wanglab/gogpt-training-data huggingface dataset:
Protein: Chitinase 3 (EC 3.2.1.14) (P40954)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation.
Subcellular location: Secreted {ECO:0000269|PubMed:20641015}.
Interaction partners:
- Chitinase 4
- Glucan endo-1,3-beta-D-glucosidase 1
- Chitinase 2
- Ngs1p
- chitin deacetylase
- Beta-hexosaminidase
- Chitinase 1
- Glucan endo-1\3-beta-D-glucosidase
- Filamentous growth regulator 41
- Protein DSE1
Sequence:
MLYLLTIFSLLLPALAINARSNSNVAVYWGQNSGGSQQRLSYYCDSDAVDIVILSFMHQFPSPIQLNFANACEGTYTANGILQCQTIAEDIKYCQNKGKTILLSLGGAAGSYGFSDDATAKQFAHTLWDLFGNSKNLATNDRPFYDAVLDGFDFDIENNWSTGYPALATELRTLFQKDTSKNYYLGAAPQCPYPDASVGPLLKQSEIDFVFIQFYNNYCNLGSSSFNWDTWLNYAETDSPNKNIKLFVGVPASSRAAGSGYNDPSAVSQYLTSDILNSKYFGGISMWDVSAGWSNTNSNGNFVENMKAIVKKASPGEETTSSSTTTTTTTTSTTISSSSSSSKTSKTSTTSTTSSSISSTTSSTTSSTSSSSTSSSTSSTTSSSTTSSQISTTSTAPTSSTSLSSSTISTSASTSDTTSVTSSETTPVVTPSSLSSAITIPGDSTTTGISKSSSTKPATSTTSALSSSTTTVATIPDDKEIINTPTDTETTSKPPAIITESDATTITQNLTPSTTTKNVKTTSTNIVTEWVWAPTTLRTLTTTYQILTTRTHIETVFAEPSTVVIYN
Protein: Inter-alpha-trypsin inhibitor heavy chain H2 (ITI heavy chain H2) (ITI-HC2) (Inter-alpha-inhibitor heavy chain 2) (Q61703)
Organism: Mus musculus (Mouse)
Function: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.
Subcellular location: Secreted.
Interaction partners:
- Protein AMBP
- Vitronectin
- Alpha-2-HS-glycoprotein
- Prothrombin
- Beta-2-glycoprotein 1
- Fibrinogen alpha chain
- Heparin cofactor 2
Sequence:
MQRPVCLLIWLFLLEAQAFEIPINGNSEFAEYSDLVELAPDKLPFVQENGRHQRSLPEESGEETDTVDPVTLYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEKTVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQEVKWRKLGSYEHKIHLQPGKLAKHLEVNVWIIEPQGMRFLHVPDTFEGHFQGVPVISKGQQKAHVSFKPTVAQQRKCPNCTETAVNGELVVMYDVNREEKAGELEVFNGYFVHFFAPENLDPIPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGTNINEALLRAIFILNEASNMGLLNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLSNENRGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPQASVTDVTQNNFHNYFGGSEIVVAGKFDPSKLTEVQSIITATSANTELVLETLSQMDDLEEFLSKDKHADPDFTKKLWAYLTINQLLAERSLAPTAAIKRKITKTILQMSLDHHIVTPLTAMVIENDAGDERMLADSPPQDHSCCSGALYYGTKVASGPIPSWANPSPTPMSAMLAVGAKPLESTPPTHLNQVENDPHFIIYLPKSKRNICFNIDSEPGKILSLVSDPESGIVVNGQLIGAKRAENGKLSTYFGKLGFYFQKEGMKIEISTETITLSSGSSTSRLSWSDTAHLGNSRVLISVKKEKSVTLTLNKELFFSVLLHRVWRKHPVNVDFLGIYAPPIDKFSPRVHGLLGQFMQEPAIHIFNERPGKEPGKPEASMEVKGHKLTVTRGLQKDYRTDIVFGTDVPCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP
Protein: Creatine kinase U-type, mitochondrial (EC 2.7.3.2) (Acidic-type mitochondrial creatine kinase) (Mia-CK) (Ubiquitous mitochondrial creatine kinase) (U-MtCK) (P25809)
Organism: Rattus norvegicus (Rat)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Interaction partners:
- Creatine kinase S-type
- ADP/ATP translocase 1
- Non-selective voltage-gated ion channel VDAC1
- Non-selective voltage-gated ion channel VDAC3
- Non-selective voltage-gated ion channel VDAC2
- Guanidinoacetate N-methyltransferase
- Creatine kinase B-type
- Creatine kinase M-type
- Ankyrin repeat and SOCS box-containing 9
- ADP/ATP translocase 2
Sequence:
MAGPFSRLLSARPGLKLLALAGAGSLAAGILLRPESVRAATGERRRLYPPSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAELFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKKVEKLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVKLPLLSKDSRFPKILENLRLQKRGTGGVDTPATADVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLEKGQDIRIPPPLVHGKH
Protein: Borealin N-terminal domain-containing protein (Q57WI5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Splicing factor 3B subunit 1, putative
- Regulator of nonsense transcripts 1, putative
Sequence:
MTEQTEAEVQKRETSTSESSAGGPTFNFAEGAGTPLKELPSLKKIRARSIAMRQLETSIEPLHRLVYGRPGRMGERWGALEEFCGFPEYKREEVVDRLGRIAKRRLRDFVMATGMRINVSQKLPKLAQDVTAFLMSPQSEGVIDPELEAAKPKKGSSRKSTQRGRKTAKRPASTRSRRANGSERKTPTKRLARNSTLRAASLESPSDDTLRVAIFRRVLFTPQTERSYLTTKVLRLELQEKFGDLEHRKAIIKEAAAECVSALISAESAAIAFTNSNMSSTTDTTIKTNDFTQPGTVSSENGSPA
Protein: Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein) (OST oncogene) (Q63406)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways. Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7957046}. Cell membrane {ECO:0000250|UniProtKB:Q64096}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64096}; Cytoplasmic side {ECO:0000250|UniProtKB:Q64096}.
Interaction partners:
- Cell division control protein 42 homolog
- Transforming protein RhoA
Sequence:
MSNCWCFIFCKERVRSNSSSPQHDGTSREEADHQVDVSDGIRLVPDKAEATMATASDEIMHQDIVPLCAADIQEQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRQDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLDYCHSRWLCHRTAIESFALMVKQTAQMLQAFGTELAETELPNDVQSTSLVLSAHTEKKAKVKEDLQLALTEGNSILESLREPLAESIVHSVNQDQLDNQATVKRLLTQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGFREVKTALDSMSQKIAAFTDVGNSLAHVQHLLKDLTTFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHPKCEELQHLCDHFASEVTRRRDLLSKSLELHSLLETSMKWSDEGIFLLASQPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNKIYKEYECILNQDLLEHVQKVFQKQESTEEMFHRRQASLKKLAAKQTRPVQPVAPRPEALTKSPSPSPGSWRSSENSSSEGNALRRGPYRRAKSEMSEPRQGRTSSTGEEEESLAILRRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHLISTGLQNKKNILFGNMEEIYHFHNRIFLRELESCIDCPELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQCSDCPFFQECQKKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSHSLPLPTPASTSPTKGSTRNVKKLEDRKTDPLCLEGCVSSSLPKPPEKGKGWSKTSHSLEAPEEDGGWSSAEELINSSDAEEDGGVGPRKLVPGKYTVLMDGEKGGSDTLAMRSGDMVEVVEEGTEGLWYVRDLTSSKEGWVPASSLATLLGKSSSAQCLSSSGKTHCARQLCPEPAKILSPEPV
Protein: Zinc finger protein 860 (A6NHJ4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MLREEAAQKRKEKEPGMALPQGHLTFRDVAIEFSLEEWKCLDPTQRALYRAMMLENYRNLHSVDISSKCMMKKFSSTAQGNTEVDTGTLERHESHHIGDFCFQKIGKDIHDFEFQWQEDKRNSHEATMTQIKKLTGSTDRYDRRHPGNKPIKDQLGLSFHSHLPELHIFQTKGKVGNQVEKSINDASSVLTSQRISSRPKIHISNNYENNFFHSSLLTLKQEVHIREKSFQCNESGKAFNCSSLLRKHQIIYLGGKQYKCDVCGKVFNQKRYLACHHRCHTGEKPYKCNECGKVFNQQSNLASHHRLHTGEKPYKCEECDKVFSRKSNLERHRRIHTGEKPYKCKVCEKAFRRDSHLTQHTRIHTGEKPYKCNECGKAFSGQSTLIHHQAIHGIGKLYKCNDCHKVFSNATTIANHWRIHNEERSYKCNKCGKFFRRRSYLVVHWRTHTGEKPYKCNECGKTFHHNSALVIHKAIHTGEKPYKCNECGKTFRHNSALVIHKAIHTGEKPYKCNECGKVFNQQATLARHHRLHTGEKPYKCEECDTVFSRKSHHETHKRIHTGEKPYKCDDFDEAFSQASSYAKQRRIHMGEKHHKCDDCGKAFTSHSHRIRHQRIHTGQKSYKCHKRGKVFS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q95T82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASLQPAGSMLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFVPPDCQSLLRGMIEVNPDRRLTLAEINRHPWVTAGGKGELELELPMMEVVQTHVIPTATAVDPDVLNAICSLGCFKEKEKLIQELLSSSHNTEKVIYFLLLERKRRRPALEDDDEIAQKSRSELDAVDPPRKRLDTCRINGTNAPSYGQISEGSPLTPRRQAFNFRSYSSTRNHQRRSPTTVTSSVRSSSYHSPTRCNSPMSSAQQQANAISRPSSPAAGTRHSTYGDRDRSGHHSSVSRTPSHSSQKSIEGDVVVVREPRIERRDSLRQERGGGSPRDRGDCGIPPGSPGGNSSGSTSASPSVHHRANSGPTIAISMFHDPDSNSVVNPNGSPMMNNSSPGMPGSPCNTPGGQLWKTRLTNIKNSFLGSPRFHRRKMQVSADEVHLTPESSPELTKRSWFGNLITTEKDETFTILVKGKPIATVKAHLIHAFLSMAELSHSVVSPTSFRVEYKRNGNGPVMFQRHVKFQVDISAICKQGDIADMLFALTFTLLSGNIRRFRRICEHIQSQVCSKRFPGPSSPPTVTSVTQAVSESSSCGSVSSERLSYKRQVIENDMENDSIFSYKSGNGRRASTTNNNNANPVDIPGSPIAVRSNSETAEHERNRELQSERQATTMSGSAIA
Protein: Transcription factor twist1 (Twist family bHLH transcription factor 1a) (Twist-1 protein) (Twist-related protein 1a) (Twist1a) (Twist1b) (Q9PTE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger protein SNAI2
- Zinc finger E-box-binding homeobox 1b.
- Zinc finger E-box-binding homeobox 2a.
- Zinc finger protein SNAI2
- Cadherin 1, type 1, E-cadherin
- Catenin beta-1
- Sna-1 protein
- Cadherin-2
- Paired mesoderm homeobox protein 1a
- Forkhead box protein D3
Sequence:
MFEEEAMHEDSSSPESPVDSLGNSEEELDRRQPKRVSRKKRASRKNAEDSDSPTPGKRSKKCSNSSSSPQSLEDLQTQRVMANVRERQRTQSLNEAFASLRKIIPTLPSDKLSKIQTLKLAARYIDFLCQVLQSDELDSKMSSCSYVAHERLSYAFSVWRMEGAWSMSTSH
Protein: Hydroxycarboxylate dehydrogenase B (EC 1.1.1.-) (2-oxoglutarate reductase) (Hydroxyphenylpyruvate reductase) (EC 1.1.1.237) (Phenylpyruvate reductase) (P30178)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions.
Interaction partners:
- Aromatic-amino-acid aminotransferase
- Aspartate aminotransferase
- D-amino acid dehydrogenase
- Histidinol-phosphate aminotransferase
- Uncharacterized protein YbfB
Sequence:
MESGHRFDAQTLHSFIQAVFRQMGSEEQEAKLVADHLIAANLAGHDSHGIGMIPSYVRSWSQGHLQINHHAKTVKEAGAAVTLDGDRAFGQVAAHEAMALGIEKAHQHGIAAVALHNSHHIGRIGYWAEQCAAAGFVSIHFVSVVGIPMVAPFHGRDSRFGTNPFCVVFPRKDNFPLLLDYATSAIAFGKTRVAWHKGVPVPPGCLIDVNGVPTTNPAVMQESPLGSLLTFAEHKGYALAAMCEILGGALSGGKTTHQETLQTSPDAILNCMTTIIINPELFGAPDCNAQTEAFAEWVKASPHDDDKPILLPGEWEVNTRRERQKQGIPLDAGSWQAICDAARQIGMPEETLQAFCQQLAS
Protein: Mitochondrial potassium channel (MITOK) (Coiled-coil domain-containing protein 51) (Q96ER9)
Organism: Homo sapiens (Human)
Function: Mitochondrial potassium channel located in the mitochondrial inner membrane. Together with ABCB8/MITOSUR, forms a protein complex localized in the mitochondria that mediates ATP-dependent potassium currents across the inner membrane (that is, mitoK(ATP) channel). May contribute to the homeostatic control of cellular metabolism under stress conditions by regulating the mitochondrial matrix volume.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:31435016}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane {ECO:0000269|PubMed:31435016}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial potassium channel ATP-binding subunit
Sequence:
MMGRSPGFAMQHIVGVPHVLVRRGLLGRDLFMTRTLCSPGPSQPGEKRPEEVALGLHHRLPALGRALGHSIQQRATSTAKTWWDRYEEFVGLNEVREAQGKVTEAEKVFMVARGLVREAREDLEVHQAKLKEVRDRLDRVSREDSQYLELATLEHRMLQEEKRLRTAYLRAEDSEREKFSLFSAAVRESHEKERTRAERTKNWSLIGSVLGALIGVAGSTYVNRVRLQELKALLLEAQKGPVSLQEAIREQASSYSRQQRDLHNLMVDLRGLVHAAGPGQDSGSQAGSPPTRDRDVDVLSAALKEQLSHSRQVHSCLEGLREQLDGLEKTCSQMAGVVQLVKSAAHPGLVEPADGAMPSFLLEQGSMILALSDTEQRLEAQVNRNTIYSTLVTCVTFVATLPVLYMLFKAS
Protein: RNA polymerase II degradation factor 1 (O43024)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor rhp26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35732}. Nucleus {ECO:0000250|UniProtKB:P35732}. Chromosome, telomere {ECO:0000250|UniProtKB:P35732}. Note=During transcription stress, localizes to the nucleus following proteolytic cleavage by the proteasome. {ECO:0000250|UniProtKB:P35732}.
Interaction partners:
- Nucleoporin nup189
Sequence:
MSENKKFRPKKVGNTEQVSEKQHTDTALNISQDNKTSSSSAKRGAKGRRGTKGKSGPANSSQTSNIEGSNALELEFDRDSQLSVLQELFPSWTIDDLSFALEEADRDLELTILHITEGHASKWGEVKKKPIPKTKSKPTSHAPVSDNVSSTFRNATRKSKKPSASKDTSRGVRKSKAGAPSDPSSVHAPSSLEKPAGTGDLPSSEISTKAPASTTVSSSVDPGTINEDSSMKDHTTSNEQASVLTSANTAASTNTNGTAGGTSASAKSTSAADQAVASSKPIKKAWASVAKSKKKVTPAPAPAPESEPSKPSIAPSQPSKTNVSAAYEKPAELSSSSVPFPHKSQDSATPANVETTPSTATSAPKKSTAPFAINAVKPAPGLSNISSASLPKPSFAKQAAVGSQSSTTSMTTARLLSDRFPVVMPVANTAAIPEKVQVRFGSLTLGGEDKKSTKSSSDNIAQSGPRSSYFPKKTVSPKPEAKKEASKVAESTKIPKKQHTSAYESRAPQSKVPENLKESHVNETPYRGLHDVNLPASGNASSVSAIPPQVSAQTTIPAASTSATSGPVVGKQSAGYGGIYSPATHGISPQPYAGASLIPPSTGAAFNNETASSNAGETTALPYSSRFMNPVENRSANSPFDNFQHIDHSTELGYASNTSQQYQQTSHPAYTTMSPIEYGQAAPAAHYYNERNQYSQYDNVAGSASNTPDVHSVMHNKVASSNATSLPAAGTATPSPVVSQQQPQPYAFPPMYPIPYVSYGYGTMPYNNNKFGQPQQGYMSQSGFNDFPPIFGGHSNVYNRQQPGNVSGMSGTQTSNPINNATANTSGMTEKAAGHRDSVIGNGGVTGANSMSSTLGGLSSMSGMGRAAPGMFMGNVGSFENLSANAASPYGLPPQQTPLTNAATQQTTSFQSNANKVNNANSQPAGFPFNSGASTNAGSNGLGGYNAYNQSFINRPGGWYGNA
Protein: GTP-binding protein gtr2 (EC 3.6.5.-) (O74544)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P53290}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding protein gtr1
- Serine/threonine-protein kinase tor2
- Nitrogen permease regulator 2 homolog
- Target of rapamycin complex 1 subunit mip1
- Nitrogen permease regulator 3-like protein
- Uncharacterized protein C1778.05c
- Uncharacterized WD repeat-containing protein C4F8.11
- Serine/threonine-protein kinase tor1
- Uncharacterized WD repeat-containing protein C12G12.01c
- Vacuolar membrane-associated protein iml1
Sequence:
MKPRKIILMGLRRSGKSSIQKVVFYKMPPNETLFLESTSKLTQDHISSFIDFSVWDFPGQVDVFDAAFDFESIFTQVGALIFVIDAQDDYLDALARLHVTVARVVTINPNICIEVFIHKVDGLSDEFKIDTQRDIQQRTQDELADIGLENVPISFHLTSIFDHSIFEAFSRVIQKLIPQLPTLENLLNIFCSNSLVEKAYLFDVLSKIYVATDSSPVDVQSYEICSDFIDVILDIGSIYGRSSQLKPGHSPEILDETSSVIRLSNDLVLFLREMNQYLALICIVRADNFEKSGLIEYNVQCLQTAIQSIFSPRT
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Q583X2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial DNA polymerase I protein B, putative
- DNA polymerase theta
Sequence:
MSLHGHPYQRYVSVKLTHFQQGDENDGPTKSGGVESGSNREKWRAFGVDIGVNLASATSQSSCTSSSTQSQMVNDASITKTASVQESLRQQLAVLTSRVGQTREQIFNAVRLKEKTSSKSTSNTCTPSSVTTDTEIIGGGSAPPSQKRVPGKDGLSRDSAKNKRSTTSDNNIVLNKGAGSTATHQQQEAGQQISEKKTKTRARKSSTLSNAEATVTSRHSSKCATQRTLFKLPVDPATSPQRGLQVAFKEELDGSALFNDARDTLNDPNRFQVPTIFVGFATREGQTNFTISSSSRGKVHFMRGVNPELSHLEVSFLVVRWKDDVIVYSAAVGLELLVRVAEELPGVEIVTFNAPCLLLPLLSYKQGKFFTSCVSDVRLMTWMLEPSADTAEFADYDKLLQSYQQQIGLPAGLNAAECKGSKEAVSHRVFYMEPLYRMLYGRLGSHGLLPAFLKQEKRISIMCAAMKLNGFYVNLVEVDGFKARCAEKMEKLRSEARSMIPSMTNFNIQSADDCRVALYEVLKLGPNLVSKGTEGSTENNSLILTRGGKLSTSEETLRILARHHEFPRILIAYRKLAKLLQTYVVGFMEMAIPIEEGDGEFTDFSISEQGKEAIPNASDRHKAKWAKLHPNLVQEGTETGRLTSVEPNMQALPRSTQLVATHEKNNTNDADSENGNNENINGDVNAADAGGNESDGPVQEKEVSFIRRCLGAPDGYSLVSLDYEQVELRVLAHLSGDSALINVLTKSGDIHRSIAEIIFRKTSVTGEERSLAKKVVFGILYGAGPRGLAQQMGVSVEQALRVSSLFKSCFPTVDAYQRRIIDQCRSDGSVRTLSGRVRSIPDINDRVLTKRSHAERQAFNTVVQGSAADVMKLGMIAVEREVLQPHAPDVRLLLQVHDEIILSVPNHMLHSIVPAAMHAFAHPISLLVPLLVTTKVGRLLGDLEEWTVDHALGLRVPS
Protein: Uncharacterized protein YebV (P64503)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Protein ElaB
- Uncharacterized protein YodD
- Uncharacterized protein YgaM
- Potassium binding protein Kbp
- UPF0339 protein YegP
- Uncharacterized protein YebW
- Fructose-bisphosphate aldolase class 1
- Uncharacterized protein YqjD
- Uncharacterized protein YbgS
Sequence:
MKTSVRIGAFEIDDGELHGESPGDRTLTIPCKSDPDLCMQLDAWDAETSIPALLNGEHSVLYRTRYDQQSDAWIMRLA
Protein: Protein phosphatase 1, regulatory subunit 9A (H3BKQ7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPSENAAIIAKTRGKGRPSSPQRRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSVHESGQNHRYSPKKEKGGGTEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSEPPGALTSGKAESADYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSKPPSNKQDTDTEDAQKSDAVPVPEVAQKGTSLASLPSEESQLSTEAEDVTTAQPEALDSTDKDSPEEPSAENQAMPKSHILSPRNEPLEDAEANVVGSERAQHQKKDLTGGDLTSPDASASSCGREVPEDSNSFESSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENNYYQPDMEYSEIVGLPEEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTDGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEGGPILPSGDVAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEVERKKREEVEKAHLLEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKPSDTITTHMLPNRFCPRLGEFLLQNRSVVSHSSPP
Protein: Vacuolar protein sorting-associated protein 35 (Q54C24)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26
- WASH complex subunit 2
- Phox domain-containing protein
- PDZ domain-containing protein
- PX domain-containing protein
- PX domain-containing protein
- Ras-related protein Rab-4
- Vacuolar protein sorting-associated protein 26C
- TBC1 domain family member 5 homolog A
Sequence:
MMKKNKPTVAQTLSPEEEQAKFFEEAKNNVMIQGHHMKLSLDNSKLMDALKYASNIINELRTSLLSPKSYYALYLVAFDYLQYLNTYLYEEKHGKKMIELYEVVQHAGNVLPRLYLLITVGSVYIKTKQAPAKDVLKDLIEMCRGVQHPTRGLFLRHYLSEVTKDKLPDIDSSVENGTVMDSIDFIIQNFTETNKLWVRMQHQAPTKDRERRENERLELRLLVGKNLSRLAQLDGVDQKTYSEVVLPKVVEQIINCKDKIAQQYLMEILIQVFPDEFHLATLDIILQTCAQLQSGVDVKTIIASLIDRLANFATRNADLVPDNIKIFDIFFNNVKEIIQARPNMELQDILGLHVSLLNLTLKCYPTNKDNANEVLGLCQSIIVNKAKEDINKPTCVKQIIQLLQIPLDVFKNVLVVLKLSNYQPLISCLSYNNRKKVSLDIVNNTINNSTIIEEPEAVNNLLETIQTLIKDEQDQPDMDDIDKEDFQEEQNKVASLIHLFDSEDPEKLFKIYIIARGHFGKGGPHRIRHTLVPLVFCSLRFIRNFKQQVDSGVISLDENKWIAIGSKIFTFVSETIKALADIKLADLSFRLYLQALQTFDHCGLVSRVKELAIKALLIFQEDIADFKAQVMALQLLISTLNSLSIPNEEIYESLAAQTIKQASRLLLPQDQAKLISTCSHLFWVDNPSRQYQNPDSVLQALKKALSIISNESSPGLGTFVDILNECLFYCDKETDAVPIQFVSDLVELIRTTHVKEADPALPYLQNTIKYIQSQNYKGISI
Protein: Ubiquitin carboxyl-terminal hydrolase 17-like protein C (EC 3.4.19.12) (Deubiquitinating enzyme 2) (G5E8I7)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Important for preimplantation stage embryonic development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}.
Interaction partners:
Sequence:
MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKQVSIDMPEGRVHEVLDPEYQLKKSRRKKHKKKSPCTEDAGEPCKNREKRATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRINEILPQEQNHQKAGQSLRNTEGELDLPADAIVIHLLRSTENWGRDAPDKENQPWHNADRLLTSQDPVNTGQLCRQEGRRRSKKGKNKNKQGQRLLLVC
Protein: RING-type domain-containing protein (Q386N4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLCVLLLPAHYVFSFFSPLFFSYAEHERGWPLSARQGCLPMETEGVVQYRLLGSHPAASGRYHSFGFSGDVVTVTALTQDIVKQHQINLTKYKLEIQRVISAGNDSQEGQTPSTVADVYVPLQSNDVLHSYDRVIVNVSRRHYLDGVVDAAQDEKKAREERLQHVEGMLHEHEATTVTGTVSSSGPVGTGKRVEVRDPHKLKRVTAVSGKAFPVLPWLLNRTSVEGLTLPTPKKGICVLCELESFDEVMLECCRFYACASCLDLAKNMLTKETTCAVCGDVPGEKGSKGSLRPNAVAAVKRERSESCVGGASIAAPHVFSQFSSASGDGRGGSRATSISGTQSRVYRTTAMVSALERELNTNMAHILSLLDIPDPLTAEAKENRRMSNLFVRNLSK
Protein: Prefoldin subunit 1 (Q3SZE2)
Organism: Bos taurus (Bovine)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Interaction partners:
- Prefoldin subunit 2
- Prefoldin subunit 6
- Prefoldin subunit 3
- Prefoldin subunit 5
- Prefoldin subunit 4
- Prefoldin subunit 4
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
Sequence:
MAAPVDLELKKAFTELQAKVIDTQQKVKLADVQIEQLNRTKKHAHLTDTEIMTLVDETNMYEGVGRMFILQSKEAIHNQLLEKQKIAEEKIKELEQKKSYLERSVKEAEDNIREMLMARRAQ
Protein: Bifunctional protein TrpGD [Includes: Anthranilate synthase component 2 (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase, glutamine amidotransferase component); Anthranilate phosphoribosyltransferase (EC 2.4.2.18)] (P00904)
Organism: Escherichia coli (strain K12)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.
Interaction partners:
- Tryptophan biosynthesis protein TrpCF
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- Aminodeoxychorismate synthase component 1
- Anthranilate synthase component 1
- Bifunctional chorismate mutase/prephenate dehydratase
- Chorismate synthase
- T-protein
- Isochorismate synthase MenF
- Isochorismate synthase EntC
Sequence:
MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG
Protein: Two-component response regulator ARR22 (Q9M8Y4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histidine-containing phosphotransfer protein 3
- Histidine-containing phosphotransfer protein 5
- Histidine kinase 4
- Histidine kinase 3
- Histidine kinase 5
- Two-component response regulator ARR7
- Two-component response regulator ARR5
- Two-component response regulator ARR3
- Pseudo histidine-containing phosphotransfer protein 6
- Putative two-component response regulator ARR21
Sequence:
MATKSTGGTEKTKSIEVKKKLINVLIVDDDPLNRRLHEMIIKTIGGISQTAKNGEEAVILHRDGEASFDLILMDKEMPERDGVSTTKKLREMKVTSMIVGVTSVADQEEERKAFMEAGLNHCLEKPLTKAKIFPLISHLFDA