wanglab/gogpt-training-data huggingface dataset:
Protein: Type-1 angiotensin II receptor-associated protein (AT1 receptor-associated protein) (Q9WVK0)
Organism: Mus musculus (Mouse)
Function: Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalization as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in angiotensin II-stimulated transcriptional activity. May play a role of negative regulator in cardiomyocyte hypertrophy induced by angiotensin II through an inhibition of p38 mitogen-activated protein kinase pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Present in perinuclear vesicular membranes, Endoplasmic reticulum, Golgi and endocytic vesicles. {ECO:0000250}.
Interaction partners:
- Angiotensinogen
- Angiotensin-converting enzyme
- Type-1 angiotensin II receptor A
- Renin-1
- Proto-oncogene Mas
- Angiotensin-converting enzyme 2
- Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1
Sequence:
MELPAVNLKVILLVHWLLTTWGCLVFSSSYAWGNFTILALGVWAVAQRDSIDAIGMFLGGLVATIFLDIIYISIFYSSVATGDTGRFGAGMAILSLLLKPFSCCLVYHMHRERGGELPLRPDFFGPSQEHSAYQTIDSSSDAAADPFASLENKGQAVPRGY
Protein: RNA polymerase sigma factor SigA (Sigma-66) (Sigma-70) (Sigma-A) (P18333)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- RNA Polymerase Sigma-54
- DNA primase
- dihydrofolate reductase
- Chaperone protein DnaK
- Folate synthesis bifunctional protein
- Probable dihydroneopterin aldolase
- Coenzyme F420:L-glutamate ligase-like domain-containing protein
Sequence:
MRMDTLDSQAAEAAQEEEIQRKLEELVTLAKDQGFITYEEINEILPPSFDTPEQIDQVLIFLAGMDVQVLNQADVERQKERKKEAKELEGLAKRSEGTPDDPVRMYLKEMGTVPLLTREEEVEISKRIEKAQVQIERIILRFRYSTKEAVSIAQYLINGKERFDKIVSEKEVEDKTHFLNLLPKLISLLKEEDAYLEERLLALKDPALSKPDQARLNDELEKCRIRTQAYLRCFHCRHNVTEDFGEVVFKAYDSFLQLEQQINDLKARAERNKFAAAKLAAARRKLHKREVAAGRTLEEFKKDVRMLQRWMDKSQEAKKEMVESNLRLVISIAKKYTNRGLSFLDLIQEGNMGLMKAVEKFEYRRGYKFSTYATWWIRQAVTRAIADQARTIRIPVHMIETINKVLRGAKKLMMETGKEPTPEELGEELGFTPDRVREIYKIAQHPISLQAEVGDGGESSFGDFLEDTAVESPAEATGYSMLKDKMKEVLKTLTDRERFVLIHRFGLLDGRPKTLEEVGSAFNVTRERIRQIEAKALRKMRHPIRSKQLRAFLDLLEEEKIGSGKIKSYKN
Protein: Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (CD antigen CD321) (O88792)
Organism: Mus musculus (Mouse)
Function: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (By similarity). Involved in platelet activation (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:11036763}. Cell membrane {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of both epithelial and endothelial cells.
Interaction partners:
- Tight junction protein 1
- Occludin
- Afadin
- Tight junction protein 2
- Integrin alpha-L
- Cingulin
- Rap guanine nucleotide exchange factor
- Junctional adhesion molecule B
- Integrin beta-2
- Partitioning defective 3 homolog
Sequence:
MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV
Protein: (S)-8-oxocitronellyl enol synthase (EC 1.3.1.122) (7-epi-iridoid synthase) (EC 1.3.1.123) (Iridoid synthase) (AmISY) (A0A221J5P3)
Organism: Antirrhinum majus (Garden snapdragon)
Function: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Reduces 8-oxogeranial, generating an unstable product that is subsequently cyclized into several possible products, either non-enzymically or by dedicated cyclases. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities.
Interaction partners:
Sequence:
MSWWYRRSIGETEQKRIEINGVSPTYQSVALIVGVTGIAGSGLAETLSFSDTPGGPWKVYGVARRPCPKWLAKLNVNYVQCDIANTDETYSKVAPLTDITHIFYVSWTGSEDVALNTLMFKNILDSVIPNAPNLKHVSLQTGIKYYWGNMAEMDSTNQPHECPFYENMPRLKQDNFYYNLEDLVYDSAVRKNGLSWSIHRPALIFGFSPCSMMNTVSTLCVYAAICKHENKPLVYTGTETSWTCLWDAVDSDLLAEHFLWAATVPNAKNQAFNINNGDVFKWKHMWKVLAKEFDIEAIGYEGKEPVLLEDLMKDKDSVWDEIVKKHDLVPTKLRDIAAFWLADVVFRNKETLCSMNKNKEFGFMGFRDTTKSFVSSINKMRDFKFIP
Protein: Chromo domain-containing protein (Q54RQ4)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Origin recognition complex subunit 2
- Histone H3.3 type b
- Histone H3.3 type a
- Histone H3.3 type c
Sequence:
MGKRDKKIIIEEPEELEEAEDVFEVEKILDKRVQHGRIQYNVRWIGFSSDYDTWEDEDNVAGCPELVKEFESSRQQEKKKSKKRKHTIINDDPTAVEISSSSSPPTTKPSSSTTAAAPASSSASVTTKTATATVTTDTYFSNNTTSTHQKTNHSVEVEENIKNEYIKFGVPYIEGVGFENGHCVEEVIGCKPFGQDNTLFFFVKWRDQEKLSWVPNEILKHKEPLQLIEFYESRLKFGYSGQPS
Protein: Gamma-aminobutyric acid receptor subunit alpha-5 (GABA(A) receptor subunit alpha-5) (GABAAR subunit alpha-5) (Q8BHJ7)
Organism: Mus musculus (Mouse)
Function: Ligand-gated chloride channel subunit which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. May be involved in GABA-A receptor assembly, and GABA-A receptor immobilization and accumulation by gephyrin at the synapse.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P31644}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P31644}. Cell membrane {ECO:0000250|UniProtKB:P31644}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P31644}.
Interaction partners:
- Trafficking protein, kinesin binding 2
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Huntingtin-associated protein 1
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit gamma-2
Sequence:
MDNGMLSRFIMTQTLLVFCISMTLSSHFGFSQMPTSSVQDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVRTDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASKIWTPDTFFHNGKKSIAHNMTTPNKLLRLEDDGTLLYTMRLTISAECPMQLEDFPMDAHACPLKFGSYAYPNSEVVYVWTNGSTKSVVVAEDGSRLNQYHLMGQTVGTENISTSTGEYTIMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKKALEAAKIKKKERELILNKSTNAFTTGKLTHPPNIPKEQPPAGTANAPTVSIKASEEKTAESKKTYNSISKIDKMSRIVFPILFGTFNLVYWATYLNREPVIKGATSPK
Protein: Formin-H (Diaphanous-related formin dia2) (dDia2) (Q54N00)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Formins play an important role in the nucleation of actin and the formation of linear actin filaments. Important for cell migration and formation, elongation and maintenance of filopodia. Specifically controls filopodial dynamics by regulating actin turnover at the barbed ends of actin filaments.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:15908944}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15908944}. Note=Enriched at the tips of filopodia. The N-terminus of the protein targets the protein to the cell cortex and the FH1/FH2 region refines the localization specifically to filopodial tips.
Interaction partners:
- Profilin-2
- Protein VASP homolog
Sequence:
MSFDLESNSSGGSTIGRNSSIRLSSGLAPSESTVSLNEIIDLDREFELLLDKLAIEDPIKRKQMQSLPDISKRTLLEQNKADIYRTVKHKGPIESFADVKSVISSINTKHVPIDIIKTLRIHLNTADRDWIQSFLDNDGVQPILNILKRLERNKNRKRKEHSILQWECTRCIAALMKIKIGMEYIASFPQTTNLMVLCLDTPLIKAKTLVLELLAAIAVTDRGHGAVLTSMIYHKEVKKEITRYFNLVQSLKIEKNAEYLTTCMSFINCIISSPSDLPSRIEIRKAFLNLKILKYIENLRADYNEDKNLLTQLDVFEEELSTDEQLNSQQGTQIGIEDLFSQISSRVTGTPSQQELITLMTHFQRMSSSNLGLGVWTLYNALANQLEDELKIHPDLDVTLVSLLFPEVKKSSSGLFGFGSKSKSPSSSPALSSMAKTELKKDNEEKQKTIEHLLKQLNKFSGGQNTERWMIEREEKNKLIAQLMAQTKNGGGGGGGGVGGDSSLSNDEALKRENQLLRMEIENIKNNPSVLLNSGNSINGDVPNLFISSPGSTLSPSPSGEPPIPSTDFGITSSSIHTSTDKLTNSTEPILGSPPPPPPPPMSGGGGPPPPPPPPGGKSNKPAKPIIKPSVKMRNFNWITIPALKVQGTFWDKLDETSFIQSLDKVELESLFSAKAPTVKVESKQLTRKVVVTVIDMKKANNCAIMLQHFKIPNEQLKKMQIMLDEKHFSQENAIYLLQFAPTKEDIEAIKEYQGDQMQLGAAEQYMLTVMDIPKLDSRLKAFIFKQKFEGLVEDLVPDIKAIKAASLELKKSKRLSDILKFILAIGNYVNGSTTRGGAFGFKVLETLPKMRDARSNDNKLSLLHFLAKTLQDRIPEIWNIGAELPHIEHASEVSLNNIISDSSEIKRSIDLIERDFVPMINDPLFAHDKHWIHKITEFQKIAKVQYQRIEKEIDEMNKAFEEITSYFGEPKSTQPDVFFSTINNFLEDLEKAYGEYQAMIRKAELENSKMEDPEKGGLQDLSSQIRSGQLFKDRRVGDSVIAQMQNVDSLRKNLKSTSTTTPNTPPTIKIELPSQSILKPSGQLKK
Protein: Cdr4p (A0A1D8PE84)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- ATP-binding cassette transporter
- Ife2p
Sequence:
MADADTSSNSSKTNEDRSQEGFGTYQGYTDRVASEVQELARIISHASIQQLKLKRQHSRQESQKSNEQESELSGKLGVIPVDENGNFVDQRLNPNSPEFNAAYWIQNAHKLVSSDIDYFKPVTIGVAYKNLRAYGSASDADYQSTLVNLIPKYLSLFFREYILRHTGPTFDILKPMDGLIKPGELTVVLGRPGAGCSTFLKTIASQTYGYHIDKDSVIRYNSLTPHEIKKHYRGEVVYCAETENHFPQLTVGDTLEFAAKMRTPQNRPLGVSRDAYARHLAAVVMAVYGLSHTRNTKVGNDFIRGVSGGERKRVSIAEITLNNAMVQCWDNSTRGLDSATALEFIRALKASADIVHTTPLVAIYQCSQDAYDLFDKVVLMYQGYQIYFGSAKKAKQYFIDMGYECPQRQTTADFLTSLTNPAERIVRQGFEGKVPQTPQEFYEYWKKSPEGQQIVADVDQYLTEHSSAAEKEAIKEAHQARQSDHLKPASPYTVSFFMQVRYIAHRNILRIKGNPSIHLFQIFGNIGMSFILSSIFYNLPTATSSFYHRTAALFFAVLFNAFSCLLEIFSLYEARSIVEKHKKYALYHPAADAFASIVTELPTKFIIAIGFNLVYYFMVNFRRTPGNFFFYLLINFSATLAMSHIFRTIGAATKTLQEAMTPAAILLLALTIFTGFVIPTPNMHGWCRWINYLDPLAYAFESLIANEFHNRDFECSQYVPSGGSYPTAGPNRICTPVGSVPGQDFVDGTRYMEMSFDYRNSHKWRNFGIVIGFIVFFFCTYILLCEINKGAMQKGEILLFQQRALKKRKKANNDIESGEIEKVTPEFDNEYENNQDKMLQSGGDTFFWRDLTYQVKIKSEDRVILDHVSGWVKPGQVTALMGASGAGKTTLLNALSDRLTTGVVTEGIRLVNGRPLDSSFQRSIGYVQQQDLHLETSTVREALEFAAYLRQPKSVSRKEKNEYVDYIIRLLEMEQYADAVVGVSGEGLNVEQRKRLSIGVELVAKPKLLVFLDEPTSGLDSQTAWSICKLIRKLADNGQAILCTIHQPSAILLAEFDRLLFLQRGGRTVYFGDLGENFTTLINYFEKYGAPKCPPEANPAEWMLEVIGAAPGSKANQDYYDVWLKSSEFQEMNSELDLMSEELVKKPLDDDPDRLKPYAAPYWEQYLFVTKRVFEQNWRTPSYLYSKFLLVVTSSLFNGFSFYKADRSLQGLQNQMFSVFMFLVILHTLIQQYLPTFVSQRDLYEVRERPSKTFSWITFIAAQVTAEIPWNIICGTLGYFCWYYPVGLYQNATYTNTVHQRGAFMWFAIVLFFIYTSTMAQLCISFLEIDDNAANLSVLLFTMCLAFCGVLVTKEQLPGFWVFMYRCSPFTYLVSVMLSVGLVDAPVTCAAKEYLRFSPPQGYTCIQYMEPYMKVAGGYLLNENSTTECEFCTMKVTNVFLKMIGSDYSKRGRDIGIYIAFIGINIIGTFILYWFARVPKNFDIKLRRKR
Protein: Inositol transporter 1 (Q8VZR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar inositol-proton symporter involved in the release of myo-inositol from vacuoles. Not involved in glucose or fructose transport.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:18441213, ECO:0000269|PubMed:22253225}; Multi-pass membrane protein {ECO:0000269|PubMed:18441213, ECO:0000269|PubMed:22253225}.
Interaction partners:
- At2g14110 superfamily protein)
- Protein VAC14 homolog
Sequence:
MTLTIPNAPGSSGYLDMFPERRMSYFGNSYILGLTVTAGIGGLLFGYDTGVISGALLYIKDDFEVVKQSSFLQETIVSMALVGAMIGAAAGGWINDYYGRKKATLFADVVFAAGAIVMAAAPDPYVLISGRLLVGLGVGVASVTAPVYIAEASPSEVRGGLVSTNVLMITGGQFLSYLVNSAFTQVPGTWRWMLGVSGVPAVIQFILMLFMPESPRWLFMKNRKAEAIQVLARTYDISRLEDEIDHLSAAEEEEKQRKRTVGYLDVFRSKELRLAFLAGAGLQAFQQFTGINTVMYYSPTIVQMAGFHSNQLALFLSLIVAAMNAAGTVVGIYFIDHCGRKKLALSSLFGVIISLLILSVSFFKQSETSSDGGLYGWLAVLGLALYIVFFAPGMGPVPWTVNSEIYPQQYRGICGGMSATVNWISNLIVAQTFLTIAEAAGTGMTFLILAGIAVLAVIFVIVFVPETQGLTFSEVEQIWKERAYGNISGWGSSSDSNNMEGLLEQGSQS
Protein: ADP-ribose 1''-phosphate phosphatase (EC 3.1.3.84) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase) (P38218)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose.
Interaction partners:
- Probable ADP-ribose 1''-phosphate phosphatase YML087W
- mRNA-binding protein PUF3
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Small ribosomal subunit protein mS37
Sequence:
MSNITYVKGNILKPKSYARILIHSCNCNGSWGGGIAYQLALRYPKAEKDYVEVCEKYGSNLLGKCILLPSYENSDLLICCLFTSSFGGSSHGEKQSILNYTKLALDKLKTFREAKDKTRTSEDSIGDYLNGHIKYPIGEYKLEMPQINSGIFGVPWKETERVLEEFSGDMSFTVYQL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M4MD44)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATDVVIVKEGWLHKRGEYIKTWRPRYFLLKSDGTFIGYKERPQDVDQLETPLNNFSVAQCQLMKTERPKPNTFIIRCLQWTTVIERTFHVETPEERQEWTKAIQTVAESLQKQEEEMMDASAEHTDMETSLSKPPHKVTMHDFEYLKLLGKGTFGKVILVKEKATGKYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKSSFQTHDHLCFVMEYANGGELFFHLSRERVFSEERACFYGAEIVSALHYLHSERNVVYRDLKLENLMLDKDGHVKITDFGLCKEGITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEDIRFPRTLAPDAKSLLSGLLKKDPMQRLGGGPDDAKEIMQHKFFTGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTGQTITITPPGQDDCMEAFDSERRPHFPQFSYSASGTA
Protein: V-type proton ATPase subunit e (V-ATPase subunit e) (Low dye-binding protein 10) (Vacuolar proton pump subunit e) (Q3E7B6)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14970230}; Multi-pass membrane protein {ECO:0000269|PubMed:14970230}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit c
- V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit G
- V-type proton ATPase subunit E
Sequence:
MSSFYTVVGVFIVVSAMSVLFWIMAPKNNQAVWRSTVILTLAMMFLMWAITFLCQLHPLVAPRRSDLRPEFAE
Protein: BURP domain-containing protein 13 (OsBURP13) (Protein RAFTIN 1) (OsRAFTIN1) (Q7F8U7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Required for pollen development. Probably synthesized in the tapetum, packaged in Ubisch bodies and transported at appropriate stages to the micropsores.
Interaction partners:
- Os04g0589400 protein
Sequence:
MARFLLLLVAVAAAAAVLSLGDAAPSTAEVFWRAVLPESPLPDAFLRLLRPDTSFVVGKAEAAGGAARTGFPFDYTDYRGSDSPTTASGLDLAGDFGEPAPFGYDYSAQGEGGGGGAAAAAGEQVLAVDAGFNYDKYVGARKLRGGSSTAGGENDDEPFGYDYKAPSSGSGTAASTTARGVGTGATTTVFFHEEAVRVGERLPFYFPAATTSALGFLPRRVADSIPFTAAALPAVLALFGVAPDTAEAAGMRETLRTCEWPTLAGESKFCATSLEALVEGAMAALGTRDIAALASTLPRGGAPLQAYAVRAVLPVEGAGFVACHDQAYPYTVYRCHTTGPARAYMVEMEGDGGGDGGEAVTVATVCHTNTSRWNPEHVSFKLLGTKPGGSPVCHLMPYGHIVWAKNVKSSTA
Protein: SET domain bifurcated histone lysine methyltransferase 1 (D4A081)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVLGVFKSQLSTGKQNSGESMSSLPGCMSLAAAPAAADSAEIAELQQAVVEELGISMEELRQFIDEELEKMDCIQQRKKQLAELETWVLQKESEVAYVDRLFDDASREVTNCESLVKDFYSKLGLQYHDSSSDDEASQPTEIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDLHKGTLGQVSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGLGKKYKVKFDNKGKSLLSGNHIAYDYHPPADKLFVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDGYASYVTQSELYPICRPLKKTWEDIEDSSCRDFIEEYITAYPNRPMVLLKSGQLIKTEWEGTWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASAMEKKQGGQLRTRPNMGAVRSKGPVVQYTQDLTSTGIQFKPMEPLQPIVPPAPLPMLPLSPQAGDSESLESQLAQSRKQVAKKSTSFRPGSVSSGHSSPTSPTLSENVPPGKIGMNQTYRSPSASVTSTPAPAAPSGPPAPPGPLAPPGPPAPPAFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRIRPMRNEQYRGKNPLLVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLYLEMFCLDPYVLVDRKFQPFKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFINTGPEFLVGCDCKDGCRDKSKCACHQLTVQATACTPGGQINPSSGYQHKRLEECLPTGVYECNKRCKCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIESVENFKEGYESDVPSSSDSSGVDMKDQEDGNSGSEDPEESNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKESELSEVTSKDSRAPDRGPPHVPITPSGSVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSRSSFKTSEGGDGRAGGGRGEAERASTSGLSFKDEGDSKQSKKEDPEDRNKMSVVTEGSQNHGHNPPMKSEGLRRPASKISMLQSQRVVTSTQSNPDDILTLSSSTESEGESGTSRKPTTGQTSATAVDSDDIQTISSGSDGDDFEDKKNLSGPTKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQFYDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTELTWDYNYEVGSVEGKELLCCCGAIECRGRLL
Protein: DNA replication licensing factor mcm4-B (EC 3.6.4.12) (CDC21 homolog-B) (Minichromosome maintenance protein 4-B) (xMCM4-B) (P1-CDC21-B) (P30664)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:8605878}. Chromosome {ECO:0000269|PubMed:8605878}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000269|PubMed:30979826, ECO:0000269|PubMed:8605878}.
Interaction partners:
Sequence:
MSSPTSTPSRRRNKRGRGSNPPTPHGEEVQSPPSQRRRTEDSTSIGELLPMPTSPSGDVQSPSGQELLFSSPAPSRHSAHQSELDLSSPLTYGTPSSRVEGTPRSGIRGTPARQRPDLGSARKVKQVDLHSDQPAAEELVTSEQSLGQKLVIWGTDVNVATCKEKFQRFVQRFIDPSAKEEDNVGLDLNEPIYMQRLEEINVVGDPFLNIDCDHLRNFDQDLYRQLVCYPQEVIPTFDMAANEIFFERYPDSILEHQIQVRPYNALKTRNMRSLNPEDIDQLITISGMVIRTSQIIPEMQEAFFKCQVCAFTTRVEIDRGRIAEPSVCKHCNTTHSMALIHNRSMFSDKQMIKLQESPEDMPAGQTPHTTILYGHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVRNVKSVYKTHIDVIHYRKTDSKRLHGIDEDTEQKLFTEERVAMLKELAAKPDIYERLAAALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEVNILLCGDPGTSKSQLLQYVFNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPVESQWNPKKTTIENIQLPHTLLSRFDLIFLMLDPQDEAYDRRLAHHLVALYYQSEEQMKEEHLDMAVLKDYIAYARTYVNPRLSEEASQALIEAYVSMRKIGSGRGMVSAYPRQLESLIRLSEAHAKVRFSNKVETIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATARKRKEELAQVLKKLIQSKGKTPALKYQQLFEDLRGQSDAAITKDMFDEALHALADDDYLTVTGKTVRLL
Protein: PHD finger protein ALFIN-LIKE 3 (Protein AL3) (Q9M2B4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:19154204}.
Interaction partners:
- Multiple organellar RNA editing factor 1, mitochondrial
- F-box/LRR-repeat protein At4g14103
- G-type lectin S-receptor-like serine/threonine-protein kinase At1g61370
- Protein TRAUCO
- Late embryogenesis abundant
- Protein RBL
- PHD finger protein ALFIN-LIKE 6
Sequence:
MEGGAALYNPRTVEEVFKDFKGRRTAIVKALTTDVQEFYQQCDPEKENLCLYGLPNEEWEVNLPAEEVPPELPEPALGINFARDGLSEKEWLSLVAIHSDAWLLSVSFYFGSRFSFHKEERKRLFNMINDVPTIFEVVTGMAKAKDKSSAANQNGNKSKSNSKVRTSEGKSSKTKQPKEEDEEIDEDDEDDHGETLCGACGDSDGADEFWICCDLCEKWFHGKCVKITPARAEHIKQYKCPSCSNKRARA
Protein: Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10) (P0A0R3)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
Interaction partners:
- Chaperonin GroEL
- Chaperone protein DnaK
- Protein GrpE
- Chaperone protein HtpG
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent protease subunit HslV
- Chaperone protein DnaJ
- Dihydrolipoamide acetyltransferase
- Chaperone protein ClpB
- NADH-quinone oxidoreductase
Sequence:
MKFQPLGERVLVERLEEENKTSSGIIIPDNAKEKPLMGVVKAVSHKISEGCKCVKEGDVIAFGKYKGAEIVLDGTEYMVLELEDILGIVGSGSCCHTGNHDHKHAKEHEACCHDHKKH
Protein: COP9 signalosome complex subunit 3 (Signalosome subunit 3) (Protein FUSCA 11) (Q8W575)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex-related / CSN complex-like protein
Sequence:
MIGAVNSVEAVITSIQGLSGSPEDLSALHDLLRGAQDSLRAEPGVNFSTLDQLDASKHSLGYLYFLEVLTCGPVSKEKAAYEIPIIARFINSCDAGQIRLASYKFVSLCKILKDHVIALGDPLRGVGPLLNAVQKLQVSSKRLTALHPDVLQLCLQAKSYKSGFSILSDDIVEIDQPRDFFLYSYYGGMICIGLKRFQKALELLYNVVTAPMHQVNAIALEAYKKYILVSLIHNGQFTNTLPKCASTAAQRSFKNYTGPYIELGNCYNDGKIGELEALVVARNAEFEEDKNLGLVKQAVSSLYKRNILRLTQKYLTLSLQDIANMVQLGNAKEAEMHVLQMIQDGQIHALINQKDGMVRFLEDPEQYKSSEMIEIMDSVIQRTIGLSKNLLAMDESLSCDPLYLGKVGRERQRYDFGDDFDTVPQKFSM