wanglab/gogpt-training-data huggingface dataset:
Protein: Alanine--glyoxylate aminotransferase (AGT) (EC 2.6.1.44) (Serine--pyruvate aminotransferase, mitochondrial) (SPT) (EC 2.6.1.51) (O35423)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification.
Subcellular location: [Isoform Peroxisomal]: Peroxisome {ECO:0000250|UniProtKB:P21549}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix {ECO:0000250|UniProtKB:P09139}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- 2-Hydroxyacid oxidase 1
- 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- 2-Hydroxyacid oxidase 2
- L-serine dehydratase/L-threonine deaminase
- Peroxisomal sarcosine oxidase
- Aminomethyltransferase, mitochondrial
- L-threonine aldolase
- Glycine dehydrogenase
Sequence:
MFRMLAKASVTLGSRAAGWVRTMGSYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSFYTDITYLAKLWGCEGETRVIHHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLDHFSIEISGGLGPTEERVLRIGLLGYNATTENVDRVAEALREALQHCPKNKL
Protein: Sorcin (B4DHQ6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MAYPGHPGAGGGYYPGGYGGAPGGPAFPGQTQDPLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVNSIAKRYSTNGKITFDDYIACCVKLRALTDSFRRRDTAQQGVVNFPYDDFIQCVMSV
Protein: SET domain-containing protein (Q38AF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVLPSPHWNYCESFYAPVTEGASFRIQTDSVKGKGLVAQKKIREGDVVHEETALCCSQNLDDHLSKVAVCGNCLLFLESPAQSVARVTKDEALTSALPFRESCADIRQVPCVRSESGCAMVFCSVRCREAAWSRFHRCGCRGRMSEEQKGAYDEFVTHDWNLGALNYSDTVFLGFRFVCMVVTNIRFHKQPVDVAYQPVSQLAKLPLTDFRLTYLLGPSKENGGIVAERGSESSSKSGGEEDDNSGQQWQQHWLRKLEESRCTSVHRYSAEDSHAAGVFLEKGVELLDRVLRFTDEERHFFTPTRWSELLGAMLLNGQERSRPSYYEQLKCKVKVIPDAAARMDAFEEKVRAAGFDARQLMCGSRGQGIYTIGCLLNHSCEPNLQVLYTAVGDETLSIEALRDIEPGEELNISYVDETLPYPQRQLILYEHYFFICKCPKCTREAPDWERQVNGSEK
Protein: Caerin-2.1 (P86504)
Organism: Litoria rothii (Roth's tree frog) (Hyla rothii)
Function: Inhibits the formation of NO by neuronal nitric oxide synthase.
Subcellular location: Secreted {ECO:0000269|PubMed:16124032}.
Interaction partners:
Sequence:
GLVSSIGRALGGLLADVVKSKQPA
Protein: RING finger protein 141 (Zinc finger protein 230) (Q99MB7)
Organism: Mus musculus (Mouse)
Function: May be involved in spermatogenesis.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q8WVD5}; Lipid-anchor {ECO:0000250|UniProtKB:Q8WVD5}.
Interaction partners:
Sequence:
MGQQISDQTQLVINKLPEKVAKHVTLVRESGSLTYEEFLGRVAELNDVTAKVAAGQEKHLLFEVQPGSDSSAFWKVVVRVVCTKINKSSGIVEASRIMNLYQFIQLYKDITSQAAGVLAQSSTSEEPDENPSSVTSCQASLWMGRVKQLTDEEECCICMDGRADLILPCAHSFCQKCIDKWSDRHRNCPICRLQMTGANESWVVSDAPTEDDMANYILNMADEAGQPHRP
Protein: Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase) (P50440)
Organism: Homo sapiens (Human)
Function: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis.
Subcellular location: [Isoform 1]: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Probably attached to the outer side of the inner membrane.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Guanidinoacetate N-methyltransferase
- Antizyme inhibitor 2
- Serine hydroxymethyltransferase, cytosolic
- Alanine--glyoxylate aminotransferase
- Arginase-2, mitochondrial
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Arginase-1
- Sodium- and chloride-dependent creatine transporter 1
- Serine hydroxymethyltransferase, mitochondrial
- Glycine N-methyltransferase
Sequence:
MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD
Protein: threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (Q8MRL7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLKLAPQGGRYYSQISRICQWILPKIQTQSKPPKQQQQQQPQLKEQQQHSYATLAAKMKKEKKEKPSGGGDTRKELSPLPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIENGFYYDMHLEGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSPTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADCDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQKIRDEFIANEDSF
Protein: Chaperone Ric-8B (Brain synembryn) (hSyn) (Synembryn-B) (Q9NVN3)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP. Able to potentiate G(olf)-alpha-dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:12652642}. Note=Localizes to the cell cortex. {ECO:0000269|PubMed:12652642}.
Interaction partners:
- Synapsin-1
- Guanine nucleotide-binding protein G
- Synapsin-3
- Guanine nucleotide-binding protein G
- Synapsin-2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide exchange factor MSS4
- Protein O-mannosyl-transferase TMTC1
- Guanine nucleotide-binding protein G
Sequence:
MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPTTCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKCLCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRSQLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVDSWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPLTHEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYREGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGVKQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKNAKPKEELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD
Protein: B melanoma antigen 1 (B melanoma antigen) (Antigen MZ2-BA) (Cancer/testis antigen 2.1) (CT2.1) (Q13072)
Organism: Homo sapiens (Human)
Function: Unknown. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAARAVFLALSAQLLQARLMKEESPVVSWRLEPEDGTALCFIF
Protein: Sirt4 protein (B2RZ30)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRGLIFRPTRGRWITQMSQLRSHGSTGLFVPPSPPLDHEKIKELQRFISLSKKLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHIDFIRSAPVRQRYWARNFVGWPQFSSHQPNPAHWALSNWEKLGKLHWLVTQNVDALHSKAGNQRLTELHGCMHRVLCLSCGEQTARRVLQDRFQALNPSWSAEAQGVAPDGDVFLTEEQVRSFRVPCCDRCGGPLKPDVVFFGDTVNPDKVDFVHQRVKEADSLLVVGSSLQVHPHRPGEEAPNRHSEHRTHEV
Protein: Transcription factor TCP1 (Q9FYG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in petal morphogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor TCP11
- Transcription factor TCP22
Sequence:
MSSSTNDYNDGNNNGVYPLSLYLSSLSGHQDIIHNPYNHQLKASPGHMVSAVPESLIDYMAFKSNNVVNQQGFEFPEVSKEIKKVVKKDRHSKIQTAQGIRDRRVRLSIGIARQFFDLQDMLGFDKASKTLDWLLKKSRKAIKEVVQAKNLNNDDEDFGNIGGDVEQEEEKEEDDNGDKSFVYGLSPGYGEEEVVCEATKAGIRKKKSELRNISSKGLGAKARGKAKERTKEMMAYDNPETASDITQSEIMDPFKRSIVFNEGEDMTHLFYKEPIEEFDNQESILTNMTLPTKMGQSYNQNNGILMLVDQSSSSNYNTFLPQNLDYSYDQNPFHDQTLYVVTDKNFPKGKVWIQDSFVN
Protein: Wings apart-like protein 2 (AtWAPL2) (Q9C951)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of CTF7. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). Essential for the prophase removal of cohesin during meiosis thus determining the timely release of meiotic cohesion. Important for proper spindle attachment and assembly during meiosis. Helps to prevent abnormal centromere association during prophase I in meiocytes. Required for early embryonic patterning. Also involved in chromosome segregation during mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7Z5K2}. Chromosome {ECO:0000250|UniProtKB:Q7Z5K2}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion 1 protein 4
- Sister chromatid cohesion protein SCC2
- Sister chromatid cohesion protein SCC4
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Sister chromatid cohesion 1 protein 1
- Sister chromatid cohesion 1 protein 3
- Tudor/PWWP/MBT superfamily protein.
- Binding protein.
- Sister chromatid cohesion 1 protein 2
Sequence:
MMERTYGRRKPGMLNDDVSRAEHIFPSSSSPELEPVDFSTQESSCVWNYSSRSTFSDNDFSEKRNKRPRNGGGGFGSNSTLMEAQEFGELIENEDEVNFALDGLKKGHKVRIRRAALSSLLSICESQYQRRSLRALGISQSIIDAILGLCLDDIPSNLAAATLFFVLTTDGQDDHFMESPNSIKFLVKLLRPVVSASTKVKPRNIGSRLLSIIKDVDAARDAASMHDLSSCDIIDRAQEILVNCKELRLIDSYKIERMRPELSTKWVALLVMEKACLSKISFDDTSGTVKKSGGMFKEKLRELGGLDAVFDVVMDCHTVMESWVTHDTLSVEDIKDDLNKQSLMLLLKCLKIMENATFLSTENQIHLLRLNKSMGSHESRLSFTELMISVIKILSGLQLRAHRNEKHPHPQPHLASAVKKGFVTIISSDTCSTTGFSSIKSLSVSKRNQSAFLVGCSTTPKPGSQSSVMSTIDHCTLTTTAGSNTGSFAGRLASLGSGISRSKTRTSQTRESSCKKVENFASFEDSQDPFSFDLEDSGPSRWAVGKQKKSKGQKRKGSYRDKKDERSLQLFSSQEESNHGLNSQEESSDRDHHVTEQPSLTYDIDKGCLCLLSDCLLTAVKVLMNLTNGNSVGCREVAACGGLESMAELVVGHFPSFTRSPLYSQMESGTCHQKDKHLTDQELDFLVAILGLLVNLVEKNGINRSRLAAASVPITNPEGLQDSEQDMIPLLCSIFLTNKGSADTKDETSTFTLDDEEAVLESEKEAEKMIVEAYSALLLAFLSTESRSIRNAIRDYLPKRDMAILVPVLDRFVAFHTTLDMIPPETHKVVMEVIESCKLP
Protein: 3',5'-cyclic-AMP phosphodiesterase, isoforms N/G (EC 3.1.4.53) (Learning/memory process protein) (Protein dunce) (cAMP-specific phosphodiesterase, isoforms N/G) (Q9W4S9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Vital for female fertility. Required for learning/memory (By similarity).
Interaction partners:
Sequence:
MIATLFIIFAFIRAFPWSRKRGRPALALTLMPEGGEDHRGDLNQKGENNNRPRPSISLANNGEAMAPRTRRKSSKFHEVTFSGSVGGGDSDGGGEAINGGNLDVSPSKRHSLSTTTSNSSSAPYRYLSGSSRSRGSRGDCHEYYQLQQHSSSLSNGNRGNRGLSQRSDTMATEAEGEEFDVDPMDEDDEDQTYDRETEEFYSNIQDAAGTGSSSRSKRSSLFSRSDSSATTTSSSGGGTFTGGKRRSAASILSSSMCSDLMTSDRRSSTATEYSVKSVTTGNTSQRRSSGRIRRYVSRMTIAGARRRTTGSFDVENGQGARSPLEGGSPSAGLVLQNLPQRRESFLYRSDSDFEMSPKSMSRNSSIASESHGEDLIVTPFAQILASLRSVRNNLLSLTNVPASNKSRRPNQSSSASRSGNPPGAPLSQGEEAYTRLATDTIEELDWCLDQLETIQTHRSVSDMASLKFKRMLNKELSHFSESSRSGNQISEYICSTFLDKQQEFDLPSLRVEDNPELVAANAAAGQQSAGQYARSRSPRGPPMSQISGVKRPLSHTNSFTGERLPTFGVETPRENELGTLLGELDTWGIQIFSIGEFSVNRPLTCVAYTIFQSRELLTSLMIPPKTFLNFMSTLEDHYVKDNPFHNSLHAADVTQSTNVLLNTPALEGVFTPLEVGGALFAACIHDVDHPGLTNQFLVNSSSELALMYNDESVLENHHLAVAFKLLQNQGCDIFCNMQKKQRQTLRKMVIDIVLSTDMSKHMSLLADLKTMVETKKVAGSGVLLLDNYTDRIQVLENLVHCADLSNPTKPLPLYKRWVALLMEEFFLQGDKERESGMDISPMCDRHNATIEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEENRDYYQSMIPPSPPPSGVDENPQEDRIRFQVTLEESDQENLAELEEGDESGGESTTTGTTGTTAASALSGAGGGGGGGGGMAPRTGGCQNQPQHGGM
Protein: Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (Nei homolog 1) (NEH1) (Nei-like protein 1) (Q8K4Q6)
Organism: Mus musculus (Mouse)
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Chromosome. Note=During mitosis, associates with centrosomes and condensed chromatin. {ECO:0000250}.
Interaction partners:
- DNA polymerase beta
- DNA repair protein XRCC1
- N-glycosylase/DNA lyase
- Endonuclease 8-like 2 lyase Neil2)
- Endonuclease 8-like 3
- Endonuclease III-like protein 1 lyase)
- Flap endonuclease 1
- Transcription factor Maf
- Bifunctional polynucleotide phosphatase/kinase
- DNA ligase 3
Sequence:
MPEGPELHLASHFVNETCKGLVFGGCVEKSSVSRNPEVPFESSAYHISALARGKELRLTLSPLPGSQPPQKPLSLVFRFGMSGSFQLVPAEALPRHAHLRFYTAPPAPRLALCFVDIRRFGHWDPGGEWQPGRGPCVLLEYERFRENVLRNLSDKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTVLEALQQCRPSPELTLSQKIKAKLQNPDLLELCHLVPKEVVQLGGKGYGPERGEEDFAAFRAWLRCYGVPGMSSLRDRHGRTIWFQGDPGPLAPKGGRSQKKKSQETQLGAEDRKEDLPLSSKSVSRMRRARKHPPKRIAQQSEGAGLQQNQETPTAPEKGKRRGQRASTGHRRRPKTIPDTRPREAGESSAS
Protein: Ubiquitin-conjugating enzyme E2 variant 2 (cDNA, FLJ93989, Homo sapiens ubiquitin-conjugating enzyme E2 variant 2 (UBE2V2),mRNA) (A0M8W4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN
Protein: Bifunctional pinoresinol-lariciresinol reductase (PLR-Lp1) ((+)-pinoresinol reductase) (EC 1.23.1.1) ((-)-lariciresinol reductase) (EC 1.23.1.4) (A3R052)
Organism: Linum perenne (Perennial flax)
Function: Reductase involved in the lignan justicidin B biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Low activity with the other enantiomers. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
Interaction partners:
Sequence:
MKPCSVLVVGGTGYIGKRIVSASLYLGHDTYVLKRPGTGLDIEKLQLLLSFKKRGAHLVEASFSDHDSLVRAVRLVDVVICTMSGVHFRSHNILLQLKLVEAIKEAGNVKRFIPSEFGMDPARMGQAMEPGRETFDQKMVVRKAIEEANIPHTYISANCFAGYFVGNLSQLGTLTPPSDKVIIYGDGNVKVVYVDEDDVAKYTIKAIEDDRTVNKTVYLRPPENMMSQRELVAVWEKLSGNQLEKIELPPQDFLALMEGTTVAEQAGIGHFYHIFYEGCLTNFEINAENGEEEASRLYPEVEYTRVHDYLKIYL
Protein: nitrite reductase (cytochrome; ammonia-forming) (EC 1.7.2.2) (Q0P8Q2)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
- Cytochrome c-type protein
- Cytochrome C-type haem-binding periplasmic protein
- Periplasmic nitrate reductase
- Cytochrome c oxidase subunit III
- Periplasmic nitrate reductase, electron transfer subunit
- Ferredoxin
Sequence:
MKKNILRLGIVVLVLLIAGVLWLNNDINQKKEDEANKNAIAANADFSLLSDDDPNFEKWGKVFPEQLKMYLTVEKEEPKATEFGGNLAYSKLIRFPQLTILWAGYPFSLDFNEERGHFWVQVDQMKTARNNKDFLNAHGLAAFKGQPAACMNCHSGWTPWLIKNVAKGDFTAFNSTNYWTMIKNIPAVDGIVENSPEHAGPHGGKRMGVTCADCHNPNDMSLRLTRPAAINALVSRGYEKDPVQGVKATREEMRTLVCSQCHVEYYFKPTGEKVKVMGETIVDDSSKKWWNGTQKNYDEYEFWRDGNKVKEIETDGIVLTFPWSEWKKGQPFRIEMLDDYYDKVRGVFGADFTHKLTGAQIIKIQHPESELYSGGVHAANGVSCVDCHMPYVREGAKKVTQHNITSPLRDINSACKSCHKQSEDYLKAQVLDIQNSVAHDQRTAEYAIVSLIMDTKKLRDELGNMEKFQSDGKADAKKISEELKEVLELHRKAQMRADFVNAENSTGFHNPREASRMLLQAVDMARMGQTKLVEIAAANGIKDFKTSNLGFEDIQKFNPGELYYKVDVNNHKAGERYYADEKDVNGNPPKELLEHDKELAPYNYQVIDKK
Protein: Transcription initiation factor TFIID subunit 5 (Q9VT91)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- IP01149p
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 11
Sequence:
MDLPLPILIPSSDEVYVISDSDDSDSDDIRNELMKLEDNKDKPKNKERQKSKNENSQIKMNKWYLKEFEDLMGLEIACSDDEDDIDDRNSEIWSSSESDKISDSDDSNSDGSPTEWINRIKNVNLFPFNKSAEDEKPKACEELPSIPVFTGPMPSMPIYDEETCQFEMVPPIIQPDLIKEVTDAEMPIELDKSDSELEKEKLKADEDDNFSDSNTSSSFSLSSLDDYDYGETDLDEQHNENKCTYWEEMSLRPVDKGEVSQEELMAILNEDESSPDHRSECDIDEAIRTRDGSDFYEDSAQFLENMENVSLLVIKEDSVFADYEFAVKKLIKLIQSTPSHYKYEIYILLYPLLVLTYLQMMASDKIQKARMLLVRFQDHLDDSYISRIIKLREISKPAEVPNKARKLLAGLEKVKIEMSEGAFRQLLLCTEEWTRGQQEKLLSHFQIQPYSEDDKPQQRFAIGQPLLEPIWYGAPEPLHKKDFAARPFFQKRRKKRSEPQLSDNLHLPPVNRVYNPIPNKMDLLHMKSDEQYRMKLDRNNLPSTYLYTTSPSDEVVICATFSEGNSMLALGTVSSKVYVFSLKPSKLVQVKAAQWLKNLDTGMAGVDKDMIDPIKKFTRRTLYGHQGPVYGCSFNPEDRFLITCSEDFSVRLWCLLSWSCVVIFSGHLAPVCFVVFAPRGYYFATASDDCTARVWMQDNTKPARILQGHLAELGVCLFHPNRHYMATGSADCTVRIWDIVKAVQVRIFRGHKSRITALIYSICGRYLVSGGDDNLIMIWDTANEILMQFFDHHKASINTMEISLDNNILVVGGQDCQLTLWDFEQVIKNYLNRAKISMKNQAGTQESSANNLLVSSFFTKGEPFYMIRFTRRNLLLGFCVTPREFENDVLDVKLNQNKHKEEKKKELGEWLDFLDTIKLKACYDLKDEINLDTSQVEKENKS
Protein: Protein Tat (Transactivating regulatory protein) (P04611)
Organism: Human immunodeficiency virus type 1 group M subtype D (isolate ELI) (HIV-1)
Function: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
Interaction partners:
Sequence:
MDPVDPNLEPWNHPGSQPRTPCNKCHCKKCCYHCPVCFLNKGLGISYGRKKRRQRRGPPQGGQAHQVPIPKQPSSQPRGDPTGPKEQKKKVESEAETDP
Protein: Sporulation-specific protein 77 (Q06134)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for spore wall assembly and ascus formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15590821}. Note=Diffuse location throughout the cell at all stages of sporulation.
Interaction partners:
- Spore membrane assembly protein 2
- Protein DCV1
- Uncharacterized protein YFR012W-A
- Uncharacterized protein YGR146C-A
- Putative N-terminal acetyltransferase 2
Sequence:
MFRRGDNSNFNVQNSFFLPLEYEYTVKDNVPSKKKSSIGFFPLDDSLFTSKNNSGHHKSEQLHRGNAETIRSQFGTDAVPIRIDEKEGKWDRIQDDNSSNLNYQINNSNDPASSGKYTQSIDCNHIAESKFSKKNGNIDSLRSNSATFMLNTADEDVIEFSFDDNVPYAELLSGATLEKCSLTLNEINKKLFNTLYDFRVSKDNPEENLVELILPNCVVLLNFFEDIELLADSSDEAFEKSTFINTIEFIVHDIWVETLIKNINLLQMFDADLKCYNDKYIICKLKGQYPSTNIVDIMCRLKHFSNSILETFKFGIELKEQDQCHNRNTIINYVLFSRVFSTIVLEIQKCFILIVKFMYSVNFLEKFSDEVFLSFIEILIKIVFEHQIPQLFLGIDEIIQLWLKNNEGKRQQLLSAWCNGTVQDMKQSQQRESSNAESESITSSTEEDEEGLQFNKWDVIEPFIDNIKALNQSKSHM
Protein: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha) (Q42777)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- methylcrotonoyl-CoA carboxylase
- methylcrotonoyl-CoA carboxylase
- Ribulose bisphosphate carboxylase large chain
- Ribulose bisphosphate carboxylase large subunit C-terminal domain-containing protein
- Uncharacterized protein
- hydroxymethylglutaryl-CoA lyase
- hydroxymethylglutaryl-CoA lyase
- hydroxymethylglutaryl-CoA lyase
- hydroxymethylglutaryl-CoA lyase
Sequence:
MASLALLRRTTLSHSHVRARAFSEGKSSNRHRIEKILVANRGEIACRITRTARRLGIQTVAVYSDADRDSLHVATADEAIRIGPPPARLSYLNGASIVDAAIRSGAQAIHPGYGFLSESADFAKLCEESGLTFIGPPASAIRDMGDKSASKRIMGAAGVPLVPGYHGYDQDIEKMKLEADRIGYPVLIKPTHGGGGKGMRIVHTPDEFVESFLAAQREAAASFGVNTILLEKYITRPRHIEVQIFGDKHGNVLHLYERDCSVQRRHQKIIEEAPAPNISADFRAQLGVAAVSAAKAVNYYNAGTVEFIVDTVSDEFYFMEMNTRLQVEHPVTEMIVGQDLVEWQILVANGEALPLSQSQVPLSGHAFEARIYAENVQKGFLPATGVLHHYHVPVSSAVRVETGVKEGDKVSMHYDPMIAKLVVWGENRAAALVKLKDSLSKFQVAGLPTNVNFLQKLANHRAFAIGNVETHFIDNYKEDLFVDANNSVSVKEAYEAARLNASLVAACLIEKEHFILARNPPGGSSLLPIWYSSPPFRIHHQAKRRMELEWDNEYGSGSSKIMKLTITYQPDGRYLIETEQNGSPVLEVKSTYVKDNYFRVEAAGVINDVNVAVYSKDQIRHIHIWQGSCHHYFREKLGLELSEDEESQHKPKVETSANPQGTVVAPMAGLVVKVLVENKTRVEEGQPVLVLEAMKMEHVVKAPSSGYVHGLQLMVGEQVSDGSVLFSVKDQ
Protein: CarD protein (Q50887)
Organism: Myxococcus xanthus
Interaction partners:
Sequence:
MPEGSASLQLAVGDRVVYPNQGVCRVSAIDVKEVAGQKLTFVTMRREEDGAVVMVPEGKVLAIGVRKVASAEDVEAIFTFLRSDSDKADLDWKQRARTNLDRMTQGGIMGLAEVVKGLQVLSELRPLPTKERELYDNARHLLVTEVAAALGTAEVNAEDAIDIVLFPPGRERPKRTAAEFQREEGDLDLDSDLLGLDSDLDLPSDEEPSEPSEEESSEEGESEEAASSEESAPKKRGRPPKAKTEAPEGAEPPAPKKRGRPPKPKPEATAEGAEPPAPKKRGRPPKPKPPEVEGAAPAAPKKRGRPPKVKPPEGES