTGYVATRWYRAPEIMLNWMHYTQTVDVWSVGCILAELVSGRPLFPGDDHIDQLTKIMSVVGTPKEEFWSKIQSEEARNYIKNRSPIIRQDFVTLFPMASPYALELLEMMLILDPDRRISVSSALRHDYLREYSVPNDEPVAMDTVINSIVTIDPAEERATTLSDWRELIWNEIRLFQNSARRLSFVSCTDTEEEPMKI
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (P51008)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- coproporphyrinogen oxidase
- Outer membrane protein
- Protoporphyrinogen IX oxidase
- Protoporphyrinogen IX oxidase
- Coproporphyrinogen III oxidase, anaerobic 1
- Transcriptional activator protein FnrL
- cytochrome-c oxidase
- Cbb3-type cytochrome c oxidase CcoO subunit
- Cbb3-type cytochrome c oxidase subunit CcoP
Sequence:
MAAVSHLAKLGLFDARVPRYTSYPTAPNFGVGVTENLHADWISSIPAGGSISLYLHVPFCRRLCWFCACRTQGTSSDAPVRAYAAALKSELALLRARLAPGVRLARMHWGGGTPTLLPPTLIHELALAIRDAVPSDAETDFSVEIDPTEIDAARLDALFEAGMTRVSIGVQDFDPLIQQSIGREQSFELTQRLTEDLRHRGLMGLDADILYGLPHQTAPGVADSVQKLLSLSPDRVAVLGYAHVPAVSRRQLMIPTASIPGPEERLDLFETARTLILWDGYQQVGLDHFARAGDPLAHAHACGRLCRSFQGYTDDRAEVLIGLGASAISRFPQGFTQNAPSTSDHLRAIRSGRFSTARGHVLSDEDRLRGRMIEQLLCEFRISRAQILARFAVAPERLETLFRTCAAAFPGVVEITGHGLEILEEGRPLARIVARSFDRYDASGKPQGAI
Protein: Nucleolar pre-ribosomal-associated protein 1 (Unhealthy ribosome biogenesis protein 1) (P34241)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 60S ribosomal subunit formation and pre-rRNA processing. Required for normal accumulation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15208443, ECO:0000269|PubMed:15226434}. Note=Accumulates in the immediate vicinity of the dense fibrillar component of the nucleolus.
Interaction partners:
- 60S ribosome subunit biogenesis protein NOP8
- Nucleolar pre-ribosomal-associated protein 2
- ATP-dependent RNA helicase DBP6
- rRNA biogenesis protein RRP5
- Ribosome assembly protein 3
- ATP-dependent RNA helicase MAK5
- Ribosome biogenesis protein MAK21
- U3 small nucleolar RNA-associated protein 10
- Nucleolar complex protein 2
- ATP-dependent RNA helicase DBP7
Sequence:
MSNHSEAYGSRDQRREKYTQGKEFEDGTLETLESIISAVEDETLSKDYQPLIVFFQRGFGAQLVQTWSYYAQVNNHGKFSKTTSLLTKTLRVLSSDTSTVTIGSGLIRLILTDYTKVLYRGLNNMRAQLTNPILRLLKQIVNFNNGQHIEELVSYFDFSLPILPRLLVPSKSELANGNSSADSSKHDSLRFTFIKFWLTLISNASPFVRKELLTENFKIMSNLFKFMNKADSDKLSEHILSVFINDILKEKSFKRTTKTKILNELAASKIHHFYYSSNKNLVKKANEFFLTFGASRDFSVAFPDNCVWFKNSVADGASHGAPITVNQVEFQIHNKLLFNTLRLFKPWEDTLQLGTLIKILENVPELVAPYSIFLTTNGNYDPKMTSYWFGITLLINKIINLKIPQFMEKVDSNIPPATSLVIENILPSLLTKSSLVKSLQFETPIIRQLACQSIVLALKKLEKVSTFYDQKGWRNEKTILLNEFHTRIPDLPIFVSTLSNSLASNKDNRILPLSISIIFNYYSKMFPNLFSINLPSSNIYTDIMQKSKISGIEFAILDNYLQFQEFNSTQTRWWNPSSGGNSLFTLLLKLASSKNASNVITTRISNLLDELTRTNVIFNISLISPVMALVNSLQGLSLQVSEIDNMEQVWKWFDETISRVVKTPYKYVDMAKEYNYISPFIMCLSEQWKYVDKSGNPEFLIKWLILFLRNMIFIGEDHIGIDKLVKNVFPEVSDHDVNIYLKLDSFEENIKKTNSSNSLISSMKSSSFFQYISALPSKNLMNISRLPVNKLDAAGILFRVQLLVEDDSVVYDNWFEATACELTGKIASYMVTDTEFPIIKVLERYINFALPKLAIEKRNALLMKKSRFMCNLIGAVCFETGHQLVEFREIIQKVVFSGENVEEYANYNELYQKEDVNAFLTSVSEYLSTSALTSLLMCSTKLESTRNILQKLFNEGKTIKISLVKNILNKAANEDPASIKEVNISLAKFFEENKVCVDASSDPMGKLSLSETTSLINSFVSSDLNYLVLKAFYRWEHFSFPSFIPSIWRIKDSPLLSIVTTAALFKHMQDKDFSAFAHETISKYGNEIAKSTYTTSKSEIFDEILNMITTYIDFYDETKRNEILKCVLSQSDHKYHAATVRYIAAHNNFTYPGVETWLHKTLLYLTKYLSERKVISNSFFELLRAMAELLKLEEVPNKLNVKIINSQLEAILGSEWIKQIKVLEYVIVLIFCVSKKSIQSQRMVQLLLSNDSYSSIMIKDNDEDSSYRKFLSTMILFSLFSIDPVVNSTPIVQEKLLTFYSGTISSNDKLILKILETIESHTATSWTNMIFSWEFIKDEEEEILEAIGDTRLITKEREGLILTLQKNMIKKSIDRYVLERPQVPELYTDSNTNNYDATTRCDLVKKYYDDTERSGVDMYDPLFLLLLIIHNKELVKMVKDDEGNVTYRYEFENFLDCKIFQFIICSLSDCHTVANISYEHLSNLASSLEKKTAQMNLEKQITSKDNERKESDSDLIKYNSIYQVLIKRILYQRQQNQDPINPLIWFSISRIVDLLGSPTAPLHEKAYRWVLSNSTIRSWDIPMVSDVMMSYNKRQQDDNKKEIDMEIYYGELSWVLTTICKGIKTDEDYKMLEKKGVFEWLLNLINMPYLKERLRELIYFIFYKVQRVADDGGLNLISRNGIVSFFEVLNNNIKSRLPQDDILNNIGTLRNENRGTLNTTLRLAQEQNGIEKLLLGYNELVKSQKRLILWTEGDSDNVVKRLRK
Protein: LL-diaminopimelate aminotransferase (DAP-AT) (DAP-aminotransferase) (LL-DAP-aminotransferase) (EC 2.6.1.83) (O84395)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to use meso-diaminopimelate, cystathionine, lysine or ornithine as substrates.
Interaction partners:
- 4-hydroxy-tetrahydrodipicolinate reductase
- Diaminopimelate epimerase
- Aspartate semialdehyde dehydrogenase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- ABC transporter substrate-binding protein
- Bifunctional enzyme MurC/Ddl
- Aspartokinase
- 4-hydroxy-tetrahydrodipicolinate synthase
Sequence:
MKRNPHFVSLTKNYLFADLQKRVAQFRLENPQHTVINLSIGDTTQPLNASVAEAFASSIARLSSPTTCRGYGPDFGLPALRQKLSEDFYRGFVDAKEIFISDGAKVDLFRLLSFFGPNQTVAIQDPSYPAYLDIARLTGAKEIIALPCLQENAFFPEFPEDTHIDILCLCSPNNPTGTVLNKDQLRAIVHYAIEHEILILFDAAYSTFISDPSLPKSIFEIPDARFCAIEINSFSKPLGFAGIRLGWTVIPQELTYADGHFVIQDWERFLSTTFNGASIPAQEAGVAGLSILPQLEAIHYYRENSDLLRKALLATGFEVFGGEHAPYLWVKPTQANISDRDLFDFFLREYHIAITPGIGFGRSGSGFVRFSSLGKREDILAACERLQMAPALQS
Protein: Biopolymer transport protein ExbD (P0ABV2)
Organism: Escherichia coli (strain K12)
Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
Subcellular location: Cell inner membrane; Single-pass type II membrane protein.
Interaction partners:
- Protein TonB
- Biopolymer transport protein ExbB
- Ferrichrome outer membrane transporter/phage receptor
- Ferrienterobactin receptor
- Tol-Pal system protein TolQ
- Vitamin B12 transporter BtuB
- Fe
- Catecholate siderophore receptor Fiu
- Hydroxamate siderophore receptor FhuE
- Ferric siderophore reductase
Sequence:
MAMHLNENLDDNGEMHDINVTPFIDVMLVLLIIFMVAAPLATVDVKVNLPASTSTPQPRPEKPVYLSVKADNSMFIGNDPVTDETMITALNALTEGKKDTTIFFRADKTVDYETLMKVMDTLHQAGYLKIGLVGEETAKAK
Protein: Putative ciliary rootlet coiled-coil protein-like 1 protein (Ciliary rootlet coiled-coil protein pseudogene 2) (Q86T23)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLQAKKTEVAEALTKAEAGRMELELSVTKLRAEEASLQDSLSKLSALNESLAQDKLDLNCLVTQLEEEKAMLQGRQRQAEQEATVAPAEQEWLEELWLEQEVARQGLEGSL
Protein: NKD inhibitor of WNT-signaling pathway 3 (Uncharacterized protein isoform X2) (E7EZ18)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSLFTSVFRQLSACFTPSWGRRLSPQIADIGAEAGESKAMSTQKHRKVKSHHGHRPDKEGEGLKDQAEEEKQALSAENIQSTEREGGNGEPGGKKRKRRKLKNKKTLPLPVEVKPLPAPACFSSSPPVGDQPEHPDVLALPAAGLKPLLKDKESLPRLVEVKPLPASACFSSLTPVGDQPEHPEVLVLPASRLKALSPLSNPASRPQSPVEETDEVLPSSVIQVAPCVSPEPVLLPLQSSSEVASLCSIPSFSEPSLLQSPPETLPIPPIFAFDEVVSLVKPQASECSPSSGLMLFDFEDEELEFMEYTEEDIEAFYESEMKPRRMAAWLEQEEVTEVQKDGGKGASQVIQNPLNEVSRDEAFEELLIQAFCTGPPVYTEIKSRKKPKRNGPLVLFSLMEEKVKKKQEKKLRKEEERNERNLLRERYRNDPKLKHLCINKHNPNFCWS
Protein: Decaprenyl diphosphate synthase (DecaPP) (EC 2.5.1.86) (EC 2.5.1.87) (Decaprenyl pyrophosphate synthase) (Long-chain isoprenyl diphosphate synthase) (Trans,polycis-decaprenyl diphosphate synthase) (A0R0S4)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate (E-FPP or EE-FPP) is used in vitro, both primary products decaprenyl diphosphate and heptaprenyl diphosphate are synthesized. It is probably due to the fact that M.smegmatis synthesizes both (2E,6E,10E)-geranylgeranyl diphosphate (EEE-GGPP) and (2E,6E,10Z)-geranylgeranyl diphosphate (EEZ-GGPP). Can also accept many different allylic substrates, including E-geranyl diphosphate (E-GPP), neryl diphosphate (NPP), and all-trans-geranyl-geranyl diphosphate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11004176}.
Interaction partners:
- Uncharacterized protein
- DNA repair protein RecO
- 
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Hydrolase, nudix family protein
- Phosphatidate cytidylyltransferase
- amidase
- Polyprenyl synthetase
- Bifunctional short chain isoprenyl diphosphate synthase
- GTPase Era
Sequence:
MATTRGKKTYPQLPPAPDDYPTFPDKSTWPVVFPEIPAGTNGRFARPPQHTSKAAAPKIPADQVPNHVAVVMDGNGRWATQRGLGRTEGHKMGEAVLIDITCGAIEIGIKHLTVYAFSTENWKRSTEEVRFLMGFNREVVRRRRENLNDMGVRMRWVGSRPRMWRSVIKEFDIAEQMTVDNDVITINYCVNYGGRTEIVEAARALAQEAVDGKINPARISEAMFAKHLHRADIPDVDLFIRTSGEQRASNFLLWQAAYAEYVFQDKLWPDYDRRDLWAACEEYVNRNRRFGRA
Protein: Synaptoporin (Q8TBG9)
Organism: Homo sapiens (Human)
Function: Intrinsic membrane protein of small synaptic vesicles. Probable vesicular channel protein (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
Interaction partners:
- Synaptogyrin-1
- Synaptogyrin-2
- Synapsin-1
Sequence:
MCMVIFAPLFAIFAFATCGGYSGGLRLSVDCVNKTESNLSIDIAFAYPFRLHQVTFEVPTCEGKERQKLALIGDSSSSAEFFVTVAVFAFLYSLAATVVYIFFQNKYRENNRGPLIDFIVTVVFSFLWLVGSSAWAKGLSDVKVATDPKEVLLLMSACKQPSNKCMAIHSPVMSSLNTSVVFGFLNFILWAGNIWFVFKETGWHSSGQRYLSDPMEKHSSSYNQGGYNQDSYGSSSGYSQQASLGPTSDEFGQQPTGPTSFTNQI
Protein: Glucokinase (EC 2.7.1.2) (Glucose kinase) (ORF 3) (P0A4E1)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: A probable glucose kinase (Probable). Required for glucose repression of many different genes, restores glucose kinase activity in E.coli glk mutants.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0A6V8}.
Interaction partners:
- Sugar phosphotransferase
- Uncharacterized protein SCO2127
- Polyphosphate glucokinase
- Glucokinase
- Aldose 1-epimerase
- Phosphoglucomutase
- Sugar kinase
- Sugar kinase
- Glucose-6-phosphate isomerase 2
- Glucose-6-phosphate isomerase 1
Sequence:
MGLTIGVDIGGTKIAAGVVDEEGNILSTHKVPTPTTPEAIVDAIASAVEGARVGHEIVAVGIGAAGYVNRQRSTVYFAPNIDWRQEPLKEKVEARVGLPVVVENDANAAAWGEYKFGGGKGHRNVICITLGTGLGGGIIIGNKLRRGHFGVAAEFGHIRMVPDGLLCGCGSQGCWEQYASGRALVRYAKQRANATPERAEVLLALGDGTPDGIEGKHISVAARQGCPVAVDSYRELARWAGAGLADLASLFDPSAFIVGGGLSDEGDLVLDPIRKSYKRWLVGGNWRPVADVIAAQLGNKAGLVGAADLAREPDPIM
Protein: RH23455p (Q7JYX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI01423p
- RH17287p
Sequence:
MQGGQFTKQTDETGKVFIVTGANTGIGKETVLEIAKRGGTVYMACRDMNRCEKARQDIIRETNNQNIFSRELDLSSLESIRKFAAGFKKEQDKLHVLINNAGVMHCPRTLTKDGFEMQLGVNHMGHFLLTHLLLDVLKKTAPSRIVNVSSLVHTQGFIKTADLNSEKSYSRIGAYSQSKLANVLFTRELAKRLEGTGVTTNSLHPGAVDTELSRNWKFLKHPFAQLLLKPLLWVLFKTPRNGAQTTLYAALDPALKDVSGLYFSDCQPKEVSAAAQDDKTGKFLWAESEKWTGVNSTKVD
Protein: Annetocin receptor (Q75W84)
Organism: Eisenia fetida (Red wiggler worm)
Function: Receptor for annetocin. Activation by annetocin may induce egg-laying behavior through calcium-dependent signaling.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEMDDDEAILLDDIYALASTPNQTIVTSSFPQTVSPGFLARRNEALAMVEVAVQSTILILTVVGNAAVLAMIVSLSRHKDLGRMYTMIGHLSCADLFVAIFNLLPQLLWDVTHRFRGGRVLCKLVKYVQVVAMYASAYVLMSTAVDRYTAICHPMRSHTWTSTTAHYLVIGAWVLALVFAVPQLVIFDYVEVVPGSGVYDCVDHFRPRWTLPVYITWFALAVYVIPLVVLATIYLRICVVVWKSANRKSTPMINVAARTSGATEQPSLDDASVSFNVADGGGVDLDPSGGGGSLSRHAAQLSHRQQQQQANNVVLSRAKTKTVKLTLTVVISYLVCWAPFFVSHIWSAWDPHAPFEGTEMVITLLLGSLNSCINPWIYLAFSDQLRRKVTQCCPRSWGQRPSTLSHDSTDFRSGSRPTHS
Protein: Cbp/p300-interacting transactivator 4 (MSG1-related protein 2) (MRG-2) (Q96RK1)
Organism: Homo sapiens (Human)
Function: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances estrogen-dependent transactivation mediated by estrogen receptors. May function as an inhibitor of transactivation by HIF1A by disrupting HIF1A interaction with CREBBP. May be involved in regulation of gene expression during development and differentiation of blood cells, endothelial cells and mammary epithelial cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:15342390}. Cytoplasm {ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:15342390}.
Interaction partners:
- Histone acetyltransferase p300
- Transcription factor AP-2-alpha
- CREB-binding protein
Sequence:
MADHLMLAEGYRLVQRPPSAAAAHGPHALRTLPPYAGPGLDSGLRPRGAPLGPPPPRQPGALAYGAFGPPSSFQPFPAVPPPAAGIAHLQPVATPYPGRAAAPPNAPGGPPGPQPAPSAAAPPPPAHALGGMDAELIDEEALTSLELELGLHRVRELPELFLGQSEFDCFSDLGSAPPAGSVSC
Protein: Transcription factor CAULIFLOWER (AtCAL) (Agamous-like MADS-box protein AGL10) (Q39081)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that promotes early floral meristem identity in synergy with APETALA1, FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1. Positively regulates the APETALA1 and LEAFY expression.
Subcellular location: Nucleus.
Interaction partners:
- Protein LEAFY
- Protein TERMINAL FLOWER 1
- B3 domain-containing transcription factor VRN1
- Polycomb group protein VERNALIZATION 2
- Inactive protein FRIGIDA
- Protein TWIN SISTER of FT
- Squamosa promoter-binding-like protein 3
- CASP-like protein 4D1
- Floral homeotic protein APETALA 2
Sequence:
MGRGRVELKRIENKINRQVTFSKRRTGLLKKAQEISVLCDAEVSLIVFSHKGKLFEYSSESCMEKVLERYERYSYAERQLIAPDSHVNAQTNWSMEYSRLKAKIELLERNQRHYLGEELEPMSLKDLQNLEQQLETALKHIRSRKNQLMNESLNHLQRKEKEIQEENSMLTKQIKERENILRTKQTQCEQLNRSVDDVPQPQPFQHPHLYMIAHQTSPFLNMGGLYQEEDQTAMRRNNLDLTLEPIYNYLGCYAA
Protein: Regulator of CtrA degradation (Q9A3A9)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Cell cycle transcriptional regulator CtrA
- CpdR
- Sensor protein DivL
- ATP-dependent Clp protease proteolytic subunit
- Non-motile and phage-resistance protein
- Pilus assembly protein CpaA
- TadE-like domain-containing protein
- TadE-like domain-containing protein
- Pilus assembly protein CpaD
Sequence:
MTEVNAFADTPWRAGVIQDFARSELFDRTFEEGMQLVEETAAYLDGAGRHDSKVLSRNAALGYATESMRLTTRLMQVASWLLVQRAVREGEMPPEAACAEAYRLAEEAPADGPAVEELPFGLMNLLQRSERLYERVRHLDRRMYVESPNEEAPRPVQNQLDRLTAAFGG
Protein: Uncharacterized protein (Q54C82)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MPSVTVDYKVFMTHDHTNNTSIGTDGLATCIGIIARLNNGDTYCGHISNEIQGTTANLPIIMQRTQTIMTARLNPANVISVHCATTSTFPDTNAMYNAIVNTYPGLVQPKMEGTGIYWDGNAVGVINGLYDNINGNTEGTNDDQGPLNVTN
Protein: Partner of xrn-2 protein 1 (Q21738)
Organism: Caenorhabditis elegans
Function: Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA in complex with the exoribonuclease xrn-2. Stabilizes and enhances the accumulation and activity of the exoribonuclease xrn-2, and thus contributes to miRNA turnover.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:24462208}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24462208}.
Interaction partners:
- 5'-3' exoribonuclease 2 homolog
- 3'
Sequence:
MGKLEDVEAEKKLWESDDAWELRKAFMLAHYDDYPKIQLQCLSQLFINVTLLGCEYSQTLMQKIRTMGAGIAANKDRTKTGSYVKASAAKKRQAVKTSDLEGASDESKKVKMEKSPSPVARESFDERLGKLKASLAMTPHHLTGEQMMKTATNSCLMKWHVNKINQKIEITIDRYVAFRHTFSQYCVDPRDCAINTLIESILSCDAAVHEESYEIRFDGVPVDECYAKSVTRRLAKIKSAVSNGAHTVKGLTTYLDAVNMSMIQNTQKLEGWSQQLDLVTADLLLSSRVLSSTECTKPAMATIANQMSEDVCQLILNDKINVINSMKSHSSLAFQ
Protein: Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2) (GABAAR subunit alpha-2) (P23576)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain (By similarity). Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). 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 alpha2/beta2/gamma2 receptor exhibits synaptogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P26048}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P26048}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Cell projection, dendrite {ECO:0000250|UniProtKB:P26048}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit beta-1
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Vesicle-fusing ATPase
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid type B receptor subunit 1
- Gamma-aminobutyric acid receptor subunit gamma-1
Sequence:
MRTKLSTCNVWFPLLVLLVWNPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNSMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNPSDSVQVAPDGSRLNQYDLLGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKGSVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP
Protein: Cytoglobin (Nitric oxygen dioxygenase CYGB) (EC 1.14.12.-) (Nitrite reductase CYGB) (EC 1.7.-.-) (Pseudoperoxidase CYGB) (EC 1.11.1.-) (Stellate cell activation-associated protein) (Superoxide dismutase CYGB) (EC 1.15.1.1) (Q921A4)
Organism: Rattus norvegicus (Rat)
Function: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. Plays a role in the development of liver fibrosis. Has a peroxidase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14647402}. Nucleus {ECO:0000250|UniProtKB:Q8WWM9}.
Interaction partners:
- Neuroglobin
- Androglobin
Sequence:
MEKVPGDMEIERRERNEELSEAERKAVQATWARLYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSPQLRKHACRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVEPMYFKILSGVILDVIAEEFANDFPVETQKAWTKLRGLIYSHVTAAYKEVGWVQQVPNTTTLPATLPSSGP