wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional glutathionylspermidine synthetase/amidase (GspSA) [Includes: Glutathionylspermidine amidase (Gsp amidase) (EC 3.5.1.78) (Glutathionylspermidine amidohydrolase [spermidine-forming]); Glutathionylspermidine synthetase (Gsp synthetase) (EC 6.3.1.8) (Glutathione:spermidine ligase [ADP-forming]) (Gsp synthase)] (P0AES0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1).
Interaction partners:
- Polyamine aminopropyltransferase
- Glutathione synthetase
- Glutathione reductase
- Uncharacterized protein YacC
- Glutathione S-transferase YfcF
- Glutathione-specific gamma-glutamylcyclotransferase
- Glutathione hydrolase proenzyme
- Glutathione S-transferase GstB
- Thioredoxin/glutathione peroxidase BtuE
- Glutathione S-transferase GstA
Sequence:
MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELGWDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDESLVIKKESDIEPLIVVKK
Protein: Alpha-1B-glycoprotein (Alpha-1-B glycoprotein) (P04217)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Growth factor receptor-bound protein 2
- Cysteine-rich secretory protein 3
- Tyrosine-protein phosphatase non-receptor type 11
- GRB2-associated-binding protein 2
- Alpha-2-HS-glycoprotein
- GRB2-associated-binding protein 3
- Adapter molecule crk
- Alpha-1-antitrypsin
- Protein AMBP
Sequence:
MSMLVVFLLLWGVTWGPVTEAAIFYETQPSLWAESESLLKPLANVTLTCQAHLETPDFQLFKNGVAQEPVHLDSPAIKHQFLLTGDTQGRYRCRSGLSTGWTQLSKLLELTGPKSLPAPWLSMAPVSWITPGLKTTAVCRGVLRGVTFLLRREGDHEFLEVPEAQEDVEATFPVHQPGNYSCSYRTDGEGALSEPSATVTIEELAAPPPPVLMHHGESSQVLHPGNKVTLTCVAPLSGVDFQLRRGEKELLVPRSSTSPDRIFFHLNAVALGDGGHYTCRYRLHDNQNGWSGDSAPVELILSDETLPAPEFSPEPESGRALRLRCLAPLEGARFALVREDRGGRRVHRFQSPAGTEALFELHNISVADSANYSCVYVDLKPPFGGSAPSERLELHVDGPPPRPQLRATWSGAVLAGRDAVLRCEGPIPDVTFELLREGETKAVKTVRTPGAAANLELIFVGPQHAGNYRCRYRSWVPHTFESELSDPVELLVAES
Protein: ABC-type transport system, permease protein, involved in antimicrobial peptide resistance (Q4QL74)
Organism: Haemophilus influenzae (strain 86-028NP)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
Interaction partners:
Sequence:
MFWSVLRHILWVALLLLVLSLLGFVILLRDPLNANLVTQNIYIGYFHYLGTLLQGDFGITYNGGKSLMNLILTVLPPTLELCFITLFLAFIFGLPLGIISAVNSEQVFAKSLQILSYVGLSIPIFWLAPILLYVAALSHWEIAAIGQYNLLYEIKPITGFPVIDMWFMEVPYRTKIVQNILQHLALPTLVLCILPTMEIIRIIHQRAEYILNQNFSKVATTRGWSKWKILHQYVFRNTFPLLVPQVPRVFTLVLTQCMLVETALGWPGIGRWLINAVNEQDYNSIAAGVIVIGVCIILIDTFTKIFTFILDPFKKKGWYAR
Protein: DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4) (Q9LL84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair. May be involved for T-DNA integration even if not absolutely required. Seems to be dispensable under normal growth conditions.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA repair protein XRCC4
- ATP-dependent DNA helicase 2 subunit KU80
- ATP-dependent DNA helicase 2 subunit KU70
- DNA-repair protein XRCC1
- DNA polymerase lambda
- At1g61410
- Transcription factor bHLH140
- Exonuclease 1
- Polynucleotide 3'-phosphatase ZDP
- Proliferating cellular nuclear antigen 1
Sequence:
MTEEIKFSVLVSLFNWIQKSKTSSQKRSKFRKFLDTYCKPSDYFVAVRLIIPSLDRERGSYGLKESVLATCLIDALGISRDAPDAVRLLNWRKGGTAKAGANAGNFSLIAAEVLQRRQGMASGGLTIKELNDLLDRLASSENRAEKTLVLSTLIQKTNAQEMKWVIRIILKDLKLGMSEKSIFQEFHPDAEDLFNVTCDLKLVCEKLRDRHQRHKRQDIEVGKAVRPQLAMRIGDVNAAWKKLHGKDVVAECKFDGDRIQIHKNGTDIHYFSRNFLDHSEYAHAMSDLIVQNILVDKCILDGEMLVWDTSLNRFAEFGSNQEIAKAAREGLDSHKQLCYVAFDVLYVGDTSVIHQSLKERHELLKKVVKPLKGRLEVLVPEGGLNVHRPSGEPSWSIVVHAAADVERFFKETVENRDEGIVLKDLESKWEPGDRSGKWMKLKPEYIRAGADLDVLIIGGYYGSGRRGGEVAQFLVALADRAEANVYPRRFMSFCRVGTGLSDDELNTVVSKLKPYFRKNEHPKKAPPSFYQVTNHSKERPDVWIDSPEKSIILSITSDIRTIRSEVFVAPYSLRFPRIDKVRYDKPWHECLDVQAFVELVNSSNGTTQKQKESESTQDNPKVNKSSKRGEKKNVSLVPSQFIQTDVSDIKGKTSIFSNMIFYFVNVPRSHSLETFHKMVVENGGKFSMNLNNSVTHCIAAESSGIKYQAAKRQRDVIHFSWVLDCCSRNKMLPLLPKYFLHLTDASRTKLQDDIDEFSDSYYWDLDLEGLKQVLSNAKQSEDSKSIDYYKKKLCPEKRWSCLLSCCVYFYPYSQTLSTEEEALLGIMAKRLMLEVLMAGGKVSNNLAHASHLVVLAMAEEPLDFTLVSKSFSEMEKRLLLKKRLHVVSSHWLEESLQREEKLCEDVYTLRPKYMEESDTEESDKSEHDTTEVASQGSAQTKEPASSKIAITSSRGRSNTRAVKRGRSSTNSLQRVQRRRGKQPSKISGDETEESDASEEKVSTRLSDIAEETDSFGEAQRNSSRGKCAKRGKSRVGQTQRVQRSRRGKKAAKIGGDESDENDELDGNNNVSADAEEGNAAGRSVENEETREPDIAKYTESQQRDNTVAVEEALQDSRNAKTEMDMKEKLQIHEDPLQAMLMKMFPIPSQKTTETSNRTTGEYRKANVSGECESSEKRKLDAETDNTSVNAGAESDVVPPLVKKKKVSYRDVAGELLKDW
Protein: Replication factor C subunit 4 (Replication factor C4) (Activator 1 37 kDa subunit) (P40339)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Proliferating cell nuclear antigen
- Replication factor C subunit 2
- Replication factor C subunit 3
- Telomere length regulation protein ELG1
- Replication factor C subunit 5
- Replication factor C subunit 1
- Checkpoint protein RAD24
- Chromosome transmission fidelity protein 18
- DNA damage checkpoint protein 1
- Sister chromatid cohesion protein DCC1
Sequence:
MSKTLSLQLPWVEKYRPQVLSDIVGNKETIDRLQQIAKDGNMPHMIISGMPGIGKTTSVHCLAHELLGRSYADGVLELNASDDRGIDVVRNQIKHFAQKKLHLPPGKHKIVILDEADSMTAGAQQALRRTMELYSNSTRFAFACNQSNKIIEPLQSRCAILRYSKLSDEDVLKRLLQIIKLEDVKYTNDGLEAIIFTAEGDMRQAINNLQSTVAGHGLVNADNVFKIVDSPHPLIVKKMLLASNLEDSIQILRTDLWKKGYSSIDIVTTSFRVTKNLAQVKESVRLEMIKEIGLTHMRILEGVGTYLQLASMLAKIHKLNNKA
Protein: Putative acyl carrier protein, mitochondrial (ACP) (Q10217)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of very-long-chain fatty acids.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- RNA polymerase I-specific transcription initiation factor rrn11
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Membrane-bound O-acyltransferase gup1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Large ribosomal subunit protein bL17m
- Probable mitochondrial-processing peptidase subunit beta
Sequence:
MLSRFSSQLRFISAVRPVIPKFQPLRFYSVARPDAEKRILKVVSSFDKIQDPKKVTPTSTFANDLGLDSLDAVEVVMAIEEEFSIQIPDKDADEITSVGDAISYITKNPEAK
Protein: Peptide transport system ATP-binding protein (E0SFZ9)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004417}.
Interaction partners:
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Peptide transport system ATP-binding protein
- Peptide transport periplasmic protein
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
Sequence:
MVETLLEARNLTKTFRYRTGWFRRQHVEAVKSVSFTLRERQTLAIIGENGSGKSTLAKMLTGVIPPTSGELVIDDHPLEYGDYHYRSQRIRMIFQDSANSLNPRQRIGQLLELPLRLNTDLTPQEREKAINLALRQVGLRADHATYYPHALAPGQKQRIGLARALILQPKVIVADEVLASLDMSVRSQIINLMLELQEKHGISYIYVTQHLGMMKHISDQILVMQAGEVVERGSTADVLASPLHDLTKRLITSHFGEALSADAWRRDSSPV
Protein: Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (Madh6) (SMAD family member 9) (SMAD 9) (Smad9) (O15198)
Organism: Homo sapiens (Human)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 5
- Bone morphogenetic protein receptor type-2
- Mothers against decapentaplegic homolog 3
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-1B
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 6
Sequence:
MHSTTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQPPCSALPPSPSHAFSQSPCTASYPHSPGSPSEPESPYQHSVDTPPLPYHATEASETQSGQPVDATADRHVVLSIPNGDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: Uncharacterized protein C16E9.19 (Q9C0X2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit alg14
Sequence:
MFPKIKQTSKNYNGKEIQAISMRFSNQITILVTISGKIGQMYMMTYEKSVMSPVSITGDMSTLPEIGVRTLLGGGGEDDIKSHWAQITAGQVGSLLARQQMLVRPDVRIPRVCLGLHVPWTDDNEKNGDLTVVILELVKEICF
Protein: Asparagine--oxo-acid transaminase (EC 2.6.1.14) (Asparagine:2-oxoglutarate aminotransferase) (Q8DTM1)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Catalyzes the transamination reaction between L-asparagine and 2-oxoglutarate to produce L-glutamate and 2-oxosuccinamate. Is not active with pyruvate as amine acceptor. May also use other amino acids as substrates.
Interaction partners:
- Carbon-nitrogen hydrolase
- asparaginase
- Prephenate dehydratase
Sequence:
MTKLSRRVLEMEESVTLATSARAKTLKAQGRDVLELSLGQPDFVTPKNIQEAAMKSIRDGRASFYTIASGLPELKDAISQYFEKFYGYSVERKQIVVGTGAKFILYALFAAVINPKDEVIIPTPFWVSYADQIKMNDGVPVFIRTSEENHFKATVEQLEAARTNKTKMIVLNSPSNPTGMIYSKKELEAIGNWAVKHDILILSDDIYGRLVYNGARFTPISTISQPICQQTIVINGVSKTYSMTGWRVGYAVGDPEIIGAMSKIVSQTTSNLTTAAQYAAIEALIGNQDTVEVMRQAFEERLNTIYPLLAKVPGFHVVKPEGAFYFFPNVKKAMEMKGYTDVTEFTTALLEETGVALVTGAGFGAPENVRLSYATDMVTLKEAINRIQAFMEK
Protein: Dynein, axonemal, intermediate chain 2, isoform C (M9PC80)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- Putative inner dynein arm light chain, axonemal
- Radial spoke head protein 9 homolog
- GH13165p
- Zinc finger MYND domain-containing protein 10 homolog
- Spag1 axonemal dynein assembly factor
- Dynein axonemal assembly factor 5
- Dynein axonemal light chain 1
- AT19426p
- Coiled-coil domain containing protein 151
- Dynein heavy chain at 93AB, isoform C
Sequence:
MEYIFKKERRSFGARVHFEDKDEVVFTENSNPELVKSYILKNPVDRVTQYAGQTSLSVANTERATYKSTGITHNEGGWPKDINMHDPEQTVRYKRKIEKDENYITQVMNLTKPMEHYIHQNNAVNIYENYFENLDPAPLPEPCKSRTVNVYRDPNPIKVPVKHLSWSPDGGIKMAVSHCDMRFQGDKSNQKCNSYIWEVENPNEPFLTLEPKVPCVCLEYNQKDPTSLVSGMYNGQVAAWDTRHGKLPVMISEREVCHRDPVNSVLWNNSKSGTEFFSGGSDGQVLWWDTRKLTEPLDRLLMDPVKSDDQDLSRSYGISVLEYETTIPTRFMAGTEMGMLFSCNRKGKTPTEKIQIRMMCHLGPVYAITRNPAFVKNFLTVGDWCARIWSEDCRESSIIWTKSSSSMLTDGAWSYTKVSQFFITRMDGVLDTWDLLQQQNEPVLTVKVCDEPLYCVRTNENGKFVSCGSQLGATFLVEVSDNMVMSAKNDKPLLTAMFERENRREKILEAKSRESKLKVKANHGQDQGDTMMVNGKINMAPFEAACEQAASEYFAAVEQERQRRLPGGKQDAEEADVSEAESSKL
Protein: DNA repair protein RecN (Recombination protein N) (Q9A6V0)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Protein RecA
- Transcription-repair-coupling factor
- LexA repressor
Sequence:
MLIGLSIRDVVLIESLDLAIGEGLTALTGETGAGKSIILDALGLATGARADAGLVRRGATGHASATAIFALPADHPAFAYLDDKGLSYARDEDVVLRRQLSPDGRSRAFVNDQATSVGVLKDLGALLLEVHGQHETVGLLDPKTHRGLLDTFGGVSLGAVASAWSAWRAARDRAEALRDLAGRAAAETEELTLRLSELDRLDPREGEEASLAEERALLSSAEKAMADIAAAQDALAGDNLSGRLAQAYRALERARDRALQAGAPAEGSAMTRLSAACEAVDRALVEAQEASAAIDAVAETFEFEPDRLEKAEERLFALRGMARKLNVLVDDLPAKRAEFAARLQAIETSEDSLRAAEKDAAEAREAYLYAAEALSAERRAAGDALAKAVEAELTPLKLEKARFRVAVEPLGEDRAGPSGLDRVAFEISTNPGAPFGAMEAIASGGELARFALALKAALAGRGGGPQPLMIFDEVDQGVGGAVADAVGLRLKRLAANAQVLVVTHSAQVAARGDAHWRISKSGDDTSTRTRVEPLSPAQREEEIARMLSGAEVTEAARAAARALLTLHA
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-) (Q811B3)
Organism: Mus musculus (Mouse)
Function: Metalloprotease that plays a role in the degradation of COMP (By similarity). Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Cartilage oligomeric matrix protein
- A disintegrin and metalloproteinase with thrombospondin motifs 7
Sequence:
MPCARGSWLAKLSIVAQLINFGAFCHGRQTQPWPVRFPDPRQEHFIKSLPEYHIVSPVQVDAGGHVLSYGLHHPVTSSRKKRAAGGSGDQLYYRISHEEKDLFFNLTVNWEFLSNGYVVEKRYGNLSHVKMVASSGQPCHLRGTVLQQGTTVGIGTAALSACQGLTGFFHLPHGDFFIEPVKKHPLTEEGSYPHVVYRRQSIRAPETKEPICGLKDSLDNSVKQELQREKWERKTLRSRSLSRRSISKERWVETLVVADTKTVEYHGSENVESYILTIMNMVTGLFHSPSIGNLVHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQKSINPKSDLNPVHHDVAVLITRKDICAGVNRPCETLGLSQLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGKENDCEPVGRHPYIMSQQIQYDPTPLTWSKCSKEYITRFLDRGRGFCLDDIPSKKGLKSNVIAPGVIYDVHHQCQLQYGPNATFCQEVENVCQTLWCSVKGFCRSKLDAAADGTRCGEKKWCMAGKCITVGKKPESIPGGWGRWSPWSHCSRTCGAGAQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPCRSDTPTFRQMQCSEFDTVPYKNQFYRWFPVFNAAHPCELYCRPIDEQFSERMLEAVIDGTPCFEGGNSRNVCINGICKRVGCDYEIDSNATEDRCGVCLGDGSACQTVKKLFRQKEGSGYVDIGLIPKGARDIRVMEIKAAGNFLAIRSEDPEKYYLNGGFIIQWNGNYKLAGTVFQYDRKGDLEKLIAPGPTNESVWLQLLFQVTNPGIKYEYTVRKDGLDNDVEKLLYFWQFGRWTECSVTCGTGIRRQAAHCVKKGHGIVKTTFCNPETQPSVRQKKCHEKDCPPRWWAGEWEACSTTCGPYGEKKRTVLCIQTMGSDEQALPATDCQHLLKPKALVSCNRDILCPSDWTVGNWSECSVSCGGGVRIRSVTCAKNLNEPCDKTRKPNSRALCGLQQCPFSRRVLKPNKDIAPSGKNQSTAEHDPFKPIPAPTSRPTPLSTPTVPESMSTSTPTINSLGSTIASQEDANGMGWQNNSTQAEEGSHFPTSSGSTSQVPVTSWSLSIQPDDENVSSSAIGPTSEGDFWATTTSDSGLSSSDAMTWQVTPFYSTMTTDPEVEIHSGSGEDSDQPLNKDKSNSVIWNKIGVPEHDAPMETDAELPLGPPPTSYMGEEPSWPPFSTKMEGSLPAWSFKNETPRDDGMIAEKSRKIPLPLAGDHHPATSEKLENHDKLALPNTTNPTQGFGPVLTEEDASNLIAEGFLLNASDYKHLMKDHSPAYWIVGNWSKCSTTCGLGAYWRSVECSSGVDADCTTIQRPDPAKKCHLRPCAGWRVGNWSKCSRNCSGGFKIREVQCMDSLDHHRSLRPFHCQFLAGAPPPLSMSCNLEPCGEWQVEPWSQCSRSCGGGVQERGVSCPGGLCDWTKRPATTVPCNRHLCCHWATGNWELCNTSCGGGSQKRTIHCIPSENSTTEDQDQCLCDHQVKPPEFQTCNQQACRKSADLTCLKDRLSISFCQTLKSMRKCSVPSVRAQCCLSCPQAPSIHTQRQRKQQLLQNHDML
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FXS9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Glutathione reductase
- Protein URE2
- Glutathione hydrolase
- Glutathione synthetase
- glutathione-specific gamma-glutamylcyclotransferase
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Sulfiredoxin
- Candida glabrata strain CBS138 chromosome M complete sequence
- Catalase
Sequence:
MSTFMRQYARNMARVPVSTRLNAQRFACANYRFYSEKTNYKQADQPRLRINSSAPNFDADTSHGKINLYDYLGDSWGILFSHPADFTPVCTTEMGAFAKMKPQFDKRGVKLLGLSVEDAESHRKWIKDIEEINGIDKFGFPIIADTKRHVAFLYDMCDEEGFGNINDGSLTTVRSVYVIDPAKKIRVIFTYPSQVGRNTAEVLRVIDALQTADKHGVVTPGNWSPNDDVIIPPKVSDAEASEKFGDFKTVKSYLRYTKLK
Protein: Large ribosomal subunit protein bL17m (39S ribosomal protein L17, mitochondrial) (L17mt) (MRP-L17) (LYST-interacting protein 2) (Q9NRX2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL5
- Elongation factor Tu, mitochondrial
Sequence:
MRLSVAAAISHGRVFRRMGLGPESRIHLLRNLLTGLVRHERIEAPWARVDEMRGYAEKLIDYGKLGDTNERAMRMADFWLTEKDLIPKLFQVLAPRYKDQTGGYTRMLQIPNRSLDRAKMAVIEYKGNCLPPLPLPRRDSHLTLLNQLLQGLRQDLRQSQEASNHSSHTAQTPGI
Protein: Zinc finger and BTB domain containing 1 (G3V2I8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKPSHSSYVLQQLNNQREWGFLCDCCIAIDDIYFQAHKAVLAACSSYFRMFFMNHQHSTAQLNLSNMKISAECFDLILQFMYLGKIMTAPSSFEQFKVAMNYLQLYNVPDCLEDIQDADCSSSKCSSSA
Protein: Elongation factor G (EF-G) (P13551)
Organism: Thermus thermophilus
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Protein: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (EC 6.3.5.13) (O69679)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MVTTRARLALAAGAGARWASRVTGRGAGAMIGGLVAMTLDRSILRQLGMGRRTVVVTGTNGKSTTTRMTAAALGTLGAVATNAEGANMDAGLVAALAAHRDAELAVLEVDEMHVPHISDAVDPAVVVLLNLSRDQLDRVGEINVIERTLRAGLARHPDAVVVANCDDVLMTSAAYDSPNVVWVAAGGAWSNDSVSCPRSGEVIVRKAPSQEDHWYSTGADFKRPAPHWWFDDATLYGPDGLALPMRLALPGSVNRGNAAQAVAAAVALGADPAVAVAAVCQVDEVAGRYRTVRIGAHQARILLAKNPAGWQEALAMVDKHADGVVIAVNGRVPDGEDLSWLWDVRFEHFEKTRVVAAGERGTDLAVRLGYAGVEHTLVHDTVAAIASCPPGRVEVVANYTAFLQLQRALARRG
Protein: Coatomer subunit beta'-1 (Beta'-coat protein 1) (Beta'-COP 1) (Q9CAA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta-1
- Coatomer subunit delta
- Coatomer subunit epsilon-1
- Coatomer subunit beta-2
- Coatomer subunit alpha-2
- Coatomer subunit alpha-1
- Coatomer subunit gamma
- Coatomer subunit epsilon-2
- Structural molecule
- Coatomer subunit zeta-3
Sequence:
MPLRLEIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWLCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTIKIWNLGSPDPNFTLDAHLKGVNCVDYFTGGDKPYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMVKLGREIPVASMDNSGKIIWAKHNEIHTVNIKSVGADEVTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSSDGEHAVRESSTKIKIFSKNFQEKKTVRPTFSAEHIFGGTLLTMCSSDFICFYDWAECRLIRRIDVTVKNLYWADSGDLVAIASDTSFYILKFNRDIVSSYFDGGKQIDEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSWRLNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQANEVLPSIPKEHHNSVAHFLESRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLLYSSLGDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLPSKVSEIVALWRNDLTKISPKAAESLADPEEYPNLFEEWQVALSLENRAAETRGVHPPAGDYCSHADRDHTTLVDAFRIMQIEEEGRLEQGDVLDEVGEEGEDGEEEEEEDRQEESSDGRQQNVEEEAVVVDADSTDGAVLVNGNESEEQWVLTPPQE