wanglab/gogpt-training-data huggingface dataset:
Protein: 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (HSP-65) (Heat shock protein 60) (HSP-60) (Hsp60) (Mitochondrial matrix protein P1) (P63039)
Organism: Rattus norvegicus (Rat)
Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P10809}.
Interaction partners:
- Toll-like receptor 4
- Stress-70 protein, mitochondrial
- 10 kDa heat shock protein, mitochondrial
- Toll-like receptor 2
- 10 kDa heat shock protein, mitochondrial
- Heat shock 70 kDa protein 4
- T-complex protein 1 subunit alpha
- Endoplasmic reticulum chaperone BiP
- Monocyte differentiation antigen CD14
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MLRLPTVLRQMRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
Protein: Ribosomal RNA-processing protein 12 (Q12754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: In association with GSP1, required for nuclear export of both pre-40S and pre-60S ribosomal subunits. Required for the late maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14729571}. Nucleus, nucleolus {ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14729571}.
Interaction partners:
- Periodic tryptophan protein 2
- RNA cytidine acetyltransferase
- Essential nuclear protein 1
- Nucleolar protein 58
- KRR1 small subunit processome component
- Nucleolar complex protein 4
- rRNA biogenesis protein RRP5
- Ribosome biogenesis protein BMS1
- Nucleolar complex protein 14
- Ribosome biogenesis protein TSR1
Sequence:
MDQDKVAFLLELEDKLAKIRSQVNSKLENQKHIAIILTAVEENIAGQATNDVSKNIVNYIISFMSLLDQAVDPSTHEIKDIQLASSSTYLLDLIFHYSPKVLLRSKFSEILTKIAPCITAEKANAPLIRAAIGCLESLLIAQDAQAWNNTYDLNVTPKRGLQGILELSLDVRPKVRKRALDAVHAVLLNPPVAPTAEHVAAVFVADFCDKQLAGILNDLSNLSNKQLKAQKTKEDINASVMRSLRLITSVVSTGQWPSSQIEPLCDVLLGVTKSSEQYLVSASFECFESMFKTMAETTISSGLAENKYLRVLDTIFALKPSNVDTLLTKSWIAVVIKGMSTYATHQPLKALRKIPGVFHIMCTYLASETPEVYQAASQCLISILSESVKDDLLLYTPSVDEKVFKNVDEIISQIAKTFIDFLSIRYSHCSREILKILVAAFNKFRYRSNPHFLKSLKIVDTWRVNEEQFMDLRNEIELVIGASISAMGPEMILAEAPLNLDNPSSERPGRAWLLPLIRDYTKNANLATFQNELAPYIKSFQSKFDKVPEESIQLRVFQTIVDQIWSTLPRFCELPMDLRESFTDEFASELSSLLYSEVELRTTICHALKVLAESNVSYAEESSSHNVLLLQRFPISEAQKNIEYLSTKSTNLLAVLFNVYTQTTPNARSYILETIDQYLKITSKEDLEKTFNNVCGLLKNSMNEESSGNVNKEKKKPQLTATLLDLIICMITYLPVSSYSALFSMFSLTVNSADALIQKRAYRIITKLSELKSGSTAVAQFISDIENVMVDSASSVQTSAKAARLTAIKTIVELLPLDHLDFIVRTVAEVILSTKDVNEKSRETAFDTLICMGRKMNEPNGIIKLFQIPGYDPTTPDQSSSISEFFKIISAGLIGESQHMVSSSITGYACLVFEFKNELDSGILMDIYDTIELYLTSNSREIVKSAIGFTKVCVLGLPEELMRPKVPELLLKLLRWSHEHTGHFKAKVKHIIERLIRRFGYDYIEANFPEEDRRLLTNIRKMRNRNKRKDEEVTTGVSDVAATKGSRFMSAFDEAVYGSDEENDNGSDQEENVAGGKMKNGAKQFIVESGDNPLDLLDSQTLAHISSTRPKKFNKNQNRARFNDDAFNFDSEGKLVVKGQPKPSTNVDDPLSAVTSGINAYLEAVKSGPVRGQRNKLKFRKNGKDSDEFGDDDDGEKDSRLMRGRVNQGNKIGKHNKKGPKFKSRKKL
Protein: Aminopeptidase (EC 3.4.11.-) (B0BCZ2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPNHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG
Protein: AT07729p (Q8IHF4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDRIKIGEQLLFQRSDGRVHQVVCTAKNLERDSITGEWTEGTVVKGKEVPLSTLIGINHHIFAENQPPISKPPSSLLPKPRGSSPTGGPKSHTGNPYAERMRVQDGRSKIATRKTDPAAVGAGNHELGRAHTPRVPASRPDRDASPTQGRKSQGGNNSNQRFSSVVREVNRMKEQREKRRARQAEQLQEKDALRRNNPGNPNWEVSVMLRQYRSTLIFSPLRCLDPNGGTVQQITVCVRKRPMSRKEENSKNLDIITVPSADSLIVHELRLKVDLTKFLEHHKFRFDYTFDEECSNALVYDHTARPLIRTMFEGGNATCFAYGQTGSGKTHTMGGEFFGKVQDCGTGIYAMAARDVFEEVSRPEYRQMGAKITCSFFEIYGTKVFDLLLPNKPMLRVLEDARQQVVVVGLTEMPVTKVEDVLRLIEHGSKERTSGQTSANAKSSRSHAVFQIALHFPDSWGPHGKCSFVDLAGNERGADTQSADRQTRIEGAEINKSLLALKECIRALSRQSSHLPFRGSKLTQVLRDSFVGGKKNKTCMIAMISPSMSCVENTLNTLRYADRVKELIAKEDEHLQSVEGDGEKSPDLNEESEPEMMADEEGDEEPEDEDNQHLTISSEEASSYNNMSYDMSFNHTLNILGPSRNVDIQEVAEQHALLVENLETYAHNFRQLKTDKEIEQYTQNSESALMKLLAMVNRTRDVTHNYNTQKLLKEENQNAYKKGELDESE
Protein: DNA polymerase III subunit alpha (EC 2.7.7.7) (P9WNT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. Pol III also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Beta sliding clamp
- Probable DNA polymerase III subunit delta
- DNA polymerase III subunit gamma/tau
- DNA polymerase III subunit delta'
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- Probable DNA polymerase III
- Protein RecA
- Protein translocase subunit SecA 1
- DNA primase
- DNA polymerase I
Sequence:
MSGSSAGSSFVHLHNHTEYSMLDGAAKITPMLAEVERLGMPAVGMTDHGNMFGASEFYNSATKAGIKPIIGVEAYIAPGSRFDTRRILWGDPSQKADDVSGSGSYTHLTMMAENATGLRNLFKLSSHASFEGQLSKWSRMDAELIAEHAEGIIITTGCPSGEVQTRLRLGQDREALEAAAKWREIVGPDNYFLELMDHGLTIERRVRDGLLEIGRALNIPPLATNDCHYVTRDAAHNHEALLCVQTGKTLSDPNRFKFDGDGYYLKSAAEMRQIWDDEVPGACDSTLLIAERVQSYADVWTPRDRMPVFPVPDGHDQASWLRHEVDAGLRRRFPAGPPDGYRERAAYEIDVICSKGFPSYFLIVADLISYARSAGIRVGPGRGSAAGSLVAYALGITDIDPIPHGLLFERFLNPERTSMPDIDIDFDDRRRGEMVRYAADKWGHDRVAQVITFGTIKTKAALKDSARIHYGQPGFAIADRITKALPPAIMAKDIPLSGITDPSHERYKEAAEVRGLIETDPDVRTIYQTARGLEGLIRNAGVHACAVIMSSEPLTEAIPLWKRPQDGAIITGWDYPACEAIGLLKMDFLGLRNLTIIGDAIDNVRANRGIDLDLESVPLDDKATYELLGRGDTLGVFQLDGGPMRDLLRRMQPTGFEDVVAVIALYRPGPMGMNAHNDYADRKNNRQAIKPIHPELEEPLREILAETYGLIVYQEQIMRIAQKVASYSLARADILRKAMGKKKREVLEKEFEGFSDGMQANGFSPAAIKALWDTILPFADYAFNKSHAAGYGMVSYWTAYLKANYPAEYMAGLLTSVGDDKDKAAVYLADCRKLGITVLPPDVNESGLNFASVGQDIRYGLGAVRNVGANVVGSLLQTRNDKGKFTDFSDYLNKIDISACNKKVTESLIKAGAFDSLGHARKGLFLVHSDAVDSVLGTKKAEALGQFDLFGSNDDGTGTADPVFTIKVPDDEWEDKHKLALEREMLGLYVSGHPLNGVAHLLAAQVDTAIPAILDGDVPNDAQVRVGGILASVNRRVNKNGMPWASAQLEDLTGGIEVMFFPHTYSSYGADIVDDAVVLVNAKVAVRDDRIALIANDLTVPDFSNAEVERPLAVSLPTRQCTFDKVSALKQVLARHPGTSQVHLRLISGDRITTLALDQSLRVTPSPALMGDLKELLGPGCLGS
Protein: Twinfilin-1 (Protein A6) (Protein tyrosine kinase 9) (Q12792)
Organism: Homo sapiens (Human)
Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity).
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts (By similarity). {ECO:0000250}.
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
- Actin, alpha skeletal muscle
- Cofilin-1
- Adenylyl cyclase-associated protein 1
- WD repeat-containing protein 82
- Gelsolin
- Unconventional myosin-Ic
- Destrin
- Plastin-1
Sequence:
MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYTCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAETEATTD
Protein: A kinase anchor protein 11 (E9Q777)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAAFQPLRSSHLKSKASVRKSFSEDVFRSVKSLLQSEKELCSVSGGECLNQDEHPQLTEVTFLGFNEETDAAHIQDLAAVSLELPDLLNSLHFCSLSENEIICMKDTSKSSNVSSSPLNQSHHSGMLCVMRVSPTLPGLRIDFIFSLLSKYAAGIRHTLDMHAHPQHHLETTDEDDDDTNQSVSSIEDDFVTAFEQLEEEENAKLYNDEINIATLRSRCDAASQTTSGHHLESHDLKVLVSYGSPKSLAKPSPSVNVLGRKEAASVKTSVTTSVSEPWTQRSLYRCPSASDKDKDTQETFFPSPVYSSESECSSPSPVIFLDEEGYQKSLKAKLELPEIPVTKDDVEDSDSEVSEFFDSFDQFDELEQTLETYLLMEDPIIGKSSQKIGHKYEKSCMNPQKFKFERPALPANVRKPTPRKPESPYGHLSDAPDSPRPVMTSEDSGLFSPIRTSAFSPPGSCTPAEWFCQTDTSENRNHENYCTYEDYANNLSCEVLGSVLHTQHANTMSDINSIKRGRNHTVTFKYGDSDQKSKCKKSSVITGSVQKFAADLVGKSLGSAFKDLQKGVSSCTNTLCHLAVKLTSSVFQMAFNELRRQCAFSLKERAIGSLASLLVSDALSNALKDLQYVKKQMFTNTVARFAADLAEELVFEGIMEVCQFSCPQTPASSQCQSFDFEDKVVKSYAKDLSESVIQEAFIELSQTNVTFTTKAAVNVSMGNVKYVSAESVSPTQTFTFSSSFSGQAVMMTKPMQEHKKEYTVQQALFCTSGIVTSIPVPLAGSALLPYHMSSTLYPSKCLSSEPSKASGGSTQEHIAIERSAEEVDCLRSTCLPSELNPCNQNDFKPTNGDIDRQSPSKLMSGPVIISNFSAAMVHTIVNETLESMTSFKATKTIDTNADYLTKTIKGKACSPSLCDQAAPQENKASSKDMFAEQLSKSIIKHSLDKSKSMLPNRDKKPGSKEHVLVLGEESQMTLGETPKFLDFSDNSPHRSLLVGNYCVAECKDSVGFGFSLEALPPCSMMTNQKSDLKEVVKDKEVTRHNLNNTALEPMPFGQESSFRHSQTFSSAVLTCVDGLHEEDKQKIRDRNVIPDTPPSTPLVPSQTSSEWDIKTLSKQLKGELAKEFAPATPPSTPHNSSVGSLSENEQTTIEKEEFMLKLMRSLSEEVESSEGEEHPGMHVKAEHPGKKVQFAEAFATHIISLATEAAASHLDHETTQEFKVQNPHLNVPSQRNVLPALSHSDESIQTCTFASDMAADVIAEAEKIANARSCMLFRHERNICHVEGGRGKAEEKLDVEDVAHPREVDTCVLSLPSGMPGLTYKYPSCESVTDEYAGHVIQVLQQQGGSGELIMEQYASRLAYRSVTAAAREAAKTVKMKCGSKLFPLHGCHGKTNKELLVFSSKERHQEVDRQRKRNGSHLCKYQTCERTQDPCRNELSELYSFSASLASSITRDAKKQLTAPKVDLPKSSTDGCFFEKSECVDSSENVTGPERSKSCQPLQSHGFCQNTGYLSGYSCAENAQAIEQYARKVVGDTLELSLGPTVFHNSETTASADRITYAEKLSPLINEACRYCDLKEFHGCTRNSAQLFSKQSPCASAKPSSRSKLSSIRQKSRIFHLDVPQIHVNLDKRAVLAEKIVAEAIEKAERELSNTSLAADSGIGQDGISFAESLTTEIMTTAVTNAGHAVSSSREIEDFQSTESLGSQQMNLSVGEDSTGSWSNLSFEDDHQDESSSFHHLSESNGNSSSWSSLGLEGDLYEDNLSFPTSDSDGSDDGDDEQEDGVEDLQQNGKTLLIMNIDMEPGAVDPQLRIILQWLIASEAEVAELYFQDSAKKEFILLSKQLQEKGWKVGDVLQAVLKYYEVVEKPSREERCKSLFDWLLENAQNRLQTSMLV
Protein: Histone H3.Y (Histone H3.Y1) (P0DPK2)
Organism: Homo sapiens (Human)
Function: Primate-specific variant histone H3, which constitutes a core component of nucleosomes. Histone H3.Y-containing nucleosomes accumulate around transcription start sites and have flexible DNA ends, suggesting that they form relaxed chromatin that allows transcription factor access. Histone H1 binds less efficiently to histone H3.Y-containing nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (Probable).
Subcellular location: Nucleus {ECO:0000269|PubMed:20819935}. Chromosome {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823, ECO:0000305|PubMed:20819935}. Note=Histone H3.Y-containing nucleosomes are depleted from repressive post-translational histone modifications (PubMed:28334823). Histone H3.Y-containing nucleosomes accumulate around transcription start sites (PubMed:27016736). {ECO:0000269|PubMed:27016736, ECO:0000269|PubMed:28334823}.
Interaction partners:
- Histone H4
- Histone H2A type 1-B/E
- Histone H2B type 1-J
- Histone H2B type 1-K
- Cytokine-like nuclear factor N-PAC
Sequence:
MARTKQTARKATAWQAPRKPLATKAAGKRAPPTGGIKKPHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQAISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRVTIMPRDMQLARRLRREGP
Protein: MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 4 (MA3 domain-containing protein 7) (Q9STL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytosol {ECO:0000269|PubMed:29084871}.
Interaction partners:
- F-box protein At5g18160
- Cytochrome P450, family 705, subfamily A, polypeptide 18
Sequence:
MATREWFVMNAQQTKLALESPPLFAVKKDDDKDHTCDTGEEPYALVGSPVFNPLEDYKREVVSIIDEYFSSGDVEVAASDLMDLGLSEYHPYFVKRLVSMAMDRGNKEKEKASVLLSRLYALVVSPDQIRVGFIRLLESVGDLALDIPDAVNVLALFIARAIVDEILPPVFLARAKKTLPHSSQGFQVILVSENSYLSAPHHAELVETKWGGSTHITVEETKRKISEFLNEYVENGDTREACRCIRELGVSFFHHEIVKSGLVLVMESRTSEPLILKLLKEATEEGLISSSQMAKGFSRVADSLDDLSLDIPSAKTLFESIVPKAIIGGWLDEDSFKERSDQNGGSENLRRFKKDAETIIQEYFLSDDIPELIRSLEDLGLPEYNPVFLKKLITLAMDRKNKEKEMASVFLASLHMEMFSTEDFINGFIMLLESAEDTALDILAASDELALFLARAVIDDVLAPLNLEEISNSLPPKSTGSETIRSARSLISARHAGERLLRSWGGGTGWAVEDAKDKIWKLLEEYEVGGVISEACRCIRDLGMPFFNHEVVKKALVMAMEKKNDRMLNLLQECFAEGIITTNQMTKGFGRVKDSLDDLSLDIPNAEEKFNSYVAHAEENGWLHRDFGCSTDS
Protein: Aminoacyl carrier protein 1 (Q89VT6)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: Aminoacyl carrier protein. Can be charged with L-glycine via the formation of a thioester bond between the amino acid and the 4'-phosphopantetheinyl prosthetic group, catalyzed by the bll0957 ligase.
Interaction partners:
- Amino acid--[acyl-carrier-protein] ligase 1
- Blr2316 protein
- Bll2237 protein
- NADH-quinone oxidoreductase subunit C
- Blr2108 protein
- Probable alginate O-acetylase AlgI
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL32
- NADH-quinone oxidoreductase subunit B
- Bll0263 protein
Sequence:
MQAFNTDVRNRIIKLVKGILEQNALAADVTPQAKLVDVGLTSMDMVNLMLGVEAEFDFTIPQSEITPENFQSVETLERMVMTQLQPATAA
Protein: Transcriptional regulator ERG (P81270)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}.
Interaction partners:
- Transmembrane protease serine 2
- Transcription factor PU.1
Sequence:
MIQTVPDPAAHIKEALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDWLSQAPARVTIKMECNPSQVNGSRNSPDECSVNKGGKMVGSPDTVGMSYGSYMEEKHVPPPNMTTNERRVIVPADPTLWSTDHVRQWLEWAVKEYGLLDVDVLLFQNIDGKELCKMTKDDFQRLTPSYNADILLSHLHYLRETPLPHLTSDDVDKALQNSPRLMHARNTGGAAFIFPNTSVYPEATQRITTRPDLPYEPPRRSAWTGHSHLTPQSKAAQPSPSAVPKTEDQRPQLDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSSNSNCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPPESSLYKYPSDLPYMGSYHAHPQKMNFVSPHPPALPVTSSSFFASPNPYWNSPTGGIYPNTRLPASHMPSHLGTYY
Protein: L-arabinitol 4-dehydrogenase (EC 1.1.1.12) (Q5BET8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Probable NAD
- L-xylulose reductase
- Short chain dehydrogenase
- Mannitol 2-dehydrogenase
- Phosphotransferase
- Hexokinase
- Phosphotransferase
- fructan beta-fructosidase
- Tc1-like transposase DDE domain-containing protein
- 2-oxoglutarate reductase
Sequence:
MATATVLEKPNIGVFTNPKHDLWVAESKPTLEEVKSGESLKPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGDVIAVAPDVTSLKVGDRVAIEPNVICNACEPCLTGRYNGCEKVAFLSTPPVDGLLRRYVNHPAVWCHKIGDMSYEDGALLEPLSVSLAAVERSGLRLGDPCLITGAGPIGLITLLSARAAGATPLVITDIDEGRLKFAKELVPEVRTYKVEIGFSAEETAEGIINAFNDGQGAGPDALRPRIALECTGVESSVASAIWSVKFGGKVFVIGVGKNEMKIPFMRLSTQEIDLQYQYRYCNTWPRAIRLVKNGVINLQKLVTHRYALEDALKAFETAANPKTGAIKVQIMSSTADVEAASAGQKN
Protein: Lipid phosphate phosphatase epsilon 2, chloroplastic (AtLPPE2) (EC 3.1.3.-) (Phosphatidic acid phosphatase epsilon 2) (Plastidic phosphatidic acid phosphatase epsilon 2) (Q6NQL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a secondary role as PAP in plastids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:17652095}; Multi-pass membrane protein {ECO:0000305|PubMed:17652095}.
Interaction partners:
- Lipid phosphate phosphatase gamma
- Lipid phosphate phosphatase 1
- Lipid phosphate phosphatase 2
- Putative lipid phosphate phosphatase 3, chloroplastic
- Mediator of RNA polymerase II transcription subunit 6
- Phosphatidate phosphatase PAH1
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 23
Sequence:
MAASSSSLLLLHKPTYNFHFAASSVPTYINSARFRISSSIFPLDRRRRRRIWSVSGFKSMADLVKTNARRDGEDRFQALEQEAFISNSSSELQNELVSDAGDGIEAIANRLSKWIVAALFGSVLLLRHDGAALWAVIGSVSNSVLSVALKRILNQERPVATLRSDPGMPSSHAQSISFISVFSVFSVMEWLGTNVLSLFLSGFILALGSYFTWLRVSQKLHTTSQVVVGAIVGSVYSTLWYVTWNSLVLEAFTSTFSVQIALFLVAAASALGFAVYVLLNWFKDDR
Protein: Methylphosphonate synthase (EC 1.13.11.73) (A9A1T2)
Organism: Nitrosopumilus maritimus (strain SCM1)
Function: Catalyzes the conversion of 2-hydroxyethylphosphonate into methylphosphonate in the methylphosphonate biosynthesis pathway.
Interaction partners:
Sequence:
MEKKIDFKPDSYLIRSGNNFLGILNDIKRRPEDAANELGVSIEEINSIISGKQKISPSLIEKAVNIWPVNERDFYIVSDDCSSGILIMTSQDSIKSSRIMERAGKPYYEYRDTAMSKTAPFRPEWILELCKVENNDPENPKAQWNNGHFMHQFTYFIGEVNFYYKDPEGKKHVAIMNTGDSMYITPFTPHTFTTRDGASQNGLILALTYGSKLTGDIQQELSSLSLDCGSQYALDFTNHENASLSLLEYYFELSNLTKEKFAKRTNFSMETLADFFTKKKLPTFDELKIIAKALNVNSRDLMPNDLTESKVIVKTHDQCDHWKYPESGNYEFYELASTTALPHSKAFEIDVSSSEDLNLDLKVGLHQYVYNIGDSALTINWNYENKTYQKSLNPGDSAYIKPFVPHNFRGNGKILILRIGGKISGDSQRELSFVGRENTQRAISETMQWFDPKGSNS
Protein: E3 ubiquitin-protein ligase RNF125 (EC 2.3.2.27) (RING finger protein 125) (T-cell RING activation protein 1) (TRAC-1) (Q96EQ8)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins, such as RIGI, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53. Acts as a negative regulator of type I interferon production by mediating ubiquitination of RIGI at 'Lys-181', leading to RIGI degradation. Mediates ubiquitination and subsequent degradation of p53/TP53. Mediates ubiquitination and subsequent degradation of JAK1. Acts as a positive regulator of T-cell activation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17990982}; Lipid-anchor {ECO:0000269|PubMed:17990982}. Note=Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane. {ECO:0000269|PubMed:17990982}.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- Interferon-induced helicase C domain-containing protein 1
- Nuclear protein localization protein 4 homolog
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- E3 ubiquitin/ISG15 ligase TRIM25
- Citrate synthase, mitochondrial
- Mitochondrial antiviral-signaling protein
- E2 ubiquitin-conjugating enzyme
Sequence:
MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDENPSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT
Protein: F-box protein dre-1 (Daf-12 redundant function protein) (Q94251)
Organism: Caenorhabditis elegans
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins including blmp-1. Heterochronic protein which is required for the timing of gonad development and epidermal seam cell differentiation. Regulates tail-spike cell death through inhibition of the apoptosis regulator ced-9.
Subcellular location: Nucleus {ECO:0000269|PubMed:17336909}. Cytoplasm {ECO:0000269|PubMed:17336909}.
Interaction partners:
- Skp1-related protein
- B lymphocyte-induced maturation protein 1 homolog
- Uncharacterized protein
- Cullin-1
- Period protein homolog lin-42
- Casein kinase I isoform delta
- Zinc finger transcription factor lin-29
- Glycerophosphocholine cholinephosphodiesterase
Sequence:
MSSSSSPFFHPPPQQVMDDTTQQSPSYSQNSNSPSQHTFESMEPAAGGSTSMRYSPSGSSEADNPTLGLFSAQASYPYSLRKRRPCLTKDEDLCFPITAATADETPQPTMKKFKLECLSPGEARDFSIEDESGTNLEAKMETTECEPEEEEAVEEEDQQDHINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELYCNLYDYRIPLFHPSHAKFEFREQSRWRDGNPWKESHRQLHHGVHVMKEPRVNLRSVNYRCFDQIEKAQSFLEEDEYREKLIFLHTGVHEPIDTILINTDVQIIGASDSRDITSSVVLEGSKNTALTFTDGSANAYFGFITVRFRADPVCRQQPQIAQQAQQMNHFYSILVTDKDAMPYIERCDITSKVGNGAAVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQGYFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRGLIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYVHEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHGLLEENDIFNHLYSGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKGLLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNGATATLEENQLFRNKYGGLCVATGVTPVQRGNRIYDNHDTISRAIKTGLCLFKVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCHLQNVPRDNDTVYDSATPISTETGTEI
Protein: Glia maturation factor (Q7ZUD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zgc:101810
- Actin-related protein 2-B
- Actin-related protein 2-A
- Twinfilin-1
- Twinfilin actin-binding protein 2b.
- Actin-related protein 3B
- Actin-related protein 3
- Twinfilin-2
- Arp2/3 complex 34 kDa subunit
Sequence:
MSESLVVCEVDEDLVKKLRDFRFRKETNNAAIIMKIDKDKQLVILEEEHEDISPEDLKNELPERQPRFVVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLVQTVELTKVFEIRNTEDLTEEWLREKLGFFR
Protein: NAC domain-containing protein 2 (ANAC002) (Q39013)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Basic leucine zipper 8
- Dehydration-responsive element-binding protein 2A
- Floral homeotic protein APETALA 2
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
- At5g52380
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- Chaperone protein ClpD, chloroplastic
- Transcription factor MYC2
- ABSCISIC ACID-INSENSITIVE 5-like protein 7
- Transcription factor MYB83
Sequence:
MSELLQLPPGFRFHPTDEELVMHYLCRKCASQSIAVPIIAEIDLYKYDPWELPGLALYGEKEWYFFSPRDRKYPNGSRPNRSAGSGYWKATGADKPIGLPKPVGIKKALVFYAGKAPKGEKTNWIMHEYRLADVDRSVRKKKNSLRLDDWVLCRIYNKKGATERRGPPPPVVYGDEIMEEKPKVTEMVMPPPPQQTSEFAYFDTSDSVPKLHTTDSSCSEQVVSPEFTSEVQSEPKWKDWSAVSNDNNNTLDFGFNYIDATVDNAFGGGGSSNQMFPLQDMFMYMQKPY