wanglab/gogpt-training-data huggingface dataset:
Protein: Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP) (P07897)
Organism: Rattus norvegicus (Rat)
Function: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Brevican core protein
- Receptor-type tyrosine-protein phosphatase zeta
- Tenascin-R
- Hyaluronan and proteoglycan link protein 1
- Cartilage oligomeric matrix protein
- Collagen alpha-1
- A disintegrin and metalloproteinase with thrombospondin motifs 4
- Fibulin-1
- Collagenase 3
- A disintegrin and metalloproteinase with thrombospondin motifs 5
Sequence:
MTTLLLVFVTLRVIAAVISEEVPDHDNSLSVSIPQPSPLKALLGTSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAIPSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRTVGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHANQTGYPDPSSRYDAICYTGEDFVDIPENFFGVGGEEDITIQTVTWPDLELPLPRNITEGEARGNVILTAKPIFDMSPTVSEPGEALTLAPEVGTTVFPEAGERTEKTTRPWGFPEEATRGPDSATAFASEDLVVRVTISPGAVEVPGQPRLPGGVVFHYRPGSTRYSLTFEEAQQACIRTGAAIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPSSETYDVYCYVDKLEGEVFFATQMEQFTFQEAQAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIVNPRPACGGDKPGVRTVYLYPNQTGLPDPLSKHHAFCFRGVSVVPSPGGTPTSPSDIEDWIVTRVEPGVDAVPLEPETTEVPYFTTEPEKQTEWEPAYTPVGTSPLPGIPPTWLPTVPAAEEHTESPSASQEPSASQVPSTSEEPYTPSLAVPSGTELPSSGDTSGAPDLSGDFTGSTDTSGRLDSSGEPSGGSESGLPSGDLDSSGLGPTVSSGLPVESGSASGDGEIPWSSTPTVDRLPSGGESLEGSASASGTGDLSGLPSGGEITETSASGTEEISGLPSGGDDLETSTSGIDGASVLPTGRGGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGESPETSASGVGDLSGLPSGGESLETSASGVEDVTQLPTERGGLETSASGIEDITVLPTGRENLETSASGVEDVSGLPSGKEGLETSASGIEDISVFPTEAEGLETSASGGYVSGIPSGEDGTETSTSGVEGVSGLPSGGEGLETSASGVEDLGLPTRDSLETSASGVDVTGYPSGREDTETSVPGVGDDLSGLPSGQEGLETSASGAEDLGGLPSGKEDLVGSASGALDFGKLPSGTLGSGQTPEASGLPSGFSGEYSGVDIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTASELEGRGTISVSGSGEESGPPLSELDSSADISGLPSGTELSGQTSGSLDVSGETSGFFDVSGQPFGSSGTGEGTSGIPEVSGQAVRSPDTTEISELSGLSSGQPDVSGEGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVLSGTTPGTPDLASGAMSGSGDSSGITFVDTSLIEVTPTTFREEEGLGSVELSGLPSGETDLSGTSGMVDVSGQSSGAIDSSGLISPTPEFSGLPSGVAEVSGEVSGVETGSSLSSGAFDGSGLVSGFPTVSLVDRTLVESITLAPTAQEAGEGPSSILEFSGAHSGTPDISGDLSGSLDQSTWQPGWTEASTEPPSSPYFSGDFSSTTDASGESITAPTGSGETSGLPEVTLITSELVEGVTEPTVSQELGHGPSMTYTPRLFEASGEASASGDLGGPVTIFPGSGVEASVPEGSSDPSAYPEAGVGVSAAPEASSQLSEFPDLHGITSASRETDLEMTTPGTEVSSNPWTFQEGTREGSAAPEVSGESSTTSDIDAGTSGVPFATPMTSGDRTEISGEWSDHTSEVNVTVSTTVPESRWAQSTQHPTETLQEIGSPNPSYSGEETQTAETAKSLTDTPTLASPEGSGETESTAADQEQCEEGWTKFQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQWIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPFTCKKGTVACGEPPAVEHARTLGQKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSADWEEPRITCTDPNTYKHRLQKRTMRPTRRSRPSMAH
Protein: Transcription factor fil1 (GATA zinc finger domain-containing protein C1393.08) (GCN four induction-like protein) (General control transcription factor fil1) (O94720)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Activates genes required for amino acid biosynthesis and acts as a master transcriptional regulator during amino acid starvation. Binds variations of the DNA sequence 5'-GAT[AC]GC-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000305|PubMed:29432178}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C2H10.01
- Uncharacterized transcriptional regulatory protein C530.11c
- Serine/threonine-protein kinase oca2
- Meiosis-specific transcription factor mei4
Sequence:
MNYNDTTEFCFPFGQPSFPTSAMTEGSFDGQFSEFDPTFTSPADTALSDIANLPIDLHKDALFANAPGKGDVDFDSVSMLQLLSDYPLAFNSTENNQKLQTNPSARWSLLDSMDFDNQRQCSDLESAQLGDSGLLKSTILSNSHIDIAALSSSKTSEPTPPFSYVQTPCIPTPSSALIDTPFPGALDSEFGFDESQAPLFPASDGDCQRAFASISYPTNYGCKLSNLGFMSPQSPVKRELNDSTSPSKLSESSSSLTGSSSALLSQSEFLGSVPSLSDSIATVDPFFSFESFETDEKARSLLMDASLKLPQFSTPNLSSNSSSLSLKSTLAEGMKGSTPLAAVKTEKASKAARVMKQKKHREHVCFNCGVTETPLWRRTSDKLNFLCNACGLYNKQYGVMRPLSPRNKGSSKALENLVCANCSSTKTSLWRKDRHGQTVCNACGLYARLHGHNRPIGLKKNKITRRRRGKGPGGEDGMSDEVKSEFPVLSKSVTMAEILSSKGLESPQLTNSVSVSKMPNTDADVSLEHAKISFDSLDNSVIVKKEEEIENKFSVSC
Protein: Cytidine deaminase (CDA) (EC 3.5.4.5) (Cytidine aminohydrolase) (Q06549)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Interaction partners:
- Uridine nucleosidase
- Cytosine deaminase
- Uridine kinase
- Deoxycytidylate deaminase
- Putative uridine kinase DAS2
- tRNA-specific adenosine deaminase subunit TAD3
- Purine nucleoside phosphorylase
- tRNA-specific adenosine deaminase subunit TAD2
- Bifunctional protein RIB2
- Bifunctional purine biosynthesis protein ADE16
Sequence:
MKVGGIEDRQLEALKRAALKACELSYSPYSHFRVGCSILTNNDVIFTGANVENASYSNCICAERSAMIQVLMAGHRSGWKCMVICGDSEDQCVSPCGVCRQFINEFVVKDFPIVMLNSTGSRSKVMTMGELLPMAFGPSHLN
Protein: Gartenzwerg, isoform C (A0A0B4K7N0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALPGNGIYVVRGEMATLMTAMRRGTRWNATAYVDDENDSLLKLFIDLKHELNRIEDLRQIEPQVFLAPFLEVIRTADATGPLTSLALASVNKLLSYGLIDPTSPNLADIVERIADAVTHARFMGTDQSSDGVTFMRVIEVLHTLIRSPEGAAVSNVSMCEVMLSCFKISFEPRLSELLRRSAEKSLKDMVLLFFMRLPQFAEERSDTMLQKRFTIGDAASGATQEKLKRKTVAQAQTAPRKSSAVEEPPQTPQSANLTVPGHLKAPILATTPASPAGNILDMQGKITQTPTTTASTGEDETTVPETPVIQVESTESEPLLDGETGEATSTLAEANSSEYINSVGVRFTQQSTDHDVTSLSPYGLPFIQELFRFLIILCNPLDKQNSDSMMHTGLSLLTVAFEVAADNIGKYEGLLELVKDDLCRNLISLLSSERLSIFAADLQLCFLLFESLRGHLKFQLEAYLRKLSEIIASDNPKTPYEMRELALDNLLQLWRIPGFVTELYINYDCDLYCTDMFESLTNLLSKYTLSATNAVYSTHIISMDTLLSVIDSIERNCAASKNSSNNRESLPEAAPATGGSRHSRHNSGLEGIVIDSGNSVAAEEKVENIASFINASSHRLRLQSGGEGVGITSEQLAKVKQKKRLLSQGTERFNQRPEKGIQYLQEHGILNAELDPMQVALFLRENPGLDKKMIGEYISKKKNVDSKILINFVDSFDFTGLRVDQALRLYLETFRLPGEAPLIFLVLEHFSDHWHKQNQDPFANVDAAFRLAYAIIMLNMDQHNSNAKRLNVPMTLEDFTKNLRGLNGGEDFDQEMLAQVFNAIKNEEIVMPAEQTGLVRENYQWKVLLRRGDTHDGHFHYVHDASYDVEIFNIVWGASLSALSFMFDKSTETGYQRTLAGFSKSAAISAHYNLHSDFDALVLTLCKFTTLLSSVEQHEPAPANNETQQAVNFGLNGKAQAAMRTVFLLVHDYGDCLRESWKHILDLYLQLFRLKLLPKSLIEVEDFCEANGKAMLILEKPREKQESGLFSSLYSFISSEGQREPTYEEQDFIKLGRKCIKECQLDQMLQESKFVQLESLQELLKCVLALLKAPQGHKSIGLPYAEDQTVFWMEFLVKIVVHNRDRMIPLWPAVRDQMYLLLMGSASCGYDYLLNRCIVAVLKLAIYLMRNEELCPIVLQSLKMLLMLKPALLLRISKQISIGIYELLKTSAQNIHSEQDWQIIFNLLECVGAGAVPPNYDDAQLPLPPNGSAKSDGAISGEEDATAVPERGYTSDSEITKASAAPAVSSPSAENWILVNNKDSELTTASRPQSPPSLSAPPVNTLVYNCQLLDHAPFALFKCWDSLAFIVRSVAHITPYNFEACVRCIRIFVEACRDGGIRQRRKLESAAKQKSSKKRSERKPGMASSASSSNLTLLTGDPSDNQINGNAAEQEDLAQRYEQLSIQLLDLMYTLYTRTAQIFRWWAEEGCTVPQSAALWSPGWCPLLQGIARLAMDRRREVRTHAISCLQQRALLVHDLQTLSGTEWCSCFHQVLFPLLNELLPESNAAGQLDAALLEESRIRTATIMSKVFLQHLTTLIELGNAFNELWLDILDYIERFMKVGSDTLSEQMQEILKNMLLVMHSVRVFHNQDGSLQQALWELTWRRIGEFLPNLKEELFHDEADSITPAVSLDYTQIRFAHSTGTTDYSLSLPLYGYSPKISSISASKCDTLPATQRKKPWAKLRSKLKLLKKVGKKN
Protein: IP11764p (Q9VW98)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDNELSYAVTRVLLELYQRHGIPMVSQPMAGVGENAYGQVLRVSWPTIVDAATVVVKMAPRNEARRSHMHVVDYYAREVFMYQKVFPVFRALSPDRNTFTVAPALQANDLKAPDEFLIFEDLSESGFRPNSRCIMPTYDIVVCSLKALAELHACSFILQQTDPLQFKQLVEFVEKDNLFTSDIEEVTIEFGKAQLRKARIILKESDGDQVAAVQEVLQLCENQLKSLALYCVDGKAQAPHAVICHGDFWNNNILYRHEPNSDQPVEAKLIDFQMSRYAPPVLDIVHYLFACTEKRLRDEHFPDFMDAYYNTMDQKLKSCNLSLEGIYPRSVFNRQLQQYGVYGLIMGAFSLPFFISNANEVIDIDTVSEAIQSISTSSDEPKYKELIEEYEMLNARTLPIFKRRITGIVEDLIKYNMTEPLFKMDSEQC
Protein: Microtubule associated serine/threonine kinase like (A0A087WUU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ESDEALGPTMMSWNAVEKLCAKSANAIETKGFNKKDLELALSPIHNSSALPTTGRSCVNLAKKCFSGEVSWEAVELDVNNINMDTDTSQLGFHQSNQWAVDSGGISEEHLGKRSLKRNFELVDSSPCKKIIQNKKTCVEYKHNEMTNCYTNQNTGLTVEVQDLKLSVHKSQQNDCANKENIVNSFTDKQQTPEKLPIPMIAKNLMCELDEDCEKNSKRDYLSSSFLCSDDDRASKNISMNSDSSFPGISIMESPLESQPLDSDRSIKESSFEESNIEDPLIVTPDCQEKTSPKGVENPAVQESNQKMLGPPLEVLKTLASKRNAVAFRSFNSHINASNNSEPSRMNMTSLDAMDISCAYSGSYPMAITPTQKRRSCMPHQQTPNQIKSGTPYRTPKSVRRGVAPVDDGRILGTPDYLAPELLLGRAHELKRHPLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNTAQHLTVSGFSL
Protein: ADAM metallopeptidase domain 28 (A0A8I5Y766)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQQWRLLVVWFLLSPVPASAIKELPKAKNYEVVYPIRLHLLHKRETKEPEPKETFETELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYYQGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAHALFKDDPKEDQENSNCGVDDALWLQGLHQDVVLPATRLIKLNDGMVQEPKKYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGNDLLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSPLPSDIISTPVCGNQLLEMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRFRVNGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQNEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSGDLPWKGLTIAFLTCKLFDPEDINQGVDMVANGTKCGNNKVCINAECVDMEKTYKSANCSSKCKGHAVCDHELQCQCKEGWAPPDCEDSATVFRVSIMVGVLFPLAAIFVVIAIVIHHQSARRKQRRVQRLPPIKDAKLHKQKCRPQKVKDIQPQELITKPNFPPPPIPVSWML
Protein: Very Early Transcript (O61775)
Organism: Caenorhabditis elegans
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase sig-7
- Forkhead box protein fkh-4
- SKN-1 Dependent Zygotic transcript
- BTB domain-containing protein
- Very Early Transcript
Sequence:
MITGYCGFCKTDYVGVDHGNKCYYKYYYDYDLEEFMPLKCLDCQPKITEKNLFPQEGTFWDPKMQKAVMPFHNVVTNWIEYYIYDIKEKCLEQIEPVVPPVSYDPTPVGDRICIVDSKTETILIRRHPEHGHVCTQQFINGEYQDVPNTKVNTLQMKELKRYGQCRSLTHYLRLPILNTSYCFKSDQYIVRVPGRNNEKPKEFYFDREFSCFMPSLLTVPEDILYPEYSVWSESLKKHVTFTAVWNGRSEIIEQYVYNCEQGQFEQVHVPELVYDPNHEVPMNILFIQMSKDRPIVIMKDEDGNFVKQEYDSLIDCFVAISPKDAKILPREYDEKLIYGKYGMAIYSIKPEPVKKVGGPFGGVKGGSFEGLPERPENGFSFETEKEQSASTGSESHDEQETVIESESITDFLSRILGEDWLTPKPLSTTYQKPLKKSSVHDESADEIDLILAKKSKRTAVPTISKSDEVENVDPPKEYGNLEVDHEAMLHQRPLRKVAVVQRESESAYESEQGSDGETSEESFLERASLFDEYDRMIEILAEEYDTPDEQTPCTKFEEYPDESDEESDQSDDESDFSYMAAPSESEDSYDKLVENFSQDYQKLVRKMSFTKNGDQQRPLKKVGGPFGGVQGGSFGGFAETKGNGFSFEKTAEVESSKDQPMKKFNFDVQDSDQSGLKSKVVSDSYEYDKVMKTLQQEYDQLRNILSKYQKPLKKVGGPFGGVKGGSFEGLPQRPANGFSFETEKVQLDVLSDSEESDEQQTIIATIAKTSSILYEEFMKLIEFKF
Protein: Zinc metalloproteinase-disintegrin-like proatherocytin (SVMP) (EC 3.4.24.-) (P85005)
Organism: Proatheris superciliaris (Lowland swamp viper)
Function: Stimulates platelet aggregation through activation of PAR-1 (F2R).
Subcellular location: Secreted {ECO:0000269|PubMed:16112700}.
Interaction partners:
Sequence:
GNYYGYCRVHLNTAY
Protein: Putative F-box/LRR-repeat protein At5g15620 (Q9LF20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDRFSNLPDDVIYHIVSFLSAKEATCLKFVSKNFQNLVTIKRNVVFHHWESFKNFVDGLLAEPASYRIKRFSLKLVSMDFAQYNIVNDCLCNVLKRGVLDLELDINVKEDYILPSDVFTCKTVVRLKLGCGFVIDILPKNALLPALKTLILDSVRFYASDGCAFTRLLSASPVLEELVIDRLNWEHWKGSRFVSSPTLKRLTLRRKEWEPEPETWTDFESVSFDTPSLAYLKYKDVIPYGYPIVNLNSIVEARLTLPREVEYDYWLNRSADPSNLIRGLKNVEILSIKVLHTMDLLFYNFKEAVPVFENLIHLSVTSEADFCWDPLQILLEKSPNLKTLTIEGPLHYNFYEKLDLEAVCECLLGYSFLLSCPIKVLKITEFVGDIGEIVQMKHVLGKLPCLELLEVHVQARRDDKKLQIMADLLMLPRTSSKCKVKVHFS
Protein: Protein EMSY-LIKE 2 (AtEML2) (Q9FG29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the regulation of chromatin states (Probable). Contributes to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1. Regulates negatively EDM2-dependent floral transition.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9C7C4}.
Interaction partners:
- Protein ENHANCED DOWNY MILDEW 2
- Tubulin-folding cofactor A
- Coilin
Sequence:
MEAQIHILEQEAYSAVLRAFQAQADEFSWDKATVMTNLRKELRISDDENRQLLNNVHNDDLIKRIRDSRPRGGNQVVRHQSLDVHPSPTFSASRKKQKTFQSYPSIGSTRSKSFNNRVVSANEPAEALIGRKVWTKWPEDNSFYEAVVTQYNANEGRHALVYDINTVNETWEWVDLNEIPTKDIRWDGEEDGVTLNVGHGGGTTRGNRRTLSHGGRGRGPRTQPRREHLATENGGGRKFFGEIELFNTDSLVKEVERVFDSNLPDPHELDKAKKLLKEHEQALIAAIARLTDASDYESDGEEPYSHELPMLLG
Protein: Serine protease FAM111A (EC 3.4.21.-) (Q96PZ2)
Organism: Homo sapiens (Human)
Function: Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors. Required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:37607234}. Chromosome {ECO:0000269|PubMed:24561620}. Cytoplasm {ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:37607234}. Note=Mainly localizes to nucleus: colocalizes with PCNA on replication sites. {ECO:0000269|PubMed:24561620}.
Interaction partners:
- Tubulin-specific chaperone E
- Tubulin-specific chaperone E
Sequence:
MSCKKQRSRKHSVNEKCNMKIEHYFSPVSKEQQNNCSTSLMRMESRGDPRATTNTQAQRFHSPKKNPEDQTMPQNRTIYVTLKVNHRRNQDMKLKLTHSENSSLYMALNTLQAVRKEIETHQGQEMLVRGTEGIKEYINLGMPLSCFPEGGQVVITFSQSKSKQKEDNHIFGRQDKASTECVKFYIHAIGIGKCKRRIVKCGKLHKKGRKLCVYAFKGETIKDALCKDGRFLSFLENDDWKLIENNDTILESTQPVDELEGRYFQVEVEKRMVPSAAASQNPESEKRNTCVLREQIVAQYPSLKRESEKIIENFKKKMKVKNGETLFELHRTTFGKVTKNSSSIKVVKLLVRLSDSVGYLFWDSATTGYATCFVFKGLFILTCRHVIDSIVGDGIEPSKWATIIGQCVRVTFGYEELKDKETNYFFVEPWFEIHNEELDYAVLKLKENGQQVPMELYNGITPVPLSGLIHIIGHPYGEKKQIDACAVIPQGQRAKKCQERVQSKKAESPEYVHMYTQRSFQKIVHNPDVITYDTEFFFGASGSPVFDSKGSLVAMHAAGFAYTYQNETRSIIEFGSTMESILLDIKQRHKPWYEEVFVNQQDVEMMSDEDL
Protein: Nuclear RNA export factor 1/2 (Q386S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NTF2-related export protein
- RNA-binding protein, putative
- Poly
- Nuclear cap-binding protein subunit 2
- Nucleoporin
- Nucleoporin NSP1-like C-terminal domain-containing protein
- RRM domain-containing protein
- Nucleoporin
- Uncharacterized protein
- Nuclear pore protein
Sequence:
MSRPYTKGGGPNRADSRRRRKGDYDRDVLTDRGGHNSSWNAKPDRSRRGSRGGSGPPGKGTGGSDNQVPQSTMMTTLLDLLFQKSSSVIFNRESGMLNLSNFSQSQDLTDVRKSVDFNNVTFCRSLVSVIKSHMGSMLRAVAVNDNKITKLSVFLSALVEADLHIGITALSATGNTIDDLSFIGPLKRFVNLGELVLKENPVTRREDYNSSVIQKVKSLMMLDDKVINRAPLRLPNPIPSSLSQLQFQVLYFLEADVFSAAAEGKWDTLTGVYAKNALFSVSRSEEPIACRIPFDAKHKSDTLNPTQRKVMTDDFVFLRKNVPWRNLHVEIHSLRSIACGQTKAVKAINILGGGERKFFSVSHELNGNANVVFLSDNMAVPTCVLTIHGRLFWHWSPIDGGEKIFARDDAPFVSCFFHRTMSLTLDPNGTTWSVHNDMMFLRPDRLLRQESGEKALPMFFANDPMRIEEMRRRYLPQAKTDVMKTIVEAVSSDADVVGFIQNCLAKLPPDQLEIALSASDVMANLLGG
Protein: SCF ubiquitin ligase complex subunit (A0A1D8PP13)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- E3 ubiquitin ligase complex SCF subunit
- Cullin
- SCF ubiquitin ligase complex subunit
- Protein phosphatase PP2A regulatory subunit B
- Ubiquitin-binding SDF ubiquitin ligase complex subunit
- Cullin
- SCF ubiquitin ligase complex subunit
- Hypha-specific G1 cyclin-related protein 1
- Serine/threonine-protein phosphatase
- Rgt1p
Sequence:
MSSPTSLDDLSNMPETGNTIKTLHELKQESSPDSNNEMNIDGEMSNDNSNHSNSNHKMHTYDGDFVMDNEYNDYEELRKSLVNKRRLSSIKRPHGPFLDHNNQIDKRSLLRLPTEILLQIFHYLERRDWYSLLTTCSEIADLIIEMLWFRPHMQNDSAFKKIKEVMEINKSVTHWDYRQFIKRLNLSFMTKLVDDELLSLFIGCPRLERLTLVNCAKLTRYPITQVLNGCERLQSIDLTGVTDIHDDIINALANNCPRLQGLYAPGCGNVSEEAIIKLLRSCPMLKRVKFNSSTNITDESILVMYENCKSLVEIDLHGCENVTDKYLKSIFLDLTQLREFRISNAPGITDKLFESIPEGHILEKLRIIDITGCNAITDRLVEKLVSCAPRLRNVVLSKCMQITDASLRALSQLGRSLHYIHLGHCGLITDYGVAALVRYCHRIQYIDLACCSQLTDWTLVELANLPKLRRIGLVKCSMITDLGILELVRRRGEQDCLERVHLSYCTNLTIGPIYLLLKNCPKLTHLSLTGISSFLRREITQYCREPPSDFNEHQKSLFCVFSGHGVNQLRNYLNQVVEERTYQIDQGDIHTLFNERRRRFLNGDIDMDEEEMNIWERRRGLGVTADLGHPDMAEINREIFRELNEGNMGPDEMREHFQRLIRNHHQQRLLEHQNRLNQQLVQQRQQQQQQEPQLEQENLQNRGQIETQAPDQLPNEGQLRLQPPLQQQRAQNTIINNPQNAPQIEQPAVFPNGENQTLPLVLNEDEDVDMEPVDLFPRNT
Protein: Small ribosomal subunit protein uS13m (Ribosomal protein S13, mitochondrial) (Q8HCP0)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Small ribosomal subunit protein uS9
- 40S ribosomal protein S29, putative, expressed
- Os10g0411700 protein
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS14c
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS19
- 40S ribosomal protein S15, putative, expressed
- Small ribosomal subunit protein uS2c
- 40S ribosomal protein S6
Sequence:
MLYILGARLLPDEQVRIALTKMDGIGPKKAIQLCYRLGISGNIKMNELTKYQIDQIEQMIAQDHVVHWELKRGERADIERLISISCYRGIRHQDGLPLRGQRTHTNARTARKLIRK
Protein: Fondue, isoform D (M9PDP3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKLLILALCLGVVCGDFQQSLGRTKRDSFHSRTHGQAVEQARKNAGYGGGYSGSFGAGVDGASAQVDDSALGKLESSYDSVGATESAEGASAGGLGGAVETLGGSAGTNTIGAGVGSSFGSNFASGFGGQNAASFGAQNAAGFGAQNAASFGAQNAASFGSSFSSNAAFQTSSASNFGSTAAHQVGSNVEFADNANAGNKVDFGGVNAVDSSAQLLSGVQTVQSVPTSEYYRHEKIVSTPQQVVYTIPGGSQRYVHHEERIVEQPTQVTQTVPVQTAHYYQRKVTTTASAPQLVQPVASSRLTYGSNAASTFGSNAASNFGSNAATNFGSNAATNFGSNAAFNSQFGSSYGQNFQQNSQLSQLLSQTQQAARQQAALQAASANQVQAGSGYAAGSQGGFNSGYNSAFNSGSQFGFNSASSLNSASSLNSASTGNSAALLSGSLLGGSQGSLLSGQVGGQQSLLSGSLLSGQQNLGLGLNAAQTGQVVGASSVGAGLSAGAGNLGSGYRTKQWEKQSKWSSQNSYDSNGHVNNYKDLVTGESESVDINGKRAGYHAVTASVDDNGKIGTHSVHS
Protein: Uncharacterized protein PB1E7.11c (Q9C0Z8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C106.19
- Aspartate aminotransferase, mitochondrial
- Probable translation initiation factor
- Pentatricopeptide repeat-containing protein 6
- Pentatricopeptide repeat-containing protein 7
- Ribonuclease Z 2, mitochondrial
- NADH kinase pos5, mitochondrial
- Pentatricopeptide repeat-containing protein 2
- Translation initiation factor IF-2, mitochondrial
- Mitochondrial inner membrane m-AAA protease component yta12
Sequence:
MTAVPKFYRAALSDKYKRIVLDAMSRGYRPSEGIWFRVRTYFPVSYPADIKSEALPSRYFQLKAFPYYNAEERLKEWIVLAKVRPEIPLPPAAPIPMKKASNTEPVEKEISSFFSEEGATKENEDFINEKEEEEDLSFSINAAHTFSNIGTWYLARANEVAEFKHQQKKIVAINKGRFPKSLLLQYVPSNISSERLFKTLKRHGLVQGVMEMNTKPLKTSKTTPTKKMLSTTDTKDWLVITPVPNKLTRLLHKSQWDLIEKLSFPLRLSDYKKITKKENIGLSSRDEMGDPLLFAHSYFELTPENKTSAPKINVKSEGK
Protein: Vacuolar transporter chaperone complex subunit 2 (SPX-dependent polyphosphate polymerase VTC subunit 2) (Vacuolar membrane polyphosphate polymerase accessory subunit 2) (PolyP polymerase) (O13718)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P43585}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vacuolar transporter chaperone complex subunit 4
- Glycerophosphocholine phosphodiesterase gde1
- Vacuolar transporter chaperone complex subunit 1
- Uncharacterized RING finger protein C6B12.07c
- Putative inorganic phosphate transporter C8E4.01c
- Serine O-succinyltransferase
- Uncharacterized transporter C3B8.04c
- T-complex protein 1 subunit alpha
- Putative inorganic phosphate transporter C23D3.12
- Probable T-complex protein 1 subunit eta
Sequence:
MRFSDSIEAGIYEPWRDKYMNYPELKHLLKTEEEAPSWGENDESKFVSVMDAQLEKVYAFHLEILKELNESVDWVKSKVSASQEPDGPPISKEEAIKLLERLDSCTETVKKLEKYTRLNLTGFFKIVKKHDKLYPGYSLRPVFQVRLRACPLGSVQFNPLLAEIFSLYNTLRDGLSAPSNSVQVKPKHEHNVDYNSSMYRRRTFRFWVHPDNVMEVKTYIMRHLPVLYYSGKQGFDKDQNGVSGILDPISTCLYLDNSNFDLYSQNLERSEQAYSLRLHWYGKLTPKTDIIVERMVRQGSTLSHSEDRFTIREKKVRELLSGRYDFRKVEDDHSTTASDQKKKLIEDVEQLIVDNHLQPVLRSVYTRTAFQIPGDDEVRINLDSDWVMIREDSLDIERPCRDPEDWHRHDIDDADFPYKHLRKGEYSRFPYSVLEIRECVRYDEDEPLWISELRNSHLISEIDGFSKYEHGVAILFEKYVSLLPMWVFSMDQDIRKDLQEVYSHPEGSAGSRNVYIKRRNQRVLKQNMTPEPSQPSPLVNRLKANEMHPVSEEPEDNREVYRNEHGDHFNFRSIPGLLKPSTYGSFKHHGKTFVTPPHIKKPEIPLRVSGPIKVEAKVWLANERTFLKWLHVVVLLGSLALALYNSAGERLGQAFGVVYTLLAIFIGFYAWKLHAKRSQMIKSRSPAPMTDYWGPLIVGTALAISLIVNMSFALKDAVYQNLIEPDRLLVKLFT
Protein: Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) (Q7K569)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- glycerol kinase
- glycerol kinase
- BcDNA.GH07066
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 4, isoform D
- Phospholipid/glycerol acyltransferase domain-containing protein
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MTSRMFKFGVTAASACVGSVLASYTLDRWNTPHVVNNATVPPKRKRTLPPRADQIKSLMSGEEFDVLIIGGGATGAGCALDSVTRGLKTALVELDDFASGTSSRSTKLIHGGVRYLQKAILGLDLEQYRMVKEALAERATMLESAPHLTHPLPIMLPVYTWWQVPYYWVGIKAYDLVAGDRNVKSSYYLSKKDALELFPMLKKDKLCGAIVYYDGQQDDARMCLAVALTAARHGATVCNHVEVKELLKKDDGTGKQVLCGAKVKDHISGKEFTVKAKCIVNAAGPFTDSIRKMDNPTVKSICCPSSGVHIVLPGYYSPDQMGLLDPSTSDGRVIFFLPWQRQTIAGTTDLPCEITHNPTPTEDEIQFILNEIKNYLNADVEVRRGDVLSAWSGIRPLVSDPNKDDTQSLARNHIVHVSPSNLITIAGGKWTTYRAMAEHTIDAAIKACNLKPERAEAVTSYLKIEGGQGWTPTMYIRLVQDFGLECEVAQHLAKSYGDRAFAVSKMASLTGKRWPIIGNRIHPEFPYIDAEIRYGVREYACTAVDMIARRLRLAFLNVQAAQEALPVIVDIMGEELGWSKDEKERQIKHATEFLANEMGHSVNRTSKERIPIKLSKEEIQTYIKRFQLIDKDKKGYVSINDIRRALKSFGDGDVSGEQLHEILREIDTNMNGQVELDEYLQMMSAIKTGDVAYSRFARMAELEEQKHEAANLKQISVDRSGGGL
Protein: Probable methyltransferase PMT10 (EC 2.1.1.-) (Q94KE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein.
Interaction partners:
- Histone H4
Sequence:
MKLSDVGLDVVKTPRLVKLIAFAFLSISTIFLFNHFSDSFSYPSLPFPISSSSNVTEAIQTNITSVAAVAPSPPPRPRLKISPPPLPPTVVRTGIINENGAMSDSFEIGGFDPDSIDELKSATGNSSVEEKESPEVGFQIEKLKLCDKTKIDYIPCLDNEEEIKRLNNTDRGENYERHCPKQSLDCLIPPPDGYKKPIQWPQSRDKIWFNNVPHTRLVEDKGGQNWIRREKDKFVFPGGGTQFIHGADQYLDQISQMIPDITFGSRTRVALDIGCGVASFGAFLMQRNTTTLSVAPKDVHENQIQFALERGVPAMVAVFATRRLLYPSQSFEMIHCSRCRINWTRDDGILLLEVNRMLRAGGYFVWAAQPVYKHEDNLQEQWKEMLDLTNRICWELIKKEGYIAVWRKPLNNSCYVSREAGTKPPLCRPDDDPDDVWYVDMKPCITRLPDNGYGANVSTWPARLHDPPERLQSIQMDAYISRKEIMKAESRFWLEVVESYVRVFRWKEFKLRNVLDMRAGFGGFAAALNDLGLDCWVMNIVPVSGFNTLPVIYDRGLQGAMHDWCEPFDTYPRTYDLIHAAFLFSVEKKRCNITNIMLEMDRMLRPGGHVYIRDSLSLMDQLQQVAKAIGWTAGVHDTGEGPHASVRILICDKRI
Protein: Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (Q6FLR5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.
Interaction partners:
- Methylthioribulose-1-phosphate dehydratase
- Acireductone dioxygenase-requiring))
- Methylthioribose-1-phosphate isomerase
Sequence:
MSPDPKYSAYLLDIEGTLCPLSFVKDTLYPFFVLHVQRIVYENFNEEHPKDEFIAEQLAKYDIKEEGQAGKNKLVEHLLDLVANDTKDSTLKALQGHVWEVGYNSGELEVPLYPDVIDFLVRNDGRGDDKVPVYIYSSGSIHAQKLLFGHVKNSGNSHAKIAGNWDLNRFIDGYFDINTAGKKTESNSYKKILDEIKMTDKPHDVLFLSDNAKELDAAKECGISVGLAMRAGNVTVPNAIDYKQYFQFTKL