wanglab/gogpt-training-data huggingface dataset:
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (Q6FLV3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA topoisomerase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- DNA repair protein RAD51 homolog
- Double-strand break repair protein
- Serine/threonine-protein kinase MEC1
- ATP-dependent DNA helicase
- Replication protein A subunit
- Candida glabrata strain CBS138 chromosome M complete sequence
- DNA repair and recombination protein RAD52
Sequence:
MVTKPSNNLRREHAWLKESNIFDNDNDILLSTLSKQFSNKKSTNEYNKGSLILHNVGSIDRNETIEVLDDDDDDDIILTNISKPNELSKAQTATSSPKNNMNPNAMNEIQRDVSTSSRVVSTYSGSNSYPFISKDISPKNVCNSSDNLQQSTLPVVYRDKRSNKTIDGSIPVLKAQKELIEKLKDLNKTMTSKIDIMESTSLSEDYKRTQINTVINPKIKSKQSEIEKMELKLETLSQEIKNISHILSDISNENVFKNIKSQKFDSQRASITANNSLTDLQINEGFNNNITKNNRDFNPIPDNSVIRGQQVNMSSFQEESLYIDSYNEPNTQSRAPYTRQMRDRHQINYRIPEADEPFEYRVGKLQPTIASDDTTYDAENTDNPDEDGYLTTQDGEKHSDVHQSDLDFIEDSPSEITHDTAYVETNNNETSSRIQIIMSSPNRLDEYGPSVQSQIDLSGDSLDSNHNVGYKMEYIGESDFNINTGATNTKHTEVIENLSTDSDNWGEVENLTDYDAESFDEERENKTRVSDIEELDNELEIITERKIGNGDGFMLTSVKKEESAIVSLSESHPTSLTDDELEEDISLLGVAENAESPPHTHITDVVSPNSWTKEVYKKLKTVFNLTSFRSNQEEAINATLSGKDVFVLMPTGGGKSLCYQLPAIVKGGCTKGTTIVISPLISLMQDQVEHLQKLNVKARMLSSKGGIDEKNHTFNLFINGFLDLIYLSPEMISVSEKCKTAIEKLYQNKQLARIVVDEAHCVSNWGHDFRPDYKQLSYFKVQYPDIPMMALTATASEQVQMDIVFNLKLKDNLFLRQSFNRTNLYYEVRKKTKNTIFEICDTIKQQFRNQTGIIYCHSKNSCEQTAQQMQRNGIKCAYYHAGMEADERLQVQREWQNDNLQVICATVAFGMGIDKADVRFVFHFTVPRTLEGYYQETGRAGRDGNYSYCITYYSFRDVRTMQTMIQKDKNLDGINKQKHLDKLQQVTAYCENDTDCRRKLVLSYFSEEFDPINCNKNCDNCRNSSSVTKEERDVTSTAISIVKLVQSIQNQKVTLIYCQNIFKGSRNSKIVQAGHDMLPQHGAGKNLTKSEIERIFFHLITKRILQEYSKVNNAGFSSSYVKVGDGCRDLLNGKLQLKIQFSVSEGNSRSSAGLPKSNSSNTNNYDRSLTKNITANNDSEQHLRNYAYSPSNSERMRAESSKHTGSTQEVNDLKSAYDRLRNAAISWGSRMVPAVNKFMDDNVLRRLAAILPATEEEFIGIVGNNSTDSKKYKYFKDIFIDLRKRRIERMCNLSSNFAFNEEGQSQIDTMEIQTTSRFFNNTDENKNLVSLTPYEQSTQVSKGVNARTAGGKKYKRNFNYKRYRNYNKWKK
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.27) (RING-type E3 ubiquitin transferase) (K7EPJ5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
Interaction partners:
Sequence:
MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKISWKVSQARFIMASGPRTTGAAPRGGSGAPGRASPQPREPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKKSKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPGRPTSMETAHGLATTS
Protein: OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne) (B2RUR8)
Organism: Mus musculus (Mouse)
Function: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B. Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2. Mediates deubiquitination of EGFR (By similarity). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains. Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure. Hydrolyzes both linear and branched forms of polyubiquitin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6GQQ9}. Nucleus {ECO:0000250|UniProtKB:Q6GQQ9}. Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q6GQQ9}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- TNF receptor-associated factor 3
- Parkinson disease protein 7 homolog
- TNF receptor-associated factor 6
- Ubiquitin thioesterase otulin
- Ubiquitin-ribosomal protein eL40 fusion protein
- UBX domain-containing protein 7
- Zinc finger-containing ubiquitin peptidase 1
- OTU domain-containing protein 3
Sequence:
MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVSAALSDFEQLRQVHAGNLSPPFSGGSTCPKTPEKGGSDREPTRPSRPILQRQDDVIQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSSEHPLEMPICAFQLPDLTVYKEDFRSFIERDLIEQSMLVALEQAGRLNWWVSMDSTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYALMEKGVEKEALRRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGSNGASGGGVESSEEPVYESLEEFHVFVLAHVLKRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKESAKEQAVIPLTDSEHKLLPLHFAVDPGKGWEWGKDDNDNVRLASIILSLEVKLHLLHSYMNVKWIPLSSDSQAPLAQPESPTASAGDEPRSTPESGESDKESVGSSSLGNEGSRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGPKPGGLGSGSGISSGTETLEKKKKNNTLKSWKGGKEEAAGDGPVSEKPPSESVGNGGSKYSQEVMQSLSTMRIAMQGEGKYIFVGTLKMGHRHQYQEEMIQRYLADAEERFLAEQKQKEVERKIMNGGLVSGPPPAKKPEPDGGEDQPSDSPAEPKAMAFSTAYPGGFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPSYATFPRQYPGRPYPHQDNIPALEPGKDGVHRGALLPPQFRVADSYSNGYREPPEPDGWAGAPRGLPPTQTKCKQPNCSFYGHPETNNLCSCCYREELRRREREPGGELLAHRF
Protein: Probable mannosyltransferase KTR7 (EC 2.4.1.-) (P40504)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possible glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAIRLNPKVRRFLLDKCRQKRYGFLFLGCIFAILYCMGTWPFFAKDIVHDPNNLPYSLQDYSTDKDEPFFRGCTDTKLYLQNPAYSKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVRNSLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVLITELYWTVPNLFRTTKSFIKKTAGLKENLGTLWKLFTFNYNILDTDDEEISRWVNFPWDAKPKLTEKLMVDFLLENHGQVNNEEDLEGIQYLVERARSKVPMLEDSLEGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSIGLGMTLDLEDVHYFRDIGYRHSSLQHCPKNALQSQENLNTFDEGYNFGCGCRCVCPKKGEDIEDHSTPCMDIFFELLHGREYEKEFPGCYKPSIKDKDVIEEIRRENFRVIE
Protein: Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese) (P52196)
Organism: Mus musculus (Mouse)
Function: Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Sulfite oxidase, mitochondrial
- Cystathionine gamma-lyase
- Persulfide dioxygenase ETHE1, mitochondrial
- Adenylyltransferase and sulfurtransferase MOCS3
- Cysteine desulfurase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- 3-mercaptopyruvate sulfurtransferase
- Putative aspartate aminotransferase, cytoplasmic 2
- Kynurenine--oxoglutarate transaminase 1
Sequence:
MVHQVLYRALVSTKWLAESIRSGRLGPSLRVLDASWYSPGTRQARKEYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGNLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQGRYLGTQPEPDIVGLDSGHIRGSVNMPFMDFLTKDGFEKSPEELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPETRVSQGKSGKA
Protein: BAG family molecular chaperone regulator 1 (J3QTA2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE
Protein: Alkali-sensitive linkage protein 1 (Q09788)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Secreted, cell wall {ECO:0000269|PubMed:17230583}. Note=Covalently attached to the cell wall. {ECO:0000269|PubMed:17230583}.
Interaction partners:
- 1,3-beta-glucanosyltransferase gas5
- 1,3-beta-glucanosyltransferase gas1
- Uncharacterized WD repeat-containing protein C17D11.16
- Small ribosomal subunit protein bS18m
Sequence:
MRTTFATVALAFLSTVGALPYAPNHRHHRRDDDGVLTVYETILETVYVTAVPGANSSSSYTSYSTGLASVTESSDDGASTALPTTSTESVVVTTSAPAASSSATSYPATFVSTPLYTMDNVTAPVWSNTSVPVSTPETSATSSSEFFTSYPATSSESSSSYPASSTEVASSYSASSTEVTSSYPASSEVATSTSSYVAPVSSSVASSSEISAGSATSYVPTSSSSIALSSVVASASVSAANKGVSTPAVSSAAASSSAVVSSVVSSATSVAASSTISSATSSSASASPTSSSVSGKRGLAWIPGTDLGYSDNFVNKGINWYYNWGSYSSGLSSSFEYVLNQHDANSLSSASSVFTGGATVIGFNEPDLSAAGNPIDAATAASYYLQYLTPLRESGAIGYLGSPAISNVGEDWLSEFMSACSDCKIDFIACHWYGIDFSNLQDYINSLANYGLPIWLTEFACTNWDDSNLPSLDEVKTLMTSALGFLDGHGSVERYSWFAPATELGAGVGNNNALISSSGGLSEVGEIYIS
Protein: TcdA protein (O86141)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004165}. Host cytoplasm, host cytosol {ECO:0000256|ARBA:ARBA00023586}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
VLISKEELIKLAYSIRPRENEYKTVLTNLDEYNKLTTNNNENKYLQLKKLNESIDVFMNKYKNSSRNRALSNLKKDILKEVILIKNSNTSPVEKNLHFVWIGGEVSDIVLEYIKQWADINAEYNIRLWYDSEAFLVNTLKKAIVESSTTEALQLLEEEIQNPQFDNMKFYKKRMEFIYDRQKRFINYYKSQINKPTVLTIDDIIKSYLISEYNRDETLLESYRTNSLRKINSNHGIDVRANSLFTEQELLNIYNQELLNRGNLAAASDIVRLLALKNFGGVYLDVDMLPGIHSDLFKTISRPSSIGLDRWEMIKLEAIMKYKKYINNYTSENFDKLDQQLKDNFKLIIESKSEKCEIFSKLENLNVSDLEIKIRFALGSVINQALISKKGSYLTNLVIEQIKNRYQFLNQHLNPAIESDNNFTDTTKIFHDSLFNSATAENSMFLTKIAPYLQVGFMPEARSTISLSGPGAYASAYYDFINLQENTIEKTLKASDLIEFKFPENNLSQLTEQEINSLWSFDQASAKYQFEKYVKDYTGGSLSEDNEVDFNKNTALDKNYLLNNKIPSNNVEEAGSKNYVHYIIQLQGDDISYEATCNLFSKNPKNSIIIQRNMNESAKSHFLSDDGESILELNKYRIPERLKNKEKVKVTFIGHGKDEFNTSEFARLSVDSLSNEISSFLDTIKLDISPKNVEVNLL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (X2JC83)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPAGRETVTKQRSMDVERRRRANTLEREMRDPTSICNVDCLLDTVSALVSDCDHESLRRLKNIEQYAAKYKPLAMQINQLRMNVEDFHFIKLIGAGAFGEVQLVRHKSSSQVYAMKRLSKFEMMKRPDSAFFWEERHIMAHANSEWIVQLHFAFQDAKYLYMVMDFMPGGDIVSLMGDYDIPEKWAIFYTMEVVLALDTIHNMGFVHRDVKPDNMLLDSYGHLKLADFGTCMRMGANGQVVSSNAVGTPDYISPEVLQSQGVDNEYGRECDWWSVGIFLYEMLFGETPFYADSLVGTYGKIMDHKNSLSFPPEVEISEQAKALIRAFLTDRTQRLGRYGIEDIKAHPFFRNDTWSFDNIRESVPPVVPELSSDDDTRNFEDIERDEKPEEVFPVPKGFDGNHLPFIGFTYTGDYQLLSSDTVDAESKEANVANSGAASNNHGHGHNHRHRPSNSNELKRLEALLERERGRSEALEQQDAGLRQQIELITKREAELQRIASEYEKDLALRQHNYKVAMQKVEQEIELRKKTEALLVETQRNLENEQKTRARDLNINDKVVSLEKQLLEMEQSYKTETENTQKLKKHNAELDFTVKSQEEKVRDMVDMIDTLQKHKEELGQENAELQALVVQEKNLRSQLKEMHKEAENKMQTLINDIERTMCREQKAQEDNRALLEKISDLEKAHAGLDFELKAAQGRYQQEVKAHQETEKSRLVSREEANLQEVKALQSKLNEEKSARIKADQHSQEKERQLSMLSVDYRQIQLRLQKLEGECRQESEKVAALQSQLDQEHSKRNALLSELSLHSSEVAHLRSRENQLQKELSTQREAKRRFEEDLTQLKSTHHEALANNRELQAQLEAEQCFSRLYKTQANENREESAERLSKIEDLEEERVSLKHQVQVAVARADSEALARSIAEETVADLEKEKTIKELELKDFVMKHRNEINAKEAALATLKEAENELHKKLGQKAAEYEDLVQQHKKQQEELALMRSSKDEEITKLLDKCKNEVLLKQVAVNKLAEVMNRRDSDLPKQKNKARSTAELRKKEKEMRRLQQELSQERDKFNQLLLKHQDLQQLCAEEQQLKQKMVMEIDCKATEIENLQSKLNETASLSSADNDPEDSQDSVFEGWLSVPNKQNRRRGHGWKRQYVIVSSRKIIFYNSDIDKHNTTDAVLILDLSKVYHVRSVTQGDVIRADAKEIPRIFQLLYAGEGASHRPDEQSQLDVSVLHGNCNEERPGTIVHKGHEFVHITYHMPTACEVCPKPLWHMFKPPAAYECKRCRNKIHKEHVDKHDPLAPCKLNHDPRSARDMLLLAATPEDQSLWVARLLKRIQKSGYKAASYNNNSTDGSKISPSQSTRSSYKPYAVNVQRSATLPANSSLK
Protein: Probable transcriptional regulatory protein (Probably TetR/AcrR-family) (O53323)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MPPVTRTTEPPRRGGRGARQRILKAAAELFYCEGINATGVELIANKASVSKRTLYQHFPSKSALVEEYLRGLRQAAGEADKMPKASNATPRERLLALFDRPNRGDGRMRGCPFHNAAVEAAGEMPGVERIVHSHKRDYIKGLARLAREAGAAHPRSLGNQLAVLFEGAAALSTSLDDAGPWAHARAAAEVLIDQATARPV
Protein: Kinesin-like protein KIF22 (Kinesin-like DNA-binding protein) (Kinesin-like protein 4) (Q14807)
Organism: Homo sapiens (Human)
Function: Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). Plays a role in congression of laterally attached chromosomes in NDC80-depleted cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:8599929}. Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-like protein KIF2C
- Kinesin-like protein KIF11
- Transforming acidic coiled-coil-containing protein 3
- Odorant-binding protein 2b
- Myc-associated zinc finger protein
- Kinesin-like protein KIFC1
- Baculoviral IAP repeat-containing protein 5
- Protein regulator of cytokinesis 1
- Rac GTPase-activating protein 1
- Serine/threonine-protein kinase PLK1
Sequence:
MAAGGSTQQRRREMAAASAAAISGAGRCRLSKIGATRRPPPARVRVAVRLRPFVDGTAGASDPPCVRGMDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQPHALGPVKLSQKELLGPPEAKRARGPEEEEIGSPEPMAAPASASQKLSPLQKLSSMDPAMLERLLSLDRLLASQGSQGAPLLSTPKRERMVLMKTVEEKDLEIERLKTKQKELEAKMLAQKAEEKENHCPTMLRPLSHRTVTGAKPLKKAVVMPLQLIQEQAASPNAEIHILKNKGRKRKLESLDALEPEEKAEDCWELQISPELLAHGRQKILDLLNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQMESFLKANILGLAAGQRCGAS
Protein: H/ACA ribonucleoprotein complex subunit GAR1 (Glycine/arginine-rich protein 1) (snoRNP protein GAR1) (P28007)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA. Essential for growth.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12756332, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9843512}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit CBF5
- H/ACA ribonucleoprotein complex subunit NHP2
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit NOP10
- Nucleolar protein 58
- Nucleolar protein 56
- Protein SHQ1
- 13 kDa ribonucleoprotein-associated protein
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- tRNA pseudouridine synthase 4
Sequence:
MSFRGGNRGGRGGFRGGFRGGRTGSARSFQQGPPDTVLEMGAFLHPCEGDIVCRSINTKIPYFNAPIYLENKTQVGKVDEILGPLNEVFFTIKCGDGVQATSFKEGDKFYIAADKLLPIERFLPKPKVVGPPKPKNKKKRSGAPGGRGGASMGRGGSRGGFRGGRGGSSFRGGRGGSSFRGGSRGGSFRGGSRGGSRGGFRGGRR
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I643)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGPQPAVTDYSKATNVKYLFDLIGETVQKKAKEKADVASRKYFEELHGDLSKATYKKDKNPEGTTPPNPCKLEYQYHTNVTKGEDKEYPCLGRKTVRFSDKEGAECYKTKIKDSTTDTVGACAPYRRLYMCDRNLEHIEPTKITTHNLLLDVCLAAQYEGQSISQNHGKHQLSYPDSPSQLCTELARSFADIGDIVRGRDLYRGNNRENDKLEKKLKGYFKKIYDNLVEKKKEEAETDYKDDAPDFYQLREDWWALNRQDVWKAITCDAHDSRYRKMGADGSITESAMRQCRNVADVPTNFDYVPQYLRWFEEWAEDFCRKRKHKLKDAIQKCRGQDGTGKDRYCDLNRYDCKRTISAKHELVQGEECKKCSVVCIPFGPWIDNQKQEFEKQKNKYTNEINKKHDETTKEISGNRRKKRSLTTKNYKGYDEEFYKIFKDEYPDVDKFLDLLSKETACESQPYDEPRTISINFKNYKNPDIFSHTEYCQACPWCGMTCTFDGKCTKNPEELCHHKIVQKEYPDTNTTDIPILTPDTTKSNIVEKYRNFCNSSDDNNSDQINNWQCHYDESKKSGQNDNCVEGTWQNFKKDQKVTSYNAFFWKWVSEMLDDSIKWRAELDKCLKNDKKTCGKKKCNRDCKCFKKWVEQKKEKEWKAIKKHFKKQKDMIETGMPPEMALKILLNDVFLQDMEKAQGDPQHIAKIKELLKKNDEKVNNLSNMETIFDFLLQEEEQDAQKCVSNNPEKCEETQKPPTDGAPGGAGPSPDTGTDDNLEDIDSDGEEDDDVSHVDEEEPEDNPVEGSSEEEKQEVVKDTEAAVPKQDTQPKEEVNPCKIVEELFKSTKNFEDACGLKYGKNYGWKCVPTTSDKGSEPTARGHSHVARSADGAPSGDKDGAICIPPRRRKLYLHKIEGVDTTDDKSLRKWFIESAAVETFFLWDRYKKLNTPQSGSPLLGGGLPGVGVENGDDENNPEKLLQKGEIPDGFLRQMFYTLGDYRDILFSGDKDKKNGYSDIVSGDNVIKERENTIKEKIASFFQNGNKEGTPHVPKNPVQTPQTWWKDNAKHIWHGMICALTYEEKTSGSDGEKKIEKDDAVYKKFFGTPNGNPLPQPGTNGTSNEPISQYQYDQVVLKEENNGAMSTSPKSTSAAPSDNTPTTLTQFVLRPTYFRYLEEWGQNFCKERKKRLAQIYEDCRGNDKVCSGDGEDCEEVRKQDYSKISNFNCPGCGRECRKYKNWIKTKRTEFDEQKKAYVDRKDKYKTENKGAESKHHSISDQNFVKKLGTDYASIESFLEKLGSCSKNNKDNGDGTINFKEPDVTFKPADNCKPCSEFKVKCENGKCSGGGKKVNCNRKNTIAATEIANMINSTEGVFMTVSDNSDHKFEGGLEPCGSANIFKGIRKDVWKCGEYCGVDICEPNTFDGKQNGKEYIQIRALLKRWVEYFLEDYNKIKHKISHCMRKGEKTICINDCVEKWINIKKKEWETIRERYVKQYTTGHSDIYKVTSFLEDPQFHNEVLKAIKPCGDLDKFQNSTDCTVAGSSENGVTNKKDIVECLLENLKTKAKTCPNQANGENQTCDSLPHVEDDDDEEPLEETEENTVEQPNICPQLPKPPPQPGDEDGCKQASPAPSEGTENQPPVIKPEEEAPAPRTPRPRPKPPQEPQPYLPPALKNAMLSSTIMWSIGIGFATFTYFYLKKKSKSSVGNLFQILQIPKSDFDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYVPGTPKYKTLIEVVLEPSGNNTTASGNNTTASGKNTPSDTQNDIPSGDTPNNKLTDNEWNTLKDEFISNMLQSEQPKDVPNDYSSGDIPFNTQPSTLYFDNNQEKPFITSIHDRDLYTGEEYNYNVNMSTNSMDDIPISGKNDVYSGIDLINDTLSGNHNVDIYDELLKRKENELFGTKHHTKHTNTYNVAKPARDDPLHNQLNLFHTWLDRHRNMCEKWKNDNERLAKLKEEWENDTSTSGNKHSDIPSGKLSDTPSDNNIHSDIHPSDIPSGKLSDIPSDNNIPSSNKTLNTDVSIQIDMNNPKTTNEFTYVDSNPNQVDDTYVDSNPDNSSMDTILEDLDKPFNEPYYDVQDDIYYDVHDHDTSTVDTNAMDVPSKVQIEMSVKNHKLVKEKYPIGDVWDI
Protein: Serine protease 7 (EC 3.4.21.-) (Melanization protease 2) (Q9V3Z2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease which, by cleaving and activating prophenoloxidase (PPO1) after immune challenge, plays an essential role in the melanization immune response to septic wounding. May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea. Important for the innate immune response to fungi. Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway.
Subcellular location: Secreted {ECO:0000269|PubMed:24260243}.
Interaction partners:
- Serine protease inhibitor 27A
Sequence:
MKSTRKVVGIFLATCLLPFTVLQNVAAQGSCRNPNQKQGQCLSIYDCQSLLSVIQQSYVSPEDRTFLRNSQCLDGVGRQPYVCCTSDRSFGSQEATSAAPPPTTTSSSSRGQDGQAGLGNLLPSPPKCGPHSFSNKVYNGNDTAIDEFNWMALLEYVDNRGRRELSCGGSLINNRYVLTAAHCVIGAVETEVGHLTTVRLGEYDTSKDVDCIDDICNQPILQLGIEQATVHPQYDPANKNRIHDIALLRLDRPVVLNEYIQPVCLPLVSTRMAINTGELLVVSGWGRTTTARKSTIKQRLDLPVNDHDYCARKFATRNIHLISSQLCVGGEFYRDSCDGDSGGPLMRRGFDQAWYQEGVVSFGNRCGLEGWPGVYTRVADYMDWIVETIRP
Protein: rRNA methyltransferase 2, mitochondrial (EC 2.1.1.-) (21S rRNA (uridine-2'-O)-methyltransferase) (P78860)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methyluridine corresponding to position 2791 in S.cerevisiae 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- rRNA methyltransferase 1, mitochondrial
- Uncharacterized GTP-binding protein P8A3.11c
- tRNA
- Pre-rRNA-processing protein esf2
- tRNA
- Mitochondrial GTPase 1
- rRNA-processing protein cgr1
- Nucleolar protein 58
- Large ribosomal subunit protein bL36m
- Uncharacterized RNA-binding protein C1827.05c
Sequence:
MFGSKTLFSWAAKRSKDFYRKKSKIDNFRSRAAYKLIELNSKYRFINKEDVVIDVGFAPGSWSQVAKKLVGNKGKVIGIDIQHIAPPEGVLPIYGDIRDPNTLTKLFEALRLLHEPNTNDSIDCRVVDAVISDMLHKATGIRIRDHALSMELCASALHVALTFLKSNGSFICKFYMGDEDADLQNLLKSHFRFVQVMKPKASLKESREAYFVCLERKP
Protein: Small G protein signaling modulator 2 (RUN and TBC1 domain-containing protein 1) (Q80U12)
Organism: Mus musculus (Mouse)
Function: Possesses GTPase activator activity towards RAB32, RAB33B and RAB38. Regulates the trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes by inactivating RAB32 and RAB38. Inhibits RAB32 and RAB38 activation both directly by promoting their GTPase activity and indirectly by disrupting the RAB9A-HPS4 interaction which is required for RAB32/38 activation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43147}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Melanosomal localization is mediated by RAB9A. {ECO:0000250|UniProtKB:O43147}.
Interaction partners:
- Ras-related protein Rab-9A
Sequence:
MGSAEDAVKEKLLWNVKKEVKQIMEEAVTRKFVHEDSSHIIALCGAVEACLLHQLRRRAAGFLRSDKMAALFTKVGKTCPVAEDICHKVQELQQQAEGRKPSGGSQEALRKQGSTGGKAPALSPQALKHIWVRTALMEKVLDRVVQYLAENCSKYYEKEALLADPVFGPILACLLVGPCALEYTKLKTADHYWTDPSADELVQRHRIRGPPNRQDSPAKRPALGIRKRHSSGSASEDRLAACAREYVESLHQNSRTRLLYGKNNVLVQPKEDMEAVPGYLSLHQSAENLTLKWTPNQLMNGTLGDSELEKSVYWDYALVVPFSQIVCIHCHQQKSGGTLVLVSQDGIQRPPLHFPQGGHLLSFLSCLENGLLPRGQLEPPLWTQQGKGKVFPKLRKRSSIRSIDVEELGVGRATDYVFRIIYPGHRHEHNAGDMIEMQGFGPSLTAWHLEPLCSQGSSCLSCSSSSSPYATPSHCSCIPDRLPLRLLCESMKRQIVSRAFYGWLAYCRHLSTVRTHLSALVHHNIIPPDRPPGASGGLTKDVWSKYQKDEKNYKELELLRQVYYGGVEHEIRKDVWPFLLGHYKFGMSKKEMEQVDTAVAARYQQVLAEWKACEVVVRQREREAHPATLTKFSSGSSIDSHVQRLVHRDSTISNDVFISVDDLEPSGPQDLEDSKPKREQEPGAGTPGIAAAEQQSVEFDSPDSGLPSSRNYSVASGIQSSLDEAQSVGFEDDGAGEDGSEGPATAAHTFPGPHDPGQETLAPASELEAGQELAAVCAAAYTIELLDTVALNLHRIDKDVQRCDRNYWYFTTSNLERLRDIMCSYVWEHLDMGYVQGMCDLLAPLLVILDNDQLAYSCFSHLMKRMGQNFPSGGAMDSHFANMRSLIQILDSELFELMHQNGDYTHFYFCYRWFLLDFKRELLYEDVFAVWEVIWAARRISSEHFVLFIALALVEAYREIIRDNNMDFTDIIKFFNERAERHDAQEILRIARDLVHKVQMLIDNK
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Glu-AdT subunit A) (EC 6.3.5.7) (Glutaminyl-tRNA synthase-like protein 1) (Q9H0R6)
Organism: Homo sapiens (Human)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:19805282}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Asparaginyl-tRNA synthetase
- Glutamine--tRNA ligase
- Asparagine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, mitochondrial
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- LIM domain-binding protein 1
Sequence:
MLGRSLREVSAALKQGQITPTELCQKCLSLIKKTKFLNAYITVSEEVALKQAEESEKRYKNGQSLGDLDGIPIAVKDNFSTSGIETTCASNMLKGYIPPYNATVVQKLLDQGALLMGKTNLDEFAMGSGSTDGVFGPVKNPWSYSKQYREKRKQNPHSENEDSDWLITGGSSGGSAAAVSAFTCYAALGSDTGGSTRNPAAHCGLVGFKPSYGLVSRHGLIPLVNSMDVPGILTRCVDDAAIVLGALAGPDPRDSTTVHEPINKPFMLPSLADVSKLCIGIPKEYLVPELSSEVQSLWSKAADLFESEGAKVIEVSLPHTSYSIVCYHVLCTSEVASNMARFDGLQYGHRCDIDVSTEAMYAATRREGFNDVVRGRILSGNFFLLKENYENYFVKAQKVRRLIANDFVNAFNSGVDVLLTPTTLSEAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVSIPVALSNQGLPIGLQFIGRAFCDQQLLTVAKWFEKQVQFPVIQLQELMDDCSAVLENEKLASVSLKQ