wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon alpha-inducible protein 6 (Interferon-induced protein 6-16) (Ifi-6-16) (P09912)
Organism: Homo sapiens (Human)
Function: Plays a role in apoptosis, negatively regulating the intrinsinc apoptotic signaling pathway and TNFSF10-induced apoptosis. However, it has also been shown to have a pro-apoptotic activity. Has an antiviral activity towards hepatitis C virus/HCV by inhibiting the EGFR signaling pathway, which activation is required for entry of the virus into cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30224801, ECO:0000269|PubMed:31142663}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:15685448, ECO:0000269|PubMed:17823654, ECO:0000269|PubMed:25757571, ECO:0000269|PubMed:27673746, ECO:0000269|PubMed:29899394}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Interferon-induced protein 44-like
- Interferon regulatory factor 9
- Interferon-induced GTP-binding protein Mx1
- 2'-5'-oligoadenylate synthase 1
- Ubiquitin-like protein ISG15
- Interferon-induced protein 44
- Interferon-induced protein with tetratricopeptide repeats 3
- 2'-5'-oligoadenylate synthase 2
- 2'-5'-oligoadenylate synthase 3
- XIAP-associated factor 1
Sequence:
MRQKAVSLFLCYLLLFTCSGVEAGKKKCSESSDSGSGFWKALTFMAVGGGLAVAGLPALGFTGAGIAANSVAASLMSWSAILNGGGVPAGGLVATLQSLGAGGSSVVIGNIGALMGYATHKYLDSEEDEE
Protein: L(3)mbt interacting protein 1, isoform A (L(3)mbt interacting protein 1, isoform E) (RE35228p) (Q9VZ22)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CoRest, isoform G
- LD05287p
- Uncharacterized protein, isoform B
- Possible lysine-specific histone demethylase 1
- Histone deacetylase HDAC1
Sequence:
MSKYHKERKYAKFRYYMEKYYVLPLELKNDIIYCQRSLRDFLKVHALVSEVFDEQADADPVQMRRILDELEEEVYEINAEQQFLLLRLNDSLQEFSVKLKENNIMFLPDIAHEYVSAQVVPLIVDPNYKIMPQSVMARDTEEMLIRKHFLLSQDDDSGMPPLKLSELDENIPLMLAPPVRGLGQQIAAVKPEPEWLQGDEATVSVPPPPPQSKSKLMKGSLDSTPAKRENISRSSPPPLAPITQTVVAELSQVPPSPQAESPPVNFHVVAQSRKNLQQALRRARKTKQQPRLFDDEEDLEITSLQNDRNKNRTSDGKGTPPSLEPTNAAANQAAKKTIPQMSSQGMAKNNTAKSKNTCRKSSPTPTSSGQSQPAVSSSGSSDDSSAELQQEQQRRVASAAQWRDEPRESRTQPEEYGQETFLGLFELYSPEVLKKLSQRHSKRKRRTVQNASGVDFHYGQQLNAVDALVMGVRGQKKTKEKSEFLLSPTEKRLQANSKRTYTRKSKSPDEISEKSSAGGGSGASGTASSSACQHKDGGASKCRKCRECRECKRRVETEAMYCHLCSGLYHMDCHEFTKNRQLMQLQNSRCPPCLREKDKLEK
Protein: Vomeronasal 2, receptor 120 (A0A3Q4EHE9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: IQ motif containing GTPase activating protein 1 (A0A8I6AJK7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MCLGDLPTSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKIELEKYGIQMPAFSKIGGILANELSVDEAALHAAVIAINEAIDHRVAADTFTALKNPNAMLVNLEEALAPTYQDVLYQAKQDKMTNAKNRTENSDRERDVYEELLTQAEIQGNVNKVNTSSALANINLALEQGCALTLLKALQSVALGLRGLQTQNSDWYLKQLQSDLQQKRQSGQTDPLQKEEVQAGVDAANGAAQQYQRRLAAVAAINAAIQKGIAEKTVLELMNPEAQLPEVKWGGSEFNTHISHSLTHPELTVAVEMLSSVALINRALESGDMNTVWKQLSSSVTGLTNIEEENCQRYLDELMKLKAQAHAENNEFVTWNDIQACVDHVNLVVHEEHERILAIGLINEALDEGDAQKTLQALQIPAAKLEGVLPEVAQHYQDTLIRAKREKAQETQDESAVLWLDEIQGGIWQSNKDTQEAQRFALGIFAINEAVESGDVGRTLSALRSPDVGLYGVIPECGETYQSDLAEAKKKRLAAGDNNSKWVKHWVKGGYHYYHNLETQAGGWAEPPDFVQNSVQLSREEIQSSISGVTAAYNREQLWLANEGLITKLQACCRGYLVRQEFRSRMNFLKKQIPAITCIQSQWRGYKQKKAYQDRLAYLHSHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINDIIKIQAFIRANKARDDYKTLINAEDPPMIVVRKFVHLLDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSHSKKLTKKNKEQLSDMMMINKQKGGLKALSKEKREKLEAYQHLFYLLQTNPTYLAKLIFQMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFQTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALSHEEVKTRLDNSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAAEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQAACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLGEVPTIESLIGESCGNSNDPSKEALAKTEVSLTLTNKFDVPGDENAEMDARTILLNTKRLIVDVIRFQPGETLTEILETPATNEQEAEHQRAMQRRAIRDAKTPDKMKKSKPMKEDNNLSLQEKKEKIQTGLKKLTELGTVDPKNRYQELINDIAKDIRNQRRYRQRRKAELVKLQQTYSALNSKATFYGEQVDYYKSYIKTCLDNLASKGKVSKKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQANQFKNVIFEIGPTEEVGDFEVKAKFMGVQMETFMLHYQDLLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK
Protein: CYtochrome P450 family (O44649)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- UDP-glucuronosyltransferase
Sequence:
MMFILIVSLILTWLIVRQYQKVSRLPPGPVSLPLIGNLPQIVYYLWTTGGIVSTLDLFRKRYGNIFTLWVGPVPHVSIADYETSYEVFVKQGNKLADVAHSPVLKEFSRGVGLIRCNGEHWQVMRRFALQTFRNMGFGKEPMEIKIMEELDARCAEIDQASINGVTVTSASEFFDLTVGSIINSMLVGTRFEDHNKQEFLDIKNTMEESIGMFSPFDLTMPVWIMKSFFRKRYDFLVGAQESARVLVASEALKRYDDIKSGKYVIDENNLQDYTDAFLLKIVKGEDEKNFNIQALKTMLYDLWLTGQETTTVTLLCGFNHLLAHPEVMDKAREELLKITENRARSLSLSDRPTTPYLNAMIGEIQRHASILNVTFWKINKELTYMGGHPVDSGAVVTAQLGALHVNDTIFKNPREFDPERFIRDDTLLQKVIPFGVGKRNCLGESLARSELYLILGNLLLRYKFEPHGKLSTEETMPYSIAKRAFNLEMKFVKI
Protein: Transferrin-binding protein A (TbpA) (Transferrin-binding protein 1) (Q9K0U9)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C-terminus.
Subcellular location: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360, ECO:0000305|PubMed:22327295}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360, ECO:0000305|PubMed:22327295}.
Interaction partners:
- Transferrin-binding protein B
- Probable TonB-dependent receptor NMB0964
- Surface lipoprotein assembly modifier 1
- Lipoprotein
- Uncharacterized membrane protein NMB1645
- RTX toxin-activating lysine-acyltransferase
- Replication initiation protein-like C-terminal domain-containing protein
- Zona occludens toxin N-terminal domain-containing protein
- Protein TonB
- Inner membrane protein
Sequence:
MQQQHLFRFNILCLSLMTALPAYAENVQAGQAQEKQLDTIQVKAKKQKTRRDNEVTGLGKLVKSSDTLSKEQVLNIRDLTRYDPGIAVVEQGRGASSGYSIRGMDKNRVSLTVDGVSQIQSYTAQAALGGTRTAGSSGAINEIEYENVKAVEISKGSNSVEQGSGALAGSVAFQTKTADDVIGEGRQWGIQSKTAYSGKNRGLTQSIALAGRIGGAEALLIHTGRRAGEIRAHEDAGRGVQSFNRLVPVEDSSNYAYFIVKEECKNGSYETCKANPKKDVVGKDERQTVSTRDYTGPNRFLADPLSYESRSWLFRPGFRFENKRHYIGGILEHTQQTFDTRDMTVPAFLTKAVFDANKKQAGSLPGNGKYAGNHKYGGLFTNGENGALVGAEYGTGVFYDETHTKSRYGLEYVYTNADKDTWADYARLSYDRQGIGLDNHFQQTHCSADGSDKYCRPSADKPFSYYKSDRVIYGESHRLLQAAFKKSFDTAKIRHNLSVNLGFDRFGSNLRHQDYYYQHANRAYSSNTPPQNNGKKISPNGSETSPYWVTIGRGNVVTGQICRLGNNTYTDCTPRSINGKSYYAAVRDNVRLGRWADVGAGLRYDYRSTHSDDGSVSTGTHRTLSWNAGIVLKPTDWLDLTYRTSTGFRLPSFAEMYGWRAGVQSKAVKIDPEKSFNKEAGIVFKGDFGNLEASWFNNAYRDLIVRGYEAQIKDGKEEAKGDPAYLNAQSARITGINILGKIDWNGVWDKLPEGWYSTFAYNRVRVRDIKKRADRTDIQSHLFDAIQPSRYVVGLGYDQPEGKWGVNGMLTYSKAKEITELLGSRALLNGNSRNTKATARRTRPWYIVDVSGYYTVKKHFTLRAGVYNLLNYRYVTWENVRQTAGGAVNQHKNVGVYNRYAAPGRNYTFSLEMKF
Protein: Protein pegasus (Q9VDG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000269|PubMed:34580289}.
Interaction partners:
- Titin
Sequence:
MKLSAVLLAIALLALSLVQCLGLPDPSTKCVMECDTQEYRSICAADDKGSTKTYRNLCVMKTENCLQNANFQKISDKECP
Protein: GTPase activating protein homolog 2 (GTPase activating factor for raC protein CC) (Rho GTPase-activating protein gacCC) (Q55CK2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Rho GTPase-activating protein involved in the signal transduction pathway (By similarity). Regulator of the contractile vacuole network as well as involved in driving vacuole emptying.
Subcellular location: Cytoplasm. Contractile vacuole {ECO:0000250}.
Interaction partners:
Sequence:
MSSSANSSPATTKFKFTDNLWDGFDLLVKRTDNDLIQSKNILNFFKKKAELEEQHSKKLEKLSLKTMMTIDESTSINAISYNSSWKKIINSSMMESEQHTLLNTSILNKVIQPLQAMIKDMETKRKKILQEGIKLKQDMKEMVDELKKSQFKYDKAGKDLESSRMELREYREQLDHQQQQQPSDSDLNNISKIERRIQRCEQDFSNCDEEYREQIKATNDFQHLYNTEKLPKILNDFEHFVISHSHFSKSYFTNLVSVLIELPSAYQQNYEFVKKSVEMIDITNDVQEFIRKNLMKKQLAQPFQYEPYIEGKLTKKTISLTWNNKILSQFSRSSNNNTATANNTSSGNLNPYLNGGIGGTKKDEPILPTASFKVSLDELMNRQKDNHPTLEVPYVLQVLSTRIAQMKGHVTEGIFRVPGIISTIKETRLRIDKADFNLSNIDDVRTPAALLKQWLRDIPTALIPDSLYQQCIDTPTNAIAIVKTIPIINQRVLCYLINFLQIFTKFEFVAHSKMGTSNLAMVFAPCILRCTSTDANVMLNNVPNERLFVETLIKQIPPPLNTNEFLNLPISMSDAINDSEDIEELNDLDQLSNDDNNNSNTNTSNISIGSGSNSNIVVNYSNNSPNIESSTLPSQSVVTTIETLPPLNDDHNSGSGNESNSSSSNSTTTPTGSPTTASKPRGPRTQTLGWVRIKPAPKPSAEPTITLSSSIAAGTTTTTTTATGITTTTTTTAGPEKTIISPVIIKPAAATPTTTTPTTTPTTTTSPTTATIPAVSTSTIKTSSPDRTTPLTSSPPLASTKSTDELMKKLDQFTQETTPSIRIATTTTPTTITTPTTTATTTTITTDKTTPVTSSPPTASNISSEDLMKKLDQFINF
Protein: Coiled-coil domain-containing protein 86 (Q9XWP4)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTGANLLVMNDTCKSNRWWKTKQEKKHSEIKKVKTLKSTWDKKMELKAKKDMVKRVQDNIREKQVQERQEKKERKVEQEKRRLENERKAEIVQKITKIHKLKKTKKRQLRSIQMRDTTQVTK
Protein: Signal transducer and activator of transcription 5B (P52632)
Organism: Rattus norvegicus (Rat)
Function: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42232}. Nucleus {ECO:0000250|UniProtKB:P42232}. Note=Translocated into the nucleus in response to phosphorylation. {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK3
- Signal transducer and activator of transcription 5A
- Receptor protein-tyrosine kinase
- Cytokine-inducible SH2-containing protein
- Signal transducer and activator of transcription
- Interferon regulatory factor 9
- Signal transducer and activator of transcription 3
- Interleukin-2 receptor subunit alpha
Sequence:
MAMWIQAQQLQGDALHQMQALYGQHFPIEVRHYLSQWIESQAWDSIDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLITQDTESELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLNPQERMSRETALQQKQVSLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRLEHLCQQLPIPGPVEEMLAEVNATITDIISALSTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFDSQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFREPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNSSSNHLEDYNSMSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCERATAKAADGYVKPQIKQVVPEFVNASTDAGSGATYMDQAPSPVVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS
Protein: FYVE, RhoGEF and PH domain-containing protein 3 (Zinc finger FYVE domain-containing protein 5) (Q5JSP0)
Organism: Homo sapiens (Human)
Function: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Cell division control protein 42 homolog
- FYVE, RhoGEF and PH domain-containing protein 1
- Guanine nucleotide-binding protein G
- Melanocortin-2 receptor accessory protein
- Coronin-1A
- Serine/threonine-protein kinase WNK2
- Serine/threonine-protein kinase WNK3
Sequence:
MESGRGSSTPPGPIAALGMPDTGPGSSSLGKLQALPVGPRAHCGDPVSLAAAGDGSPDIGPTGELSGSLKIPNRDSGIDSPSSSVAGENFPCEEGLEAGPSPTVLGAHAEMALDSQVPKVTPQEEADSDVGEEPDSENTPQKADKDAGLAQHSGPQKLLHIAQELLHTEETYVKRLHLLDQVFCTRLTDAGIPPEVIMGIFSNISSIHRFHGQFLLPELKTRITEEWDTNPRLGDILQKLAPFLKMYGEYVKNFDRAVGLVSTWTQRSPLFKDVVHSIQKQEVCGNLTLQHHMLEPVQRVPRYELLLKDYLKRLPQDAPDRKDAERSLELISTAANHSNAAIRKVEKMHKLLEVYEQLGGEEDIVNPANELIKEGQIQKLSAKNGTPQDRHLFLFNSMILYCVPKLRLMGQKFSVREKMDISGLQVQDIVKPNTAHTFIITGRKRSLELQTRTEEEKKEWIQIIQATIEKHKQNSETFKAFGGAFSQDEDPSLSPDMPITSTSPVEPVVTTEGSSGAAGLEPRKLSSKTRRDKEKQSCKSCGETFNSITKRRHHCKLCGAVICGKCSEFKAENSRQSRVCRDCFLTQPVAPESTEKTPTADPQPSLLCGPLRLSESGETWSEVWAAIPMSDPQVLHLQGGSQDGRLPRTIPLPSCKLSVPDPEERLDSGHVWKLQWAKQSWYLSASSAELQQQWLETLSTAAHGDTAQDSPGALQLQVPMGAAAP
Protein: Diacylglycerol kinase theta (DAG kinase theta) (EC 2.7.1.107) (EC 2.7.1.93) (Diglyceride kinase theta) (DGK-theta) (Q6P5E8)
Organism: Mus musculus (Mouse)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Within the adrenocorticotropic hormone signaling pathway, produces phosphatidic acid which in turn activates NR5A1 and subsequent steroidogenic gene transcription (By similarity). Also functions downstream of the nerve growth factor signaling pathway being specifically activated in the nucleus by the growth factor (By similarity). Through its diacylglycerol activity also regulates synaptic vesicle endocytosis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52824}. Cytoplasm, cytosol {ECO:0000269|PubMed:26748701}. Cell membrane {ECO:0000250|UniProtKB:P52824}. Synapse {ECO:0000269|PubMed:26748701}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus {ECO:0000250|UniProtKB:P52824}. Nucleus speckle {ECO:0000250|UniProtKB:P52824}. Nucleus matrix {ECO:0000250|UniProtKB:D3ZEY4}. Note=Translocates to the plasma membrane in response to steroid hormone receptor stimulation. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH. Translocates to the nucleus in response to thrombin stimulation (By similarity). Association with the nuclear matrix is regulated by nerve growth factor (By similarity). {ECO:0000250|UniProtKB:D3ZEY4, ECO:0000250|UniProtKB:P52824}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Phospholipase D2
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipase D1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- Phosphatidate cytidylyltransferase 2
- Lysocardiolipin acyltransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 1
Sequence:
MAAAAEPGARTWPGSGSPRLGSPAGSPVLGISGRTRPGSGPERTSRAIGSAAPGHSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKQVKTPCTSIAPSLVRVPVAHCFGSLGLYKRKFCVVCRKSLEVPAFRCEVCELHVHPDCVPFACSDCRQCHQDGQQDYDTYHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSVCSTALAPECTFGRLRSMVLPPSCVRLLSRNFSKMHCFRIPETMVLELGDGDDGVDGSAAIGTGREVLTATESTKQTLKIFDGNDSMRKNQFRLVTVSRLARNEEVMEAALRAYYISEDPKDFQLQALPLSGNAQALGKAGTTEEEASKGSCPRDSVPEAWVIRSLPRTQEILKIYPGWLKVGVAYVSIRVNSQSTARSVVQEVLPLFGQQVEDKERFQLIEVLMSSRQVQRTVLADEEPLLDRLWDIRQTSVRQVSQTRFYVAETRATAPRVSLFVGGLPPGLSPQDYSNLLHEAMATKAAVVSVSHVYSLQGAVILDVTCFAEAERLYMLARDTAVHGRPLTALVLPDVLHTKLPPDCCPLLVFVNPKSGGLKGRELLCSFRKLLNPHQVFELTNGGPLPGFHLFSQVPSFRVLVCGGDGTVGWVLAALEETRRHLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLVSVDEADAVLMDRWTILLDAHEIDSTENNVVETEPPKIVQMNNYCGIGIDAELSLDFHQAREEEPGKFTSRFHNKGVYVRVGLQKISHSRSLHKEIRLQVEQQEVELPSIEGLIFINIPSWGSGADLWGSDNDSRFEKPRIDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWVQAPGHMIISATAPKVHMLRKAKQKPRKAGANRDTRVDTLPAPEGNPL
Protein: Uncharacterized membrane glycoprotein YNR066C (P53752)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative uncharacterized protein YBR285W
Sequence:
MILLQVICTIWTCLFIPLLNAEEFVPKVTETLSEYSFSLESFDDSNSLIRLDNQVVWISSDSGENWEAVKEIEGHILELIVDPLHGQDRAFVSIHLSPKFYVTDDRGKSWRALTIPVSENCRLGTSCSIATHPTDKKYLIADCPCFINDNGYIQIQNETYFTNDGESFYNIEPSLKKKEDDHITSSSCNFVKSSKDSDIEGNDASILCLFSNHGYDSDRHLSAAYTQLALSTDGGKTFKKFDEFNDKIIYQYKILKSHIIVSTQDDRYNEMSPMDIWISNDASTFQKARLPAQVRHVHMYGIYEDSIGRIIIPISTIFTDEKNDQPAPSEILISDSQGLKFLPVEWTINPHFGYIDIASPHFLEGTIIGSFHPSFDYSHNKGKYNKKIARYETKISVDNGLTWSNLKVVDEENADSFPCDITRPERCSLQNPFYSI
Protein: Protein cbp-1 (EC 2.3.1.48) (P34545)
Organism: Caenorhabditis elegans
Function: Acetyltransferase enzyme (By similarity). Acetylates histones, giving a specific tag for transcriptional activation (By similarity). May prevent DNA damage-induced apoptosis by inhibiting cep-1-dependent transcription activation of the programmed cell death activator egl-1. In differentiated cells, negatively regulates localization of heterochromatin to the nuclear periphery. Plays a role in migration of gonadal distal tip cells, where it probably modulates expression of genes involved in integrin-mediated adhesion.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92793}.
Interaction partners:
- Forkhead box protein O
- histone acetyltransferase
- Protein pop-1
- Suppressor of hairless protein homolog
- Protein skinhead-1
- DNA repair and recombination protein RAD54-like
- XPA C-terminal domain-containing protein
- Putative transcription elongation factor S-II
- Hypoxia-inducible factor 1
- Histone deacetylase 1
Sequence:
MDEPPSKKSRADSDYDSGLDALSALESLEAFPTSSKDTDVDNNPSTSAGGSGGPSGSTPHPQGTPQPAPSNNGGFNLQPGQSQPQQPPQNMGGGVNGSVLQELLMNPSQTSNNSPRPQAYPPGQQNAFNRSPMMPNGTPNMMSPPSMGRVPGPSPGGPQPPGPGQPQMRPGQPGMFQGDQQQQMMMGAQGQQFPGMMHRYPYAQGGPPPGAQGMPQGYPGVSRGGPTPGQPMGRGAMMNGAMPRSGPMPTQGRPGIPPNQQAMMQPMMTDRQFMQHGQYGQQRPEFMQQYGRPGGYPMMHQGMMMDSNGQPIRGPNQMMMMSNGHPGMSHGPPNGQPGPQAAAAQHAAQQQAAAQAQAQAAAQQQQQQQREQEAAAAAQRNGAGRATTPGSSMLATHQDPEKRKLIQQQLVLLLHAHKCSQREKENRDFAAKNQPPPHAACTLPHCSTMKEVLTHMTSCNVGRLCHSDTTQTTKKCSVAHCASSRQIIAHWKNCSREDCPVCKPLKRIQDTPLQFSLPDLANLIGVNGNSNGSAEGDGLHQFGSPAMRTGNITNSLFEGFNGNPFQNGPNRGGPRPPGGNGEIPNLPPPDMPDCTKEWHHQVTKDLRNHLVGKLVKAIFPEPNQEAMNDNRLKDLIAYARKVEKEMFESANDREEYYHLLAEKIYKIQKELQEKKNSRLNQGAAAHDQYAIPPSNELAQMLGVEGGRSDVHSEGSSMAVAPSQQNQPWGGAPNSNMHQQIPPNGQVPQVNNSSTFPSSGNSTPNIGASSTVSAMLQPKTEPMDDQNTDSLSSRPPTAIGFGGSSSSTPAPIMNGIVKKEEDPEESSNQAPPSVKDTKDGVAESKPKEQQAKREPTPPPTEDTVFSQEDLIKFLLPVWEKLDKSEDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFVSEMDPVMKSMGYCCAKKLAFTPLSLFCYGAAMCTIAREQQYWVFEQSSTQYNVTVTERYTYCQKCFDALPPEGISLSENPNDRNNMAPKTSFTEQKNSVIDYEPFERCKYCMRKWHRICALHDKKVYPEGFICECCRTAKKYQKPDNKYLASKLPHNKLSTFLEDRVNGFIKKQLQAEAHKYPVIIRTLCVQDKEAEVKAQMKQKYVESNQFPEKFPYRTKAVFAFEIIDGVEVCFFGLHVQEYGSACPAPNARRVYIAYLDSVHFFQPRELRTDVYHELLLGYLDYAKMLGYTMAHIWACPPSEGDDYIFHCHPPEQKIPKPKRLQDWYKKMLEKGVQEGSVVEFKDIYKQARDDNLTTPTQLPYFEGDFWPNVIEDCIREASNEEAQRKVKEDDDDGEDADGGLGGGDSGKKKSSKNKKNNLKKNAKMNKKKAGSITGNEVADKLYSQFEKHKEVFFTIRLVSLQNEPAVLAKPISDPDGLMQSDMMDGRDTFLTKAREEHWEFSSLRRAKYSTLCLAYSLHETDSKGMEYTCNKCSSPAVWHCQSCDDFDLCDGCKPTTQHPHEMEKIKSLIGGGEAGDSAAGGTRYESIQRCIASLVHACQCRDANCRRMSCHKMKRVVQHTKMCKKRINGTCPVCKQLIALCCYHAKHCTRDACTVPFCMNIRQKLAEQKRSQQRRADMMMRRRMEGLQSHVGGAAPTPSTVSNGTPSNAPTPPVSAGPGPAVKGGGVGQVQMQQHQGSHVGGSGPAGMGQPMNSFGGMPGMGLGPNAQNGPGLPGMNPQMNANQSRYMPNGPGLGQSGAPGQQQQPMYSSGMPMQRPGGLGGMNPQQQPQQQQGHPGLQNPGGRPGGVHGMGQNQPVRNNQDMVMNMQMQNQHQQPPPFDSTLQPQIMKINSRLKAAKTEEERETVFSDLKKTPHLFHAWLRMRENQNLVPNRMQGYSQMSMGSSNLQNLQQQQLQQQQAGAMRGGGGFAPGQNNSQPRAPSGQFASMNPSMQQQYPQQQQGWPQQRQQNPGGMQQNANPYNQFQNRQNMMMMPQQQQPHPSNAGGQ
Protein: Importin-7 (Imp7) (Ran-binding protein 7) (RanBP7) (Q9EPL8)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (By similarity). In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:34995814, ECO:0000269|PubMed:35922041}. Nucleus {ECO:0000269|PubMed:34995814, ECO:0000269|PubMed:35922041}. Note=Localizes to the nucleus in the presence of BMP4. {ECO:0000269|PubMed:34995814}.
Interaction partners:
- Importin subunit beta-1
- Transportin-1
- Importin-5
- Transportin-3
- Importin-9
- Exportin-1
- Importin-4
- Ubiquitin-like protein FUBI
- Exportin-T
- Importin-13
Sequence:
MDPNTIIEALRGTMDPALREAAERQLNEAHKSLNFVSTLLQITMSEQLDLPVRQAGVIYLKNMITQYWPDREATPGDIAPYTIPEEDRHCIRENIVEAIIHSPELIRVQLTTCIHHIIKHDYPSRWTAIVDKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLVAAMQHFLPVLKDRFIQLLSDQSDQSVLIQKQIFKIFYALVQYTLPLELINQQNLTEWVEILKTVVNRDVPNETLQVEEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNEFAEVFLKAFAVGVQQVLLKVLYQYKEKQYMAPRVLQQTLNYINQGVSHALTWKNLKPHIQGIIQDVIFPLMCYTDADEELWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTACSKRKEVLQKTMGFCYQILTEPNADPRKKDGALHMIGSLAEILLKKKIYKDQMEYMLQNHVFPLFSSELGYMRARACWVLHYFCEVKFKSDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYITPFIRPVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEGSDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAHSLTCQQVSPQMWQLLPLVFEVFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYSMCKKVLTGVAGEDAECHAAKLLEVIILQCKGRGIDQCIPLFVEAALERLTREVKTSELRTMCLQVAIAALYYNPHLLLNTLENLRFPNNVEPVTNHFITQWLNDVDCFLGLHDRKMCVLGLCALIDMEQIPQVLNQVSGQILPAFILLFNGLKRAYACHAEHENDSDDDEDAEDDDETEELGSDEDDIDEDGQEYLEILAKQAGEDGDDEDWEEDDAEETALEGYSTIIDDEDNPVDEYQIFKAIFQTIQNRNPVWYQALTHGLNEEQRKQLQDIATLADQRRAAHESKMIEKHGGYKFSAPVVPSSFNFGGPAPGMN
Protein: H/ACA ribonucleoprotein complex subunit 2 (Nucleolar protein family A member 2) (Q8IIC4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU366039}.
Interaction partners:
- Nucleolar protein 5, putative
- Nucleolar protein 56
- rRNA 2'-O-methyltransferase fibrillarin
- U3 small nucleolar RNA-associated protein 4, putative
- U3 small nucleolar RNA-interacting protein 2, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- Small ribosomal subunit protein eS30
- WD repeat-containing protein, putative
- U4/U6 small nuclear ribonucleoprotein PRP31, putative
- Small ribosomal subunit assembling AARP2 protein
Sequence:
MSNTLISNESVHNSEVEEEEEEINAKIFPLASPELTNQILDVIQRATVYRQLKRGANEAVKSLHKGISELVVLAADAKPLEIISHIPLVCEDKNTPYVYVRSKMALGRACGISRSVIATSIVTKDGSPLETQITELKDLIEQMLI
Protein: Alanyl-tRNA editing protein AlaX-S (AlaX-S) (Alanyl-tRNA deacylase AlaX-S) (PhoAlaX) (O58307)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Functions in trans to edit the amino acid moiety from mischarged charged Ser-tRNA(Ala). Has little activity against Gly-tRNA(Ala).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Alanyl-tRNA editing protein AlaX-M
- Alanyl-tRNA editing protein AlaX-L
- Uncharacterized protein
- 449aa long hypothetical damage-inducible protein
Sequence:
MYSIEVRTHSALHVVKGAVVKVLGSEAKWTYSTYVKGNKGVLIVKFDRKPSDEEIREIERLANEKVKENAPIKIYELPREEAEKMFGEDMYDLFPVPEDVRILKVVVIEDWNVNACNKEHTKTTGEIGPIKIRKVRFRKSKGLLEIHFELLELENPS