wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein H25N7.10 (Q9N950)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MFQLVSAAEVNKAYVSYPGGVSMCLRFPFCHCVWAHAMTLIEISGHYHIWVARGESEDWDYSNSFVVVCVVLLENIATNEREGKCHLTFHAATSMHKNYMLVALRGKAVKAKVSFRFKEV
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (UDP-glucose pyrophosphorylase) (UDPGP) (UGPase) (Q91ZJ5)
Organism: Mus musculus (Mouse)
Function: UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16851}.
Interaction partners:
- Phosphoglucomutase-1
- Glycogen [starch] synthase, muscle
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, muscle form
- Glycogen [starch] synthase, liver
- Glycogen phosphorylase, brain form
- UDP-glucose 4-epimerase
- Galactose-1-phosphate uridylyltransferase
- Glycogen debranching enzyme
- UDP-glucose 6-dehydrogenase
Sequence:
MSRFVQDLSKAMSQDGASQFQEVILQELELSVKKELEKILTTAASHEFEHTKKDLDGFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSGNLRILDH
Protein: Pre-mRNA-processing factor 39-1 (AtPRP39-1) (PRP39 homolog A) (Pre-mRNA-processing factor 39a) (Q93ZR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-mRNA splicing. Involved in the determination of flowering time probably via the modulation of flowering associated genes (e.g. FLC, FT and SOC1) expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P39682}.
Interaction partners:
Sequence:
MGDSEAMVSEGYTSAPYGDYNASAATVESTGQETAPIVDASHSVNNDSLVNGTAPVENGSATDNVAVTAPAAEHGDNTGSTLSTEEERLWNIVRANSLEFNAWTALIDETERIAQDNIAKIRKVYDAFLAEFPLCYGYWKKFADHEARVGAMDKVVEVYERAVLGVTYSVDIWLHYCTFAINTYGDPETIRRLFERALVYVGTDFLSSPLWDKYIEYEYMQQDWSRVALIYTRILENPIQNLDRYFSSFKELAETRPLSELRSAEESAAAAVAVAGDASESAASESGEKADEGRSQVDGSTEQSPKLESASSTEPEELKKYVGIREAMYIKSKEFESKIIGYEMAIRRPYFHVRPLNVAELENWHNYLDFIERDGDFNKVVKLYERCVVTCANYPEYWIRYVTNMEASGSADLAENALARATQVFVKKQPEIHLFAARLKEQNGDIAGARAAYQLVHSEISPGLLEAVIKHANMEYRLGNLDDAFSLYEQVIAVEKGKEHSTILPLLYAQYSRFSYLVSRDAEKARRIIVEALDHVQPSKPLMEALIHFEAIQPPPREIDYLEPLVEKVIKPDADAQNIASSTEREELSLIYIEFLGIFGDVKSIKKAEDQHVKLFYPHRSTSELKKRSADDFLASDRTKMAKTYNGTPPAQPVSNAYPNAQAQWSGGYAAQPQTWPPAQAAPAQPQQWNPAYGQQAAYGAYGGYPAGYTAPQAPTPVPQAAAYGAYPAQTYPTQSYAPPVAAAAPAAAPVQQPAAAVAPQAYYNTYY
Protein: Jumonji and AT-rich interaction domain containing 2 (M0RBV7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein AEBP2
- SUZ12 polycomb repressive complex 2 subunit
- Histone-lysine N-methyltransferase EZH2
- Polycomb protein EED
- [histone H3]-lysine
- Metal-response element-binding transcription factor 2
- RB-binding protein 4, chromatin-remodeling factor.
- PHD finger protein 19
- Histone-binding protein RBBP7
- Elongin BC and polycomb repressive complex 2 associated protein
Sequence:
MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNAQKRQHGEGIAGSLKTVNGLLGNDQSKALGPASEQSENEKDDASQVSSTSNDVSSSDFEEGPSRKRPRLQAQRKFAQSQPNSPSTTPVKTVEPLLPPPATHISDLSKRKPKTEDFLTFLCLRGSPALPNSMVYFGSSQDEEDVEEEDDETEDVKTATNNASSSCQSTPRKGKSHKHVHNGHVFNGSNRSAREKEPAQKHRGREATPGKEKHSEHRADGRREQASVAQPTANPPAGSSTKGLAASHQPPPSHRSAQDSRKQVSKVNGVTRMSSLGAGTNSAKKIREVRPSPSKTVKYTATVTKGTVTYTKAKRELVKETKPSHHKPSSAVNHTISGKSESSNAKTRKQVLSLGGASTSTAPAASGLKASSRLNPKSCTKEVGGRQLREGLRNSKRRLEEAQQVDKQQSPPKKMKGTAGIAEAPGRKASAASGEKSLLNGHVKKEVPERSLERNRPKRAAAGKNMLGKQAHGKSEGTPCENRSTSQPESSHKPHDPQGKPEKGSGKSGWAAMDEIPVLRPSAKEFHDPLIYIESVRAQVEKYGMCRVIPPPDWRPECKLNDEMRFVTQIQHIHKLGRRWGPNVQRLACIKKHLRSQGITMDELPLIGGCELDLACFFRLINEMGGMQQVTDLKKWNKLADMLRIPKTAQDRLAKLQEAYCQYLLSYDSLSPEEHRRLEKEVLMEKEILEKRKGPLEGHTENDHHKFHSLPRFEPKNGLIHGVTPRNGFRSKLKEVGRAPLKTGRRRLFAQEKEVVKEEEEDKGVLDDFYKCIYKGRSVSLTTFYRTARNIMNMCFSKEPAPAEIEQEYWRLVEEKDCHVAVHCGKVDTNTHGSGFPVGKSEPFSRHGWNLTVLPNNTGSILRHLGAVPGVTIPWLNIGMVFSTSCWSRDQNHLPYIDYLHTGADCIWYCIPAEEENKLEDVVHTLLQGNGTPGLQMLESNVMISPEVLCKEGIKVHRTVQQSGQFVVCFPGSFVSKVCCGYNVSETVHFATTQWTSMGFETAKEMKRRHIAKPFSMEKLLYQIAQAEAKKENGPTLSTISALLDELRDTELRQRRQLFEAGLHSSARYGSHDGSSAVADGKKKPRKWLQLETSERRCQICQHLCYLSMVVQENENVVFCLECALRHVEKQKSCRGLKLMYRYDEEQIISLVNQICGKVSGKHGGIENCLNKPTPKRGPRKRATVDVPPSRLPSS
Protein: Single-strand DNA endonuclease ASTE1 (EC 3.1.-.-) (Protein asteroid homolog 1) (Q2TB18)
Organism: Homo sapiens (Human)
Function: Possible role in EGF receptor signaling.
Interaction partners:
- TATA box-binding protein-associated factor RNA polymerase I subunit B
Sequence:
MGIRGLMSFVEDHSNEFFTDLKLRDTKIVIDGYALFHRLCFSSNLDLRYGGDYDSFADVVQKFFESLFACNICPYVVLDGGCDISDKKLTTLKDRAREKIQMAHSLSVGGSGYVCPLLIREVFIQVLIKLRVCFVQCFSEADRDIMTLANHWNCPVLSSDSDFCIFDLKTGFCPLNSFQWRNMNTIKGTQNYIPAKCFSLDAFCHHFSNMNKALLPLFAVLCGNDHVNLPIMETFLSKARLPLGATSSKGRRHHRILGLLNWLSHFANPTEALDNVLKYLPKKDRENVKELLCCSMEEYQQSQVKLQDFFQCGTYVCPDALNLGLPEWVLVALAKGQLSPFISDALVLRRTILPTQVENMQQPNAHRISQPIRQIIYGLLLNASPHLDKTSWNALPPQPLAFSEVERINKNIRTSIIDAVELAKDHSDLSRLTELSLRRRQMLLLETLKVKQTILEPIPTSLKLPIAVSCYWLQHTETKAKLHHLQSLLLTMLVGPLIAIINSPGKEELQEDGAKMLYAEFQRVKAQTRLGTRLDLDTAHIFCQWQSCLQMGMYLNQLLSTPLPEPDLTRLYSGSLVHGLCQQLLASTSVESLLSICPEAKQLYEYLFNATRSYAPAEIFLPKGRSNSKKKRQKKQNTSCSKNRGRTTAHTKCWYEGNNRFGLLMVENLEEHSEASNIE
Protein: N-acetylglucosamine-1-phosphotransferase subunit gamma (GlcNAc-1-phosphotransferase subunit gamma) (M6PR domain-containing protein 1) (UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma) (Q6S5C2)
Organism: Mus musculus (Mouse)
Function: Non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors.
Subcellular location: Secreted. Golgi apparatus.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Neutral alpha-glucosidase AB
Sequence:
MAGRLAGFLMLLGLASQGPAPAYAGKMKVVEEPNTFGLNNPFLPQASRLQPKREPSAVSGPLHLFRLAGKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIINNTFKGMWMTDGDSCHSRSRQSKVELTCGKINRLAHVSEPSTCVYALTFETPLVCHPHSLLVYPTLSEALQQRWDQVEQDLADELITPQGYEKLLRVLFEDAGYLKVPGETHPTQLAGGSKGLGLETLDNCRKAHAELSQEVQRLTSLLQQHGIPHTQPTETTHSQHLGQQLPIGAIAAEHLRSDPGLRGNIL
Protein: Homeobox protein koza (Homeodomain transcription factor koza) (Q9W7E8)
Organism: Xenopus laevis (African clawed frog)
Function: May regulate cell proliferation in a tissue-specific manner.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSKLRTEDMSHPVKPLRSFLIQDILSHMGPGSKEKSLGFPKTDQDQDSSLRDTEEKYASEKLQSSSQPAEIHHSHMEADENLELDTAQPITAVENKLAKQQQKRSRAAFSHSQVIELERKFSSQKYLSAPERAQLAKSLKLTETQVKIWFQNRRYKTKRKQLATDMEEVEKSSAHPAQCRDTNISRTSLLSFYQNYQRYPYLYYLAGWPAPLW
Protein: Solute carrier family 41 member 2 (Q96JW4)
Organism: Homo sapiens (Human)
Function: Acts as a plasma-membrane magnesium transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16984228}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transient receptor potential cation channel subfamily M member 6
- Transient receptor potential cation channel subfamily M member 7
Sequence:
MTNSKGRSITDKTSGGPSSGGGFVDWTLRLNTIQSDKFLNLLLSMVPVIYQKNQEDRHKKANGIWQDGLSTAVQTFSNRSEQHMEYHSFSEQSFHANNGHASSSCSQKYDDYANYNYCDGRETSETTAMLQDEDISSDGDEDAIVEVTPKLPKESSGIMALQILVPFLLAGFGTVSAGMVLDIVQHWEVFRKVTEVFILVPALLGLKGNLEMTLASRLSTAVNIGKMDSPIEKWNLIIGNLALKQVQATVVGFLAAVAAIILGWIPEGKYYLDHSILLCSSSVATAFIASLLQGIIMVGVIVGSKKTGINPDNVATPIAASFGDLITLAILAWISQGLYSCLETYYYISPLVGVFFLALTPIWIIIAAKHPATRTVLHSGWEPVITAMVISSIGGLILDTTVSDPNLVGIVVYTPVINGIGGNLVAIQASRISTYLHLHSIPGELPDEPKGCYYPFRTFFGPGVNNKSAQVLLLLVIPGHLIFLYTIHLMKSGHTSLTIIFIVVYLFGAVLQVFTLLWIADWMVHHFWRKGKDPDSFSIPYLTALGDLLGTALLALSFHFLWLIGDRDGDVGD
Protein: Gamma-aminobutyric acid receptor-associated protein (GABA(A) receptor-associated protein) (P60517)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (By similarity). Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination a nd degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction. Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation (By similarity). Involved in apoptosis (By similarity).
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:O95166}. Endomembrane system {ECO:0000269|PubMed:11461150}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10899939}. Golgi apparatus membrane {ECO:0000269|PubMed:11461150}. Cytoplasmic vesicle {ECO:0000269|PubMed:25172774}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae (PubMed:11461150). Colocalizes with microtubules (PubMed:10899939). Also localizes to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q9DCD6, ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:11461150}.
Interaction partners:
- BCL2/adenovirus E1B interacting protein 3-like.
- Next to BRCA1 gene 1 protein
- BCL2 interacting protein 3
- Sequestosome-1
- FUN14 domain-containing protein 1
- Ubiquitin-like-conjugating enzyme ATG3
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein ATG12
- Beclin 1-associated autophagy-related key regulator
- Cysteine protease ATG4B
Sequence:
MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
Protein: Centrosomal protein of 126 kDa (Q9P2H0)
Organism: Homo sapiens (Human)
Function: Participates in cytokinesis. Necessary for microtubules and mitotic spindle organization. Involved in primary cilium formation.
Subcellular location: Midbody {ECO:0000269|PubMed:19799413, ECO:0000269|PubMed:24867236}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24867236}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24867236}.
Interaction partners:
Sequence:
MLAGRPGTRSAVGELGTESSDNLDRAPLGPRESGGHHRPGSYLDMKIHLEKNLEEERQILLQQQKICRNRARKYFVESNRRKKAFEEKRKEQEEKEHQIREQILQQRKQKFEEVTEKFQRAHVPLSQRRKAVSRKPVPPLEEALKQIQESNLKSEVNLPFSRRPTINWRAIDSALPSALSKNDHKHQKQLLSKINCEKEMNENMRATLATSKNVFQLKLEETQKLLEDQHLSNLQKFCDEVNQITNSETLSSIDSLEATEHEEIYLTLNKEHSTSIQRNTISLKPANMQSTNLSCFDEDKLAFSKTQHINNWLTNLDASNTQNVTAFSDILSKSNVLPSWEYFNSKEQNPSPLNGTVERATNTANNSVPFVSSPPMFVLDKKCEKTSETSTMRTTDSTSGAFKRERPLVTESPTFKFSKSQSTSDSLTQEVATFPDQEKYSELNQENGTTSIPTSCVPVATPLVLPSNIQSARPSAKNSIHIKEIDAVQCSDKLDELKDGKEEEIKYFNCNKEELPLFSDSFQDAYIPHNPDSKDEKQKLAETSSLSNVTSNYDFVGQHKKMKYNIHERNGVRFLKSILKKESKYEHGYLKALIINQSFKFGNQKAAAIRDSIELTKEKGAEIPKTIKKLRWFDETSNIENNAENSHSLKNKTGTTQQHSQQFHIQSGAGSNIISVSTCAVNSADTKKSREDSISENVTTLGGSGADHMPLNCFIPSGYNFAKHAWPASKKEESKIPVHDDSKTKQGKPQRGRAKIIRKPGSAKVQSGFICTNRKGAVIQPQSASKVNIFTQAQGKLIIPCPPPQSTSNIRSGKNIQVSQCQPVTPENPQNIITHNSFNSKHVLPTEHSLNQWNQESSSPLSNACSDLVTVIPSLPSYCSSECQTFAKINHSNGTQAVARQDATLYCTQRSPVCEESYPSVTLRTAEEESVPLWKRGPNVLHQNKRATGSTVMRRKRIAETKRRNILEQKRQNPGSVGQKYSEQINNFGQSVLLSSSEPKQTTRGTSYIEEVSDSTSEFLMAENLVKASVPEDEILTVLNSKQIQKSNLPLNKTQQFNICTLSAEEQKILESLNDLSERLHYIQESICKNPSIKNTLQIIPLLEKREDRTSSCRDKR
Protein: Mitogen-activated protein kinase kinase 1b (EC 2.7.12.2) (MAP kinase kinase 1b) (PpMKK1b) (A9SR33)
Organism: Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens)
Function: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin.
Interaction partners:
Sequence:
MSRRHRTGGLRVAVPKQENSIHRFLTANGVFHDDDIQLDHMGLRVVSSESTAYANPPDAQLSLADLEAVRVLGKGAGGSVQLVRHKWTNDIYALKGIQMNINETVRKQIVQELKINQLTLHQCPYIVKCYHSFYHNGIISIVLEYMDRGSLADIIKQTKQIPEPYLAVISNQVLKGLNYLHQVRHIIHRDIKPSNLLINQKGEVKISDFGVSAVLISSMAQRDTFVGTYTYMSPERLGGQSYAYDSDIWSLGLTILECALGYFPYRPPGQEEGWNNFFMLMELVINQPPVAAPPDKFSPEFCSFIAACIQKRPGDRLSTADLLKHPFLQKYSEEEYHLSNLR
Protein: Zinc finger protein 131 (Q8K3J5)
Organism: Mus musculus (Mouse)
Function: May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling (By similarity). Plays a role during development and organogenesis as well as in the function of the adult central nervous system.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- BRCA2-interacting transcriptional repressor EMSY
Sequence:
MEAEETMECLQEFPEHHKMILDRLNEQREQDRFTDITLIVDGHHFKAHKAVLAACSKFFYKFFQEFTQEPLVEIEGVSKMAFRHLIEFTYTAKLMIQGEEEANDVWKAAEFLQMLEAIKALEVRNKENSAPLEENTTGKNEAKKRKIAETSNVITESLPSAESEPVEIEVEIAEGTIEVEDEGIEALEEMASAKQSIKYIQSTGSSDDSALALLADITSKYRQGESKGQISEDDCASDPISKQVEGIEIVELQLSHVKDLFHCEKCNRSFKLFYHFKEHMKSHSTESFKCEICNKRYLRESAWKQHLNCYHLEEGGVSKKQRTGKKIHICQYCDKQFDHFGHFKEHLRKHTGEKPFECSNCHERFARNSTLKCHLTACQTGVGAKKGRKKLYECQVCNSVFNSWDQFKDHLVIHTGDKPNHCTLCDLWFMQGNELRRHLSDAHNISERIVTEEVLSVETHLQTEPVTSMTIIEQVGKVHVLPLLQVQVDSAQVTVEQVHPDLLQDSQVHDSQMTGLPEQVQVSYLEVGRIQTEEGTEVHVEELHVERVNQMPVEVQTELLEADLDHMTPEIMSQEEREPNHADAAMEEHEDAEGLETKPSEYSQARKTENDRTSLPVLE
Protein: Ferric reductase transmembrane component 4 (EC 1.16.1.9) (Ferric-chelate reductase 4) (P53746)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable ferric reductase transmembrane component 8
- Iron-regulated transcriptional activator AFT1
- Uncharacterized protein YDR344C
- Iron transport multicopper oxidase FET3
Sequence:
MLLVHIISFLLFFQLSAAKAPPSKTSLINTHERRSIYSCYVGLRKETWGFNGSAICRYEPAIQSMLYCLYEDTHEKGYSNKTLEKGFEEMRQFCYTPKFLNMTDAEFYTSLDNGTYYIQDQPKAGINITYPIRLNTTLRKAYYDAYYGYYYNHDIPYYFGGIICAYFVGVMLLAGLIRFLNYTPIKKIMFQQKLVNYVRGYTTLPTLYEKHAEPFSYLKVITGYLPTRFETLVILGYLILHTIFMAYKYQYDPYHIIFAAHRAEVAHFVAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYYKKWNTVRLRVYWKFGIATTCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTCWEHVTNFSGIEWIYAAIAIWGVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTAHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKKELMALKGLNVQVHIYNSKQELASAEKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELPLSLNDTSISDLEFATFHVGRPNVEEILNESVNHSGSLAVVCCGPPIFVDTARNQTAKAVIRNPSRMIEYLEEYQAW
Protein: GH15768p (Q9VMT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- arginine kinase
Sequence:
MEELQDASIHHMTAKVIAAIKNTKSYEPIYKELQKLVCNPSVDTHDMRNTLEDAIKSAGLETEIRNIVYNLVRTRLSKTDDKNLANKQGAKPTVSDPLGYLKRAGVLWDRRVRKSLNAMCTELKVPLHGQPRISADREDFMAKWNELSNYNMDLANYRPVYAPKDLLEVLLSLKGPAKTTENTDQIPQWEFSHIALPVKNLFELRAHYADLLRSDSYLGVPDLTVQCQRILEARHAPMCQQFLKKGCTPAPYRGALWASVLDSKLHDYDIEYWQKLRNAVWTTDHIVDKLVFKDIQLTASNDDQYFVFEDVLYQVLLCFSRDTDIGGCVEYETFPVKGKTYEGPPSGVVPFHGICMFAAPFCYLYDSPVSLYYTFRAFYIRYCHRLTTINTHPQGIVSLCLLFEKLLQTYEPQLWSHFRELQIQPLRVVFKWLMRAFSGHLPPDQLLVLWDLILGFDSLEILPLFAIIILSFRKESIMQVASLDSIEAILADLSSIKVLPLVQLALSRD
Protein: Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK) (O88454)
Organism: Mus musculus (Mouse)
Function: Voltage-insensitive potassium channel. Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure. Plays a role in the perception of pain caused by heat.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27035965, ECO:0000269|PubMed:9628867}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:G3V8V5}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000250|UniProtKB:G3V8V5}.
Interaction partners:
- Selenocysteine lyase
- Potassium channel subfamily K member 13
- Potassium channel subfamily K member 2
- MNTK1
- Piezo-type mechanosensitive ion channel component 1
Sequence:
MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQAQKKMDHGRDQFLRDHPCVSQKSLEDFIKLLVEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIVLHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAIFLKWHVPPGLVRSLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVVEPAGRPGSPAPAEKVETPSPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPSKKPSRPRGPGRLRDKAVPV
Protein: Scm-like with four MBT domains protein 1 (Q9JMD1)
Organism: Mus musculus (Mouse)
Function: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional repressor protein YY1
- Disabled homolog 1
- REST corepressor 2
Sequence:
MSGEQQLDADLGSGVEVEEFSWEDYLEETGSTTVPYASFKHVDIRLQNGFAPGMKLEVALKNDPETYWVATIITACEQLLLLRYEGYGEDRKADFWCDIRKAGLYPIGWCQQNKKTLEAPEGIRDKVSDWNAFLQQTLIGACGPPVSLLEGLRNGRNPLDLIAPGSKLECQDFRDSLSTWLVTVVENIGGRLKLRYEGLESRDGFEHWLYYLDPFLHHIGWAAQQGCDLQPPLAIKHLKSEADWQEILAKVKEEEPLPSYLFKDKQVIGTHEFSINMKLEAVDPWSPFGISPATIAKVFDDKYFLVEMDDLRPEDHTRRSFVCHANSPGIFPVQWSLKNGLHINPPPGFRSQDFDWADYLKQCGAEAAPQKCFPQSISEHQFKENMKLEAVNPLFPEEVCIATVTAVRGSYLWLQLEGSKKPVPEFIVSAESMNIFPLGWCETNGHPLSTPRRARGHKLRKIAVVQPEKQILSSRTVHEGLKNQLNSTHSVMINGKYCCPKIYFNHRCFSGPYLNKGRIAELPQCVGPGNCVLVLREVLTLLINAAYKPSRVLRELQLDKDSVWHGCGEVLKAKYKGKSYRATVEIVRTADRVTEFCRQTCIKLECCPNLFGPRMVLDTCSENCSVLTKTKYTHYYGKKKNKRIGRPPGGHSNLSCALKKSSKRRKRRKNIFVHKKKRSSASVDNTPVGSPQGSGGEDEEDADDGDEDSLTEGSTSEQQEELQEESEVSEKKSSSSSPTQSETPTPLPPDTQTNKRDAQTSSVSDDENKPPSPKEIRIEVDERLHLDSNPLKWSVADVVRFIRSTDCAPLARIFLDQEIDGQALLLLTLPTVQECMDLKLGPAIKLCHHIERIKFAFYEQFAN
Protein: Probable pleckstrin homology domain-containing family N member 1 (PH domain-containing family N member 1) (Cardiolipin and phosphatidic acid-binding protein) (Q8C886)
Organism: Mus musculus (Mouse)
Function: Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1. Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol. Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q494U1}; Lipid-anchor {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion {ECO:0000269|PubMed:27616329}. Note=Interaction with C1QBP and phosphorylation is essential for its mitochondrial localization. Localizes on the microtubule in the form of small granules. {ECO:0000250|UniProtKB:Q494U1}.
Interaction partners:
Sequence:
MGNSHCVPQAPRRLRASFSRKPSLKGNREDSARKLAGLFGTEARPDGDTAANRIFHYIPGTDIPGPEHHPENLEQPFLSVFKKGWRRTPVRNLGKVVHYSKVRLRFQHSQDISDCYLELFPSHLYFQAHGSEGLTFQGLLPLTELNICPTDGSREHAFQITGPLPAPLLVLCHSEAELSHWLYHLEKQMALLGLQRCHSAPPQGSLGDKPPWTQLRRAYGCGSMSGAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLSFKGELPLSAIHINLEEKEKEIRSFLIEGHLINTIRVVCASYEDYSQWLLCLRTVSRRDGAHLPPGPESFPGLQKPTQLVGRGRGSLSSNGRSSWKLECPVFPTSQSLPESSVPTTIGFPAPPVPNQTDSNCVSTGQKKMKPSDSSPSPRGRAQREVSGSTVPLPLPLDLTKMSALNLDSGPEAQDHSLDIPHSPLYADPYTPPATSRHKITDIQGLDEFLCAIQTSPGPDLSSPFPPVSVSVPVSESSSGISSSPGPLGSHLLTKKGALQPRASQRHRGSFKSRGPQPSDFPQLVTPAREGKPSSLPPPPDEEAPIWNKTSSPSHPKWPQPRKPAVEGGFIQWI
Protein: Rifin (Q8IAK4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILVSSKKNTYIKYNTLNTKLIRAHRTLCECELYALSNYDNDPEMKEVMQQFDRQSSQRFLEYDERMKTTRQKCKDKCDEAIQKIILKDKLEKELMDKFATLHTDMQSDAIPTCVCEKSLADKVEKGCLRCGGVLGGGVMPGFGAIGGTALYALNQLKPTALKAAIAAANEAGIAAGKIAGDAAGMKVVSFGLKHFRVDELFPDIFKNFVNTKPYNEITTIANSILENYRAICTGVENIKAPTACKTFEYKFGIFIEGSRKPGPPAYNAIPQGLKEISIKAEQAAATASKNASETVSTAIKARETALIEAGFNSSITSINASIFAIVVIVLIMVIIYLILRYRRKKKMKKKLQYIKLLDE
Protein: VirE2 (Q8VT82)
Organism: Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Interaction partners:
Sequence:
MDPNAITPSGNDVYELLRPHAAENEGDLKAKRQKLPEHLSDLMDEGEKTFNLSQESVDAPSSASSSITDDQQVEYIAALLKEIPLLPGAARRPDEYILVVGTGSGRVTGTVKGKLGRLPTRDEFNNACRLYRDGAGNYFPPPQAYNRILVPDEIEDKAAFRKDVWYKAHREMNISGTRMYFDLDPKYPLDKYGKLRPEDQYTETAYGRRKVQRHYLHSFQAGMLLPDIMIKTPDNDVYFVSRSENDRYTNKTFQEFEAIIKRTYGSESEIKLKSESGIMHDSKYLDAWQQGSADIRFASYAGEVRTHNPDLPHAIVNLKSDVRPQDVFLSVEAVFQSPGNPWAEALKRGELWDRILIRDRTGNTYKTPQRLMYSDRDHFKKILDRVGLPHGIGEFTEATATKYERFQTQAAVLVADGAIIKDIRSLSAEERTQAVTAHVLLADRNSQNQRKGTYTSLLEYARTKEQLPHDVADLLGHPIDYFSHDRVQPAPERPPIVYSGDPRTFVRVRDQTVNNL
Protein: Dipeptidyl-peptidase 7 (DPP7) (EC 3.4.14.-) (Q5LB17)
Organism: Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), followed by Leu-Arg-, and to a much lesser extent Lys-Ala-, Leu-Asp-, Leu-Glu-, Leu-Lys, and Val-Arg-MCA, while this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-Pro-MCA.
Interaction partners:
Sequence:
MNRLKLYLLALTALAVCSAKADEGMWLLQLMQQQHSIDMMKKQGLKLEAQDLYNPNGVSLKDAVGIFGGGCTGEIISPEGLILTNHHCGYASIQQHSSVEHDYLTDGFWATSRDKELPTPGLKFTFIERIEDITDIVNLRIAAKEITESESFSSTFLNKLAKELFEKSDLKGKKGIVPQALPFYAGNKFYMFYKKVYPDVRMVAAPPSSIGKFGGETDNWMWPRHTGDFSMFRIYADANGEPAEYSASNVPLKTKKHLNISIKGLKEGDYAMIMGFPGSTSRYLTVSEVKERMEASNAPRIRIRGTRQDVLKEAMNASDKVRIQYANKYAGSSNYWKNSIGMNKAIIDNNVLGTKAEQEAKFAKFAKEKNNTDYMNVVAKIDEAVAKTSPIKYQQTCLTETFFGGIEFGSPFMVMDKLKEALEQKNDSSIEANIKVLKEVFNDIHNKDYDHEVDRKVAKALLPLYAEMIPAGQRPAIYDVIEKEYKGDYNAYVDAMYDTSILANQANFDKFIKKPTVKAIEKDIATQYSRAKFDKYTNLAEQMGKLPEELALLHKTYIRGLGEMKLPVPSYPDANFTIRLTYGNVKPYSPKDGVYYKYYTTTDGILEKENPEDREFVVPAKLKELIEKKDFGRYALPNGEMPVCFLSTNDITGGNSGSPVLNENGELIGCAFDGNWESLSGDINFDNNLQRCINLDIRYVLFILEKLGGCGHLINEMTIVE