wanglab/gogpt-training-data huggingface dataset:
Protein: Ran-specific GTPase-activating protein 1 (Ran-binding protein 1) (RANBP1) (Spi1-binding protein) (Q09717)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stimulates the GTPase activity in the presence of RNA1. May potentiate the action of RanGAP1 (RNA1), thus playing the role of a negative regulator.
Subcellular location: Cytoplasm. Note=Mainly cytoplasmic.
Interaction partners:
- GTP-binding nuclear protein spi1
- Ran GTPase-activating protein 1
- Exportin-1
- Importin subunit alpha-2
- Nuclear transport factor 2
- Nucleoporin nup189
- Nucleoporin nsp1
- Probable nucleoporin C890.06
- Nucleoporin nup44
- Peptidyl-prolyl cis-trans isomerase
Sequence:
MSAEQEKKTQGTTKEEQKSSFASEDVASKQTEEAKAVFGDGVAKQENKSGASTNDEKKPAEGDEDAEPASPEVHFEPIVKLSAVETKTNEEEETVEFKMRAKLFRFDKAASEWKERGTGDARLLKHKETGKTRLVMRRDKTLKVCANHLLMPEMKLTPNVGSDRSWVWTVAADVSEGEPTAETFAIRFANSENANLFKENFEKYQEENAKILKKN
Protein: Uncharacterized protein CXorf51B (P0DPH9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKVTSEPQKPNEDVDEQTPSTSSTKGRKKGKTPRQRRSRSGVKGLKTTRKAKRPLRGSSSQKAGETNTPAGKPKKARGPILRGRYHRLKEKMKKEEADKEQSETSVL
Protein: Reactive Intermediate Deaminase A, chloroplastic (EC 3.5.99.10) (2-iminobutanoate/2-iminopropanoate deaminase) (Q94JQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes the Ser-derived enamine/imine product of Thr dehydratase, protecting the plastidial branched-chain aminotransferase BCAT3 (AC Q9M401) from inactivation. Involved in Ile biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25070638}.
Interaction partners:
- Uncharacterized protein At2g23090
- At1g21440
- Ribosomal RNA-processing protein 42
- Transcription regulator
- Threonine dehydratase biosynthetic, chloroplastic
- Serine racemase
- ceramide glucosyltransferase
- Proteasome subunit alpha type-2-B
- Transcription regulator NOT2/NOT3/NOT5 family protein
- Thiol protease aleurain-like
Sequence:
MTWSVFRSINTPTLDLSTALRSTRTPLVAAGVGCATFAGVSLFRMSSRSPPFASLSVSASSVKKEVVSTEKAPAALGPYSQAIKANNLVFLSGVLGLIPETGKFVSESVEDQTEQVLKNMGEILKASGADYSSVVKTTIMLADLADFKTVNEIYAKYFPAPSPARSTYQVAALPLNAKIEIECIATL
Protein: Kinase (EC 2.7.-.-) (Q9VL83)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Kinase
- inositol-polyphosphate 5-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- AT10229p
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- LD06095p
- Uncharacterized protein, isoform C
- Multiple inositol polyphosphate phosphatase 1
Sequence:
MTMTSTVLQRPIQAKPEKKASSKSTSSSRSRSTMAWSNEKLRFSCIDNIGLKQLWKLIALDTSASSKQRSAMMLEVEQQQQQQQQQQSNNNNERIPNENCDYLSLQRSGQAPKNHIQAQDPAQMSLLKFLAINALELSAPATPHLLQHQQAHKQAKPQGWMQLSGHPESIVPTSTGIVRKRISGLEDSEVHAYRLICKEPQTAQIVPAYFGIQEMQSQHFIELQDLLAGFRDPCVMDIKMGSRTFLESEVSNATLRPDLYQKMIAVDAGAPTPAEHEARAITKLRYMTFRESLSSSHSKGFRIEALRLRGRPPVKDLKTCRSSEQIAQTIEQFLAARRSVQKELLKRLKHMRLVIEQSTFFASHEIIGSSIFIVYDDDRVGVWLIDFAKCRELPPHVRVDHRSAWAPGNREEGLLRGMDELIRSFEEVYARCGSHRSCLKI
Protein: Laccase-5 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 5) (Diphenol oxidase 5) (Urishiol oxidase 5) (Q9SIY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lignin degradation and detoxification of lignin-derived products.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Phenylalanine ammonia-lyase 1
- Phenylalanine ammonia-lyase 4
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 3
- Trans-cinnamate 4-monooxygenase
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Basic blue protein
Sequence:
MDVTKSLLCFISFVAFLLFSSVAEANKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVLRESIRTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNAPFGNTTTTAILQYKSAPCCGVGGGSGTKKGNSFKPIMPILPAYNDTNTVTRFSQSFRSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQGPNGTRFTASMNNVSFALPSNYSLLQAHHHGIPGVFTTDFPAKPPVKFDYTGNNISRSLYQPDRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGNGVLQTIEQPPHDLPVC
Protein: IQCJ-SCHIP1 readthrough transcript protein (B3KU38)
Organism: Homo sapiens (Human)
Function: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments. May also play a role in axon outgrowth and guidance (By similarity).
Subcellular location: Cell projection, axon {ECO:0000250|UniProtKB:A0A088MLT8}. Cytoplasm {ECO:0000269|PubMed:17045569}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000250|UniProtKB:A0A088MLT8}.
Interaction partners:
- Merlin
- Serine/threonine-protein kinase TAO2
- Serine/threonine-protein kinase TAO1
- Neurogranin
Sequence:
MRLEELKRLQNPLEQVNDGKYSFENHQLAMDAENNIEKYPLNLQPLESKVKIIQRAWREYLQRQEPLGKRSPSPPSVSSEKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK
Protein: Small ribosomal subunit protein mS23 (28S ribosomal protein S23, mitochondrial) (MRP-S23) (S23mt) (Q9Y3D9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein mS35
Sequence:
MAGSRLETVGSIFSRTRDLVRAGVLKEKPLWFDVYDAFPPLREPVFQRPRVRYGKAKAPIQDIWYHEDRIRAKFYSVYGSGQRAFDLFNPNFKSTCQRFVEKYTELQKLGETDEEKLFVETGKALLAEGVILRRVGEARTQHGGSHVSRKSEHLSVRPQTALEENETQKEVPQDQHLEAPADQSKGLLPP
Protein: Zinc finger and BTB domain containing 49 (D6RJ00)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPVATHSCHLLQQLHEQRIQGLLCDCMLVVKGVCFKAHKNVLAAFSQYFRSLFQNSSSQKNDVFHLDVKNVSGIGQILDFMYTSHLDLNQDNIQVMLDTAQCLQVQNVLSLCHTFLKSATVVQPPGMPCNSTLSLQSTLTPDATC
Protein: Succinyl-diaminopimelate desuccinylase (SDAP desuccinylase) (EC 3.5.1.18) (N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase) (P0AED7)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Interaction partners:
- Diaminopimelate epimerase
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Protein YffB
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- 4-hydroxy-tetrahydrodipicolinate synthase
- 6-phospho-beta-glucosidase BglA
- Diaminopimelate decarboxylase
- 4-hydroxy-tetrahydrodipicolinate reductase
- UPF0370 protein YpfN
Sequence:
MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA
Protein: Putative lipopolysaccharide heptosyltransferase 4 (EC 2.4.1.-) (ADP-heptose:LPS heptosyltransferase 4) (HepIV transferase) (P27242)
Organism: Escherichia coli (strain K12)
Function: Adds the terminal N-acetyl-D-glucosamine group on the glucose(II) group of LPS.
Interaction partners:
- Lipopolysaccharide 1,2-glucosyltransferase
- Lipopolysaccharide 1,6-galactosyltransferase
- Probable 3-deoxy-manno-octulosonic acid transferase
- Lipopolysaccharide core biosynthesis protein WaaS
- Lipopolysaccharide glucosyltransferase WaaO
- O-antigen ligase
- Lipopolysaccharide core heptose
- Lipopolysaccharide core heptose
- Lipopolysaccharide heptosyltransferase 3
- Lipopolysaccharide glucosyltransferase WaaG
Sequence:
MRLGTFHKKKRFYINKIKINFLSFLFRNKINNQITDPAQVKSCLIIHDNNKLGDLIVLSSIYRELYSKGVKITLLTNRKGGEFLSNNKNIFEFCIKESTGFLEMLTLCKHLRDLQFDIVLDPFETMPSFKHSLILSSLKDSYILGFDHWYKRYYSFYHPHDECLKEHMSTRAIEILKHIYGEGKFSTNYDLHLPVDVEDKIKEFIGDTRIVIINPLGAKKICRLTFEQIKVIYQEVKTHFENYRIIFTGLPQDLLTIPILEIETLPFDEFIYTVALTKYSDFVISVDTALVHIAAAYHKPTLAFYPNSRTPEYPSHLIWSPNHHKSIQIVSPTYTVKDIDTETLTNSVKRLSCIDKK
Protein: Cysteine and glycine-rich protein 1 (Cysteine-rich protein 1) (Q6NZV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Dihydropyrimidinase-like 5a.
Sequence:
MPLGGGNKCGCCQKTVYFAEEVQCEGRSFHRSCFLCMVCRKNLDSTTVAVHENEIYCKACYGKKYGPKGYGYGAGAGTLSMDKGESLGIKVVEPQNHQPTNNPNTSKFAQKFGGSDVCPRCSKAVYAAEKVIGAGNAWHRGCFRCAMCGKGLESTTLADKDGEIYCKGCYAKNFGPKGFGYGQGAGALSHTQ
Protein: Cytochrome P450 144 (EC 1.14.-.-) (P9WPL1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Polyketide synthase Pks13
- Sterol 14alpha-demethylase
- Possible transcriptional regulatory protein
- Putative cytochrome P450 136
- Possible oxygenase
- Putative cytochrome P450 132
- Peptide synthetase MbtE
- NADPH oxidoreductase
- Putative cytochrome P450 138
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MRRSPKGSPGAVLDLQRRVDQAVSADHAELMTIAKDANTFFGAESVQDPYPLYERMRAAGSVHRIANSDFYAVCGWDAVNEAIGRPEDFSSNLTATMTYTAEGTAKPFEMDPLGGPTHVLATADDPAHAVHRKLVLRHLAAKRIRVMEQFTVQAADRLWVDGMQDGCIEWMGAMANRLPMMVVAELIGLPDPDIAQLVKWGYAATQLLEGLVENDQLVAAGVALMELSGYIFEQFDRAAADPRDNLLGELATACASGELDTLTAQVMMVTLFAAGGESTAALLGSAVWILATRPDIQQQVRANPELLGAFIEETLRYEPPFRGHYRHVRNATTLDGTELPADSHLLLLWGAANRDPAQFEAPGEFRLDRAGGKGHISFGKGAHFCVGAALARLEARIVLRLLLDRTSVIEAADVGGWLPSILVRRIERLELAVQ
Protein: CifR (Q9HZR6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Morphinone reductase
- CFTR inhibitory factor, Cif
- Probable epoxide hydrolase
- Probable epoxide hydrolase
- Probable epoxide hydrolase
- AB hydrolase-1 domain-containing protein
- Cytochrome c domain-containing protein
- RidA family protein
- Extradiol ring-cleavage dioxygenase class III enzyme subunit B domain-containing protein
- Probable oxidoreductase
Sequence:
MATRGRPRAFDRDTALQRAMDVFWVRGYEGASLAALTEAMEIRPPSLYAAFGSKEGLFREALAHYLGQHGRYRRDVLDGAPSAREGVAELLRETVARFCSDEFPRGCLVVLAALTGTPESEAVRDALSAERGESIRLFRERMRRGIADGDLAADTDVEELATFYATVLFGLSVQAKDRVPCERLLAVVERALRAWP
Protein: J domain-containing protein APJ1 (P53940)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Heat shock protein SSA4
- Heat shock protein SSA1
- Auxilin-like clathrin uncoating factor SWA2
- Heat shock protein SSA2
- Heat shock protein SSA3
- J protein JJJ2
- Heat shock protein 104
- Protein SIS1
- Pre-mRNA-splicing factor CWC23
- Diphthamide biosynthesis protein 4
Sequence:
MQQNTSLYDSLNVTAAASTSEIKKAYRNAALKYHPDKNNHTEESKRKFQEICQAYEILKDNRLRALYDQYGTTDEVLIQEQQAQAQRQQAGPFSSSSNFDTEAMSFPDLSPGDLFAQFFNSSATPSSNGSKSSFNFSFNNSSTPSFSFVNGSGVNNLYSSSAKYNSNDEDHHLDRGPDIKHNLKCTLKELYMGKTAKLGLNRTRICSVCDGHGGLKKCTCKTCKGQGIQTQTRRMGPLVQSWSQTCADCGGAGVFVKNKDICQQCQGLGFIKERKILQVTVQPGSCHNQLIVLTGEGDEVISTKGGGHEKVIPGDVVITILRLKDPNFQVINYSNLICKKCKIDFMTSLCGGVVYIEGHPSGKLIKLDIIPGEILKPGCFKTVEDMGMPKFINGVRSGFGHLYVKFDVTYPERLEPENAKKIQNILANDKYIKAERSTMETADSDCYCDLEKSYDSVEEHVLSSFEAPNLNNEVIEDDDLGDLINERDSRKRNNRRFDESNINNNNETKRNKYSSPVSGFYDHDINGY
Protein: Protein patched homolog 1 (Q09614)
Organism: Caenorhabditis elegans
Function: Required but not essential for cytokinesis of mitotically proliferating germ cells.
Subcellular location: Membrane {ECO:0000269|PubMed:10921907}; Multi-pass membrane protein {ECO:0000269|PubMed:10921907}. Note=Highly concentrated in a punctate pattern at the apices and internal membranes adjacent to the rachis. Expression is more intense in the distal proliferative region and in oocytes of the gonad arm.
Interaction partners:
- Protein patched homolog 3
- Frizzled-4
- BBSome complex member BBS1
- Warthog protein 5
Sequence:
MLTLLEPPGAKRSPTVGNYNNRSAQHLLNLAPEEDDLYETYEETEDYAENEPTGNILTRSFQFLDQYLVGQSSSADYNDRWKREFRARPSWCDADLCLQQMNRGKATGNRYALYSRSLIQKLLFALGNTVHRNAWSIILAVSMIFAVCCYGLQYVHIETDIVKLWVAQGGRLDEELNFLPNIKEAMRNVTGDSGPELPRENGLGGGYQVLIQTPEYEGQDALAAGPLLKHVEIMKHIASFNVSVHGVDWSLSDICFKPAPPSVAADSAASSLGDVIDKIVPCIWITPIDCFWEGSKALGPHPSLPKSSLGPLGMLLSSLSDGDMIRWSDFDPIAVIDEIHRSFNLGSHYTFFERAGVSHGYMDRPCIDPLDPECPPMAKNYFDVCPHIDRVREIAKKYGTELEEEKKKDSGYSFFDFLGRKKREAGDQPKMIHPAQPADSIPTIEDAVPAQVPVSTAPIPTTTTLSPEEARAAEEKEKKQKARELKDYCKSYRKSAFEWLKKNKDKWPEVMSENMYPQNVDYAAEMTGGCSGFASNVLNWPEDMILGNPRRAKKGGKLSGADALQSVFLVASPADVFLRFKQKPGRNSMKTGLDMDAWNETAAEQVLQAWQRNFTKSLYNHKANVDEDGNERRTLHPLASTSIADMLEEFCQFNYTIILAGYALMLAYAIVTQARFDNCLPATESSMGLALAGVLVVTFASVAGLGLATWFGIEFNAATTQIVPFLTLGIGVDNMFMLLHNYRDVVKLAGGHAEMAILMRETGMSILCTSINNILSFLTGTLLPIPALRSFCAQSSILLTFNFIAILTIYPAIISIDLRRKKAQRRDLVCCLYGDTREESYSMISKPKIQSKRIIGAPSEASIMQQFDGITQAQMASSDDPAPWSLHSFIRYYYIPFISKPASKVAIIVGCCALLGASFIGMRQSTLGLELGDVLPEHTAPAQFLRARDKYFSFYPMFAVIKGPNIDYAHQQRQIDNYRQSIGSSKYVIKNKNEEPSEKYWLGLMRDWLISIQRGFDEEVAKGSFNLTSGTVIGSNVSEDARLAHALMCSHGSLFGCAGRVGKIRLVDASGIINSDGFYNYLTAWFNVDHMMYYVSQASFFPTPPKWELSKNHTENFIPAAEPLAYSQIPFYLTGLTDTAVIVDAIKDIRSVCERFTDQGLPNFPQGIAFTFWEQYLFLTGNLMQAISIITISVFCVISVLLFNPWAALMVVCILGIMTCELAGFMGLVGIKLNPVSAVTLITAVGIGVEFTVHVVVSFLTALGTRSQRTSSAVDRVFVPVIHGSFSTLLGILMLGFSEFEFVVKYFFIVMTALICIGIINGLILLPVLLSWFGPRREISPTGGKTTLTLPPPLPKNANSSRSGGDDSDEDDEPSGLVMYSRQAPPTTRTSGGNRGTVGNNTRRLPAV
Protein: RsbT antagonist protein RsbS (Stressosome protein RsbS) (P42410)
Organism: Bacillus subtilis (strain 168)
Function: Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.
Interaction partners:
- RsbT co-antagonist protein RsbRA
- Phosphoserine phosphatase RsbX
- Phosphoserine phosphatase RsbU
- Serine/threonine-protein kinase RsbT
- Serine-protein kinase RsbW
- Anti-sigma-B factor antagonist
- RsbT co-antagonist protein RsbRB
- Blue-light photoreceptor
- RsbT co-antagonist protein RsbRC
- Phosphoserine phosphatase RsbP
Sequence:
MRHPKIPILKLYNCLLVSIQWELDDQTALTFQEDLLNKIYETGANGVVIDLTSVDMIDSFIAKVLGDVITMSKLMGAKVVLTGIQPAVAVTLIELGIALEEIETALDLEQGLETLKRELGE
Protein: OmpA-like porin (Q7CUN4)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
- Type VI secretion system contractile sheath large subunit
- Type VI secretion system contractile sheath large subunit
- Nitrogen fixation protein
- Serine/threonine phosphoprotein phosphatase
- Type VI secretion system contractile sheath small subunit
- IcmF family protein
- Type VI secretion system baseplate subunit TssF
- Type VI secretion system baseplate subunit TssK
- Type VI secretion system baseplate subunit TssG
- IraD/Gp25-like domain-containing protein
Sequence:
MSTDNPSSWQDLPTVVEITEESRRRNQNARNMAAILEDIVETDEQARPARGKVATLPVDKLLTGFHFGGEEVPTLVQSAAPLLNLAHLLRFSDAEPDPDQLRRACVEAITRYERDLASARISPERARAAHYVVCATVDDVVLSKPWGVRAGWARSGLVSTFHNDVTGGDRVFDILDHFHQSPGANKDLLLLIYLCLSLAFEGRTRVSSKGALELSRIRDSLYKTLIGQYGTFERELSPHWKGVDARHTPLRTMTALWTLLSLMALAFALGYLFFTLSLNNASDVTFERLAHLPPTETPSVLISNPPPHPPAQVEIPRVVEPPKTVAPRQPSRLEKLMAFLQPEVDKKLVTLADVNGRLRVRINNSGLFTTGSADVSPQFRDLIQRIGGALAAEKFRAVVIGYTDTVPIKTVEFPSNWHLSEARAKAVGDILSQFTGPDAILTEGRADSDPIADNKTEEGRQINRRTEIMVLTNPDEKLSDAGILSPPIENSSGQQPGEAQP
Protein: Mitochondrial acidic protein mam33 (O94675)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Non-selective voltage-gated ion channel
- Small ribosomal subunit protein mS29
- Lon protease homolog, mitochondrial
- Rsm22-cox11 tandem protein 1
Sequence:
MNSLRVLKIFRSVSRSIRIPASNGCINLGRNAYRVQLAKAPFSFSSIRRSSHTAGNPRSKLINALSSEIDYEKNQVLSEISLPPVNYDIEDVQGSAVVVLKAKHGDENIRITMNVSQDVTDAVPEEQDFTEFEDEQELQNQGESAEDEFPNEDLGRFQPCTIEISKPGNGALVFEATALDDGFDIENIYFSKDIDMLTSDSLEAEWKRRKQYLGPSFKELDPELQDLFHSYLEERKIDESLSSFIVSFGLTKELKEYINWLESVRQFLK
Protein: Corticotropin-releasing factor-binding protein (CRF-BP) (CRF-binding protein) (Corticotropin-releasing hormone-binding protein) (CRH-BP) (P24387)
Organism: Homo sapiens (Human)
Function: Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy.
Subcellular location: Secreted.
Interaction partners:
- Corticoliberin
- Corticotropin-releasing factor receptor 1
- Urocortin
- Corticotropin-releasing factor receptor 2
- Urocortin-3
- Pro-opiomelanocortin
- Urocortin-2
Sequence:
MSPNFKLQCHFILIFLTALRGESRYLELREAADYDPFLLFSANLKRELAGEQPYRRALRCLDMLSLQGQFTFTADRPQLHCAAFFISEPEEFITIHYDQVSIDCQGGDFLKVFDGWILKGEKFPSSQDHPLPSAERYIDFCESGLSRRSIRSSQNVAMIFFRVHEPGNGFTLTIKTDPNLFPCNVISQTPNGKFTLVVPHQHRNCSFSIIYPVVIKISDLTLGHVNGLQLKKSSAGCEGIGDFVELLGGTGLDPSKMTPLADLCYPFHGPAQMKVGCDNTVVRMVSSGKHVNRVTFEYRQLEPYELENPNGNSIGEFCLSGL
Protein: Two-component response regulator PprB (Q9HWA4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PprA/PprB involved in biofilm formation by controlling the expression of many related genes including type IVb pili major subunit flp pilin, adhesin bapA or cupE fimbriae. Functions as a transcription regulator by direct binding to promoter regions. Negatively regulates its own transcription.
Interaction partners:
- Two-component sensor PprA
- Flp prepilin peptidase A, FppA
- Type IVb pilin, Flp
- histidine kinase
- histidine kinase
- histidine kinase
- Oxygen sensor histidine kinase NreB
- histidine kinase
- Two-component response regulator
Sequence:
MDKPASRHFSVLIIDDEPQVTSELRELLENSGYRCVTSTHRESAIASFQADPNIGLVICDLYLGQDNGIRLIESLKEVAGNGRFFESIILTGHDGRQEVIEAMRVGAADYYQKPVAPQELLHGLERLESRLHERVRSQLSLSHVNQRLEYLAESLNSIYRDIHKIKYEVHGNSQPSALRSEDSQPSAPPAPVAESQVSPSNPLFGKLSPRQQAVARLVSKGLTNYQIAYELGITENTVKLYVSQVLRLMHMHNRTQLALALSPAAMQQGSGAVVH
Protein: Glutamate receptor (Q62683)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}. Postsynaptic density membrane {ECO:0000256|ARBA:ARBA00034112}.
Interaction partners:
Sequence:
MSTMHLLTFALLFSCSFARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYNWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEARELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGIIGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTFPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES
Protein: Diphthine synthase (EC 2.1.1.98) (Diphthamide biosynthesis methyltransferase) (O58456)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
Interaction partners:
- Elongation factor 2
- 2-
- Diphthamide synthase domain-containing protein
- Diphthamide synthase domain-containing protein
- Metallo-beta-lactamase domain-containing protein
- RutC family protein PH0854
Sequence:
MVLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVLSREDVELNFENIVLPLAKENDVAFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVGITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLHTLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGKLHIVEAEYLVEIAGAPREILRVNV
Protein: Nebulin (F6X9B6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XKAVTKHVSDTNYKKKFVKEKGKSNYSIMQEPPEVKHAMEVAKKQSDVAYKKDAKENLHYTTVADRPDIKKATQAAKQASEVEYRAKHRKEGSHGLSMLGRPDIEMAKKAAKLSSQVKYRENFDKEKGKTPKYNPKDSQLYKTMKDANNLASEVKYKADLKKLHKPVTDMKESLIMHHVLNTSQLASSYQYKKNYEKSKGHYHTIPDNLEQLHHREATELQSIVKYKEKYEKERGKPMLDFETPTYITAKESQQMQSGKEYRKDLEESIRGRGLTEMEDTPDMLRAKNATQILNEKEYKRDLELEVKGRGLNAMANETPDFMRARNATDIASQIKYKQSAEMEKANFTSVVDTPEIIHAQQVKNLSSQKKYKEDAEKSMSYYETVLDTPEMQRVRENQKNFSLVLYKEDVSPGTAIGKTPEMLRVKQTQDHISSVKYKEAIGQGTPIPDLPEVKRVKETQKHISSVLYKENVGKATPTPVTPEMQRVKRNQENISSVLYSDSFRKQIQGKAAYVLDTPEMRRVRETQRHISTVKYHEDFEKHKGCFTPVVTDPITERVKKNTQDFSDINYRGIQRKVVEMEQKRNDQDQDTITGLRVWRTNPGSVFDYDPAEDNIQSRSLHMINVQAQRRSRDQSRSASALSISGGEEKSEHSEAADQRLSTYSDGGAFFSATSTAYKHVKTTQLPQQRSSSVATQQTTLSSIPSHPSTAGKIFRAIYDYIAADADEVSFKDGDAIVNAQAIDEGWMYGTVQRTGRTGMLPANYVEAI