wanglab/gogpt-training-data huggingface dataset:
Protein: Angiopoietin-related protein 1 (Angiopoietin-3) (ANG-3) (Angiopoietin-like protein 1) (O95841)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000269|PubMed:10025962}.
Interaction partners:
- Angiopoietin-1 receptor
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Angiopoietin-like protein 8
- Tyrosine-protein kinase receptor Tie-1
Sequence:
MKTFTWTLGVLFFLLVDTGHCRGGQFKIKKINQRRYPRATDGKEEAKKCAYTFLVPEQRITGPICVNTKGQDASTIKDMITRMDLENLKDVLSRQKREIDVLQLVVDVDGNIVNEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNSLELSQLENKILNVTTEMLKMATRYRELEVKYASLTDLVNNQSVMITLLEEQCLRIFSRQDTHVSPPLVQVVPQHIPNSQQYTPGLLGGNEIQRDPGYPRDLMPPPDLATSPTKSPFKIPPVTFINEGPFKDCQQAKEAGHSVSGIYMIKPENSNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLENIYMLSNQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGDSMMWHNGKQFTTLDRDKDMYAGNCAHFHKGGWWYNACAHSNLNGVWYRGGHYRSKHQDGIFWAEYRGGSYSLRAVQMMIKPID
Protein: NACHT, LRR and PYD domains-containing protein 4 (Cancer/testis antigen 58) (CT58) (PAAD and NACHT-containing protein 2) (PAN2) (PYRIN and NACHT-containing protein 2) (PYRIN-containing APAF1-like protein 4) (PYPAF4) (Ribonuclease inhibitor 2) (Q96MN2)
Organism: Homo sapiens (Human)
Function: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. Acts as a negative regulator of the type I interferon signaling pathway by serving as an adapter to promote DTX4-mediated ubiquitination of activated TBK1, and its subsequent degradation. Suppresses NF-kappaB induction by the cytokines TNFA and IL1B, suggesting that it operates at a point of convergence in these two cytokine signaling pathways.
Interaction partners:
- E3 ubiquitin-protein ligase DTX4
- Beclin-1
- Apoptosis-associated speck-like protein containing a CARD
- Caspase-1
- Baculoviral IAP repeat-containing protein 1
- Serine/threonine-protein kinase TBK1
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 3
- NACHT, LRR and PYD domains-containing protein 1
- Pyrin
Sequence:
MAASFFSDFGLMWYLEELKKEEFRKFKEHLKQMTLQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLCMKVMRERTGYTKTYQAHAKQKFSRLWSSKSVTEIHLYFEEEVKQEECDHLDRLFAPKEAGKQPRTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDRFLYTFYFCCRELRELPPTSLADLISREWPDPAAPITEIVSQPERLLFVIDSFEELQGGLNEPDSDLCGDLMEKRPVQVLLSSLLRKKMLPEASLLIAIKPVCPKELRDQVTISEIYQPRGFNESDRLVYFCCFFKDPKRAMEAFNLVRESEQLFSICQIPLLCWILCTSLKQEMQKGKDLALTCQSTTSVYSSFVFNLFTPEGAEGPTPQTQHQLKALCSLAAEGMWTDTFEFCEDDLRRNGVVDADIPALLGTKILLKYGERESSYVFLHVCIQEFCAALFYLLKSHLDHPHPAVRCVQELLVANFEKARRAHWIFLGCFLTGLLNKKEQEKLDAFFGFQLSQEIKQQIHQCLKSLGERGNPQGQVDSLAIFYCLFEMQDPAFVKQAVNLLQEANFHIIDNVDLVVSAYCLKYCSSLRKLCFSVQNVFKKEDEHSSTSDYSLICWHHICSVLTTSGHLRELQVQDSTLSESTFVTWCNQLRHPSCRLQKLGINNVSFSGQSVLLFEVLFYQPDLKYLSFTLTKLSRDDIRSLCDALNYPAGNVKELALVNCHLSPIDCEVLAGLLTNNKKLTYLNVSCNQLDTGVPLLCEALCSPDTVLVYLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHPDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDCRLEILGLEECGLTSTCCKDLASVLTCSKTLQQLNLTLNTLDHTGVVVLCEALRHPECALQVLGLRKTDFDEETQALLTAEEERNPNLTITDDCDTITRVEI
Protein: Ubiquitin carboxyl-terminal hydrolase 19 (EC 3.4.19.12) (Deubiquitinating enzyme 19) (Ubiquitin thioesterase 19) (Ubiquitin-specific-processing protease 19) (Q6J1Y9)
Organism: Rattus norvegicus (Rat)
Function: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19015242}; Single-pass membrane protein {ECO:0000269|PubMed:19015242}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF123
- E3 ubiquitin-protein ligase SIAH1
- Hypoxia-inducible factor 1-alpha
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin carboxyl-terminal hydrolase
- E3 ubiquitin-protein ligase SIAH2
Sequence:
MSAGTSATGPRRGPPGLEEATSKKKQKDRANQESKDGDPRRVSMPRKEPTKDELLLDWRQSSDKVVVKLRVGTGPICLEEVDAAFTDTDCVVRLPDGRQWGGVFFAKIQSSCTKVQTRKGGLLQLALPKKVPLLTWPSLLKKPLGTQELVPGLRCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGASPGAQAGPSAKRAVHLCRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEQLHVPPVNPQTSLLGSEKNLALLTVEKTVSPRSDSVSPVMIRNRDPEKDDHFKEEMAVGADPAALADEPESMVNLAFVKNDSYEKGPDSVVVHVYVKESRRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRVGGAKVAVPTGPTPLDSTPPGGGPLPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVTPKPEPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIYYFAREPHSKPIKFLVSVSKENSSASEVLESLSQSVHVKPESLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRMWPPADRGPVPSTSGISSEMLASGPMEGCSLLAGERVSRPEAAVPGYQHSRESVSAHTPQFFIYKIDASSREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPSDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAAHAEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTSDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR
Protein: Hydroxysteroid dehydrogenase-like protein 2 (EC 1.-.-.-) (Q2TPA8)
Organism: Mus musculus (Mouse)
Function: Has apparently no steroid dehydrogenase activity.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q6YN16}. Mitochondrion {ECO:0000269|PubMed:38820148}.
Interaction partners:
- Catalase
- Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- Enoyl-CoA delta isomerase 2
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Delta
- Acyl-CoA dehydrogenase family member 11
- Trifunctional enzyme subunit beta, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Sterol carrier protein 2
Sequence:
MLPNTGKLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTTQKHPKLLGTIYTAAEEIEAAGGTALPCVVDVRDEQQINSAVEKAVEKFGGIDILVNNASAISLTNTLDTPTKRVDLMMNVNTRGTYLTSKACIPFLKKSKVGHILNLSPPLNLNPLWFKQHCAYTIAKYGMSMCVLGMAEEFRGEIAVNALWPRTAIHTAAMDMLGGSGVENQCRKVDIIADAAYSIFKRPKSFTGNFIIDENILKEEGIKNFDVYAIAPGHPLLPDFFLDEHPDAVMEEKESNDSVPEVKEEKLQLQEESQLQKQPQLQEQPQLQEKPQLQEKPQLQEQPQLQEKPQLQEQPQQREQPQLQQQPRPRQQPQPFVQSMLPQKPHFGAVEETFRIVKDSLSDEVVRATQAVYQFELSGEDGGTWFLDLKSKGGKVGHGEPSDRADVVMSMATDDFVKMFSGKLKPTMAFMSGKLKIKGNIALAIKLEKLMTQMNSRL
Protein: Biotin--[acetyl-CoA-carboxylase] ligase (A0A1D8PUA1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Urea amidolyase
- Acetyl-CoA carboxylase
- Pyruvate carboxylase
- biotin synthase
- Anaphase-promoting complex subunit 11
- CCA tRNA nucleotidyltransferase, mitochondrial
Sequence:
MNVLVYSGPGTTTEGVKHCLETLRLHLGSYYAVLPVNETVLLNEPWMRKTSLLVIPGGADLPYCNVLDGNGTRKISKYVKQGGKFLGLCAGGYFGSARCEFEVGNPTMEVTGPRELGFFPGTAKGCAFKGFKYESRTGARAVKLSVNTAALPGCASHIYNYYDGGAVFANAEKYKDVEILARYDDKTDIVDLEKAAVVYRKVGKGGVILSGTHPEFAPHLLHPRDEDGAGYFIVVDTLRAYDHNKKVFMRDCLKKLGLRVAESVDTTIPRVTPMYVVSPFKDKVRDVYSILTSKLGKSFEDSNDAFYFADETQETSEYVGSEEDPVKYINFLTSAGIPDLKMVPYFDIQKYFDNLRMLSGGDIKFGSILGYSEVITSTNTIMDKNPQWLEHLPNGFTITATTQIAGRGRGGNVWVNPRGVLATSVLFKIPPSPSSSSTVVTLQYLCGLALIESILGYGSNVSGQGVGYEDMPLRLKWPNDIFIMKPEYFKSLDDKSDISATVDGDDEKFVKVSGALINSQFINKTFYLVWGGGVNVSNPAPTTSLNLVLEKLNEIRRGKGLSPLPPYEPEILLAKLMFTIDQFYSVFEKSGLQPFLPLYYKRWFHTNQKVDVDNGSGKQRTCIIKGITPDYGLLIAEDVETKKVLHLQPDGNSFDIFKGLVYKKN
Protein: Transcription factor pcr1 (Transcription factor mts2) (Q09926)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in regulation of gene expression for sexual development. Binds and activates CRE sites (cAMP-response elements, also known as M26 meiotic recombination hotspots).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Transcription factor atf1
- Mitogen-activated protein kinase sty1
- Transcriptional repressor tup12
- Transcriptional repressor tup11
- General transcriptional corepressor ssn6
- Chromatin-associated protein swi6
- Phosphoribosylaminoimidazole carboxylase
- Transcription factor atf31
- Histone deacetylase clr3
- Zinc finger protein rst2
Sequence:
MTAKKKEVDDEKRRRILERNRIAASKFRQKKKEWIKELEQTANAAFEQSKRLQLLLSQLQQEAFRLKSQLLAHQGCQCSVKIRSVLTDFQTAHNALHSQHMAYRPVQPPPGDNMLESVVSVSPTQMHPSLQGLPPNQHPQMPPSSQQPNSDDVQQHMFSAAGLPRSLGGPI
Protein: Probable splicing factor YJU2B (Coiled-coil domain-containing protein 130) (P13994)
Organism: Homo sapiens (Human)
Function: May be involved in mRNA splicing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BW85}.
Interaction partners:
- Junction plakoglobin
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing factor 17
- Cell division cycle 5-like protein
- 116 kDa U5 small nuclear ribonucleoprotein component
- WD repeat-containing protein 25
- Pre-mRNA-splicing factor SYF2
- Bifunctional peptidase and arginyl-hydroxylase JMJD5
Sequence:
MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMADNEQVLTTEHEKKQKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRRRFREKKKAIQEEEERDQALQAKASLTIPLVPETEDDRKLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSAPGSASSSKVSGVLKKLAQSRRTALATSPITVGDLGIVRRRSRDVPESPQHAADTPKSGEPRVPEEAAQDRPMSPGDCPPETTETPKCSSPRGQEGSRQDKPLSPAGSSQEAADTPDTRHPCSLGSSLVADYSDSESE
Protein: Protein MEI2-like 2 (AML2) (MEI2-like protein 2) (Q9SJG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable RNA-binding protein that plays a role in meiosis and vegetative growth.
Interaction partners:
- microtubule-severing ATPase
- F-box/LRR-repeat protein 15
- LRR receptor-like serine/threonine-protein kinase ERECTA
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MVSSIIAVAEGKKMELEPNKSLSADMPSLLSRSSEAFNGGTGYRSSSDLSMFSSSLPTLFHEKLNMTDSDSWLSFDESSPNLNKLVIGNSEKDSLEDVEPDALEILLPEDENELLPGLIDELNFTGLPDELDDLEECDVFCTGGGMELDVESQDNHAVDASGMQISDRGAANAFVPRKRPNTAGRVSVEHPNGEHPSRTLFVRNINSSVEDSELSALFEPFGEIRSLYTACKSRGFVMISYYDIRAAHAAMRALQNTLLRKRTLDIHFSIPKENPSEKDMNQGTLVIFNVDTTVSNDELLQLFGAYGEIREIRETPNRRFHRFIEYYDVRDAETALKALNRSEIGGKCIKLELSRPGGARRLSVPSQSQDLERTEVTNFYNQVGSHVANSPPGNWPIGSPVKGSPSHAFTRPHGLGMVRPVNSDNMPGLASILPAHPSSFHGFSPVSNDQGLLNHSNQTILNKGLMHNISYGQPHSLPEHITGGISNSMRFIAPHSSGFGTSSDHRYRWGSPPQHMNYPGYTGVSSSSSSTERPFTVRHGFPFAERQASLLGKYQHHVGSAPSSIHFNTQMNCYTGSPEIPLGFSDMGINRNYNSAHGKANLGVSLPGNSSEQDFTGFGMSSMPTVPFGGSRGLQSVRPEPFAEQGRIHNHESHNQNQFIDGGRYHIDLDRIASGDEIRTTLIIKNIPNKYTYKMLVAEIDEKHKGDYDFLCLPTDFKNKCNMGHAFINMVSPLHIVPFQQTFNGKIWEKFNSGKVASLAYAEIQGKSALASYMQTPSSMKEQKQLFPEVSYHDDGQDANDHEQLFSSIWNITAPDSDWSYTMDLIENPRENGNSKNAAEESS
Protein: SGNH hydrolase-type esterase superfamily protein (F4JN67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSIKLLVLVFSLLIIFTRPKLIADHHLTTRISPIYPSISTFQPSIPPFLPPSPSRRAQSPTVKPSLPFVPALFVFGDSSVDSGTNNFLGTLARADRLPYGRDFDTHQPTGRFCNGRIPVDYLGLPFVPSYLGQTGTVEDMFQGVNYASAGAGIILSSGSELGQRVSFAMQVEQFVDTFQQMILSIGEKASERLVSNSVFYISIGVNDYIHFYIRNISNVQNLYTPWNFNQFLASNMRQELKTLYNVKVRRMVVMGLPPIGCAPYYMWKYRSQNGECAEEVNSMIMESNFVMRYTVDKLNRELPGASIIYCDVFQSAMDILRNHQHYGFNETTDACCGLGRYKGWLPCISPEMACSDASGHLWWDQFHPTDAVNAILADNVWNGRHVDMCYPTNLETMLHS
Protein: Kinesin-like protein 8 (Q9UTL2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Mitosis inducer protein blt1
- Rho guanine nucleotide exchange factor gef2
- Mitosis inhibitor protein kinase wee1
- Mitosis inducer protein kinase cdr2
- Uncharacterized protein C12B10.10
- Ras GTPase-activating-like protein rng2
- Mitosis inducer protein kinase cdr1
- Myosin type-2 heavy chain 1
- Cell division control protein 12
- Cell division control protein 15
Sequence:
MSTANVRVIVRVRPKSLRELSKSAEDLLSVDSHNKTVTITPPKHGLKHSRHKNRVNGPRTFAFDECFAPSAPESKNLSGQEDVYESTGPLLVKSILEGFNSCFITYGQKGTGKTYSVVGLRGQPGIIPHISESIFEEIDKLKKKSPNTTITVSISLAEIIEETPYDLLQPNVNSSHTPGETVFVQKDSLTGYHLHGLSEFEVGSAQEIDAFLRLAAKNIRTELSDISGVRKGHSVFSLVVQQRIIDPKTRHSLKKASRLQIIDLASFSKGSQRNESISSFESSSNNKSLSVLNRVIAALTSKKNDVLIPYKDSVLTTLLQDALGGNCRTIMLTCVSPCDFDDTFSALRYSEAARRIKNISNINCKEAYSTNNEGELDDILTTLESDREQLRRHEEHSQKLLKFIEEIRNDYEERIHALESQNSALKAHLRLAVDAYLNPLEFNFDDKNVKLKEFGSPNIAYKQELNSFQGELSSLFKDLKLVKSQLHDYPKPEVSDIDMDMESLRHDSLLD
Protein: Heat shock 70 kDa protein 4 (HSP70RY) (Heat shock 70-related protein APG-2) (Heat shock protein family H member 2) (P34932)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Stress-induced-phosphoprotein 1
- Heat shock cognate 71 kDa protein
- DnaJ homolog subfamily B member 1
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- BAG family molecular chaperone regulator 1
- E3 ubiquitin-protein ligase CHIP
- BAG family molecular chaperone regulator 3
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Hsp70-binding protein 1
Sequence:
MSVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACISFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVEAEKSNLAYDIVQLPTGLTGIKVTYMEEERNFTTEQVTAMLLSKLKETAESVLKKPVVDCVVSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVSVCAFNRGKLKVLATAFDTTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSANASDLPLSIECFMNDVDVSGTMNRGKFLEMCNDLLARVEPPLRSVLEQTKLKKEDIYAVEIVGGATRIPAVKEKISKFFGKELSTTLNADEAVTRGCALQCAILSPAFKVREFSITDVVPYPISLRWNSPAEEGSSDCEVFSKNHAAPFSKVLTFYRKEPFTLEAYYSSPQDLPYPDPAIAQFSVQKVTPQSDGSSSKVKVKVRVNVHGIFSVSSASLVEVHKSEENEEPMETDQNAKEEEKMQVDQEEPHVEEQQQQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIENQLLWQIDREMLNLYIENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSGEYEKFVSEDDRNSFTLKLEDTENWLYEDGEDQPKQVYVDKLAELKNLGQPIKIRFQESEERPKLFEELGKQIQQYMKIISSFKNKEDQYDHLDAADMTKVEKSTNEAMEWMNNKLNLQNKQSLTMDPVVKSKEIEAKIKELTSTCSPIISKPKPKVEPPKEEQKNAEQNGPVDGQGDNPGPQAAEQGTDTAVPSDSDKKLPEMDID
Protein: Enolase 4 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Q8C042)
Organism: Mus musculus (Mouse)
Function: Required for sperm motility, function and male fertility. May be involved in the normal assembly of the sperm fibrous sheath and provides most of the enolase activity in sperm.
Interaction partners:
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase 2
- Phosphoglycerate mutase 1
- Bisphosphoglycerate mutase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Multiple inositol polyphosphate phosphatase 1
- GDH/6PGL endoplasmic bifunctional protein
Sequence:
MGDEDGGRRGGITRDLQKLKQQAMAYYQENDVPRKLEDLLNSTFYLQPADVYGHLKANYFSKLAKPPSICKIVGKTILDGLGLPTLQVEISCTIQNFPKYICAVAIPTHFEVVENALPEALDAEDSERAQAVNTAVQWINQSITEELWGLVPSNQAEVDHRLRTFFEHKVQEDKERKELEKSQEELVPAPPPVTLPPPPPPPPPPPSKKKGQKAGRRDTLLEKPVSPPEPPEPVLHGSMAIGAVSLAVAKASATLASDPLYLTLASLKHDQEQPSTFSMPLLMGSVLSCGKSSPGKLHLMKEVICIPSPGLTAKQSVELLLEIQKQVNRAMETLPPPKQETKKGHNGSKRAQPPITGKVSHLGCLTINYDAIEQPLLLLQGICSNLGLELGVNFHLAINCAGHELMDYSKGKYEVMVGTHKSAAEMVELYVDLINKYPSIIALIDPFRKEDAEQWDSLYAALASRCYLIAGAASGSVSKLLECRNISTLKSHGLIIKHTNQTTMSDLVEITHLINGKKLLAVFGSTDSESSDDSLVDLAVGFGARFIKLGGLSRGERMTKYNRLLAIEEELIQRGVWGFSEEHNFSFFQEDATATMAEETLGLLDSIFPTEVIEESAKT
Protein: Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (Diaminopelargonic acid synthase) (P50277)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Interaction partners:
- Dethiobiotin synthetase
- Biotin synthase, mitochondrial
- Protein ARG5,6
- 7-keto 8-aminopelargonic acid transporter
- Vitamin H transporter
- Argininosuccinate lyase
- Uncharacterized protein YJR154W
- Arginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Argininosuccinate synthase
- Putative aryl-alcohol dehydrogenase AAD10
Sequence:
MSQEISYTPDVAELLDFDKKHIWHPYTSLSSPLNVYPVKSAHGCKLVLDTDSPVDVEVIDAMSSWWCVIHGYNNPELNEALTKQMLKFSHVLLGGFTHKGAVNLVQKLLKVIDEPSLQYCFLADSGSVAVEVALKMALQSNMSGEATKNRTKFLTIKNGYHGDTFGAMSVCDPENSMHHIYNDRLSENIFAQAPSIVDGLPTSQNGFEDHWNAEEVTDLKKQFELHSDKICAVILEPILQGAGGLRPYHPQFLIEVQKLCNQYDVLFIMDEIATGFGRTGEIFAFKHCQKYQDQHGISPSDQIKVVPDILCVGKGLTSGYMTMSAVVVNDKVASRISSPNSPTGGCFMHGPTFMGNALACSVAEKSMDILLRGEWRKQVSAIENQIYRELYQYIKNPDNGLIGTVVKRVSVIGAVGIVELYKKTDPEWFQKKFISKGVHIRPFNCLCYIMPPYVITTEELTKVNQVLIEVLHEWKSHINQ
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (A0A0G2JTH7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGASNNSEIKMNKKEEFKEVDYLTEEKVYEIYEFCREREDYSPLIRVIGRIFSSAEALVQSFRKVKQHTKEELKSLQEKDEDKDEDEKEKAACSAAAMEEDSEASSSRMGDSSQGDNNVQKLGPDDVTVDIDAIRRVYSSLLSDEKIETAFLNALVYLSPNVECDLTYHNVYTRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYSADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGDVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETEIGVKTLDCRKPLISFEEFINEPLNDVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATRLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFCDLGDSHPILYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVSLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIR
Protein: Myosin IA heavy chain (Myosin-like protein abmA) (P22467)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actin-based motor protein, possibly involved in a wide range of motile processes, such as cell movement across a surface, and extension and retraction of pseudopodia or lamellipodia.
Interaction partners:
Sequence:
MATFKRDLTKNVGVEDLIMLTEVSESSLHENLKIRYKEGLIYTSIGPVLVSMNPYKQLGIYGNDQINLYKGKHEFEIPPHIYSIADKAYRALRSEGENQCIIISGESGAGKTEASKYIMQYIASITGSSTEVERVKKTILESNPLLEAFGNAKTLRNNNSSRFGKYMEIQFNLGGDPEGGKITNYLLEKSRVINQTQGERNFHIFYQLLKGSSEEEKKTYNLLSPDQYHYLTRNASNGCFTADGIDDQIGFKQTKNAMKVVGIDEPLQKEIFATLSAILLLGNLSFNKSASGNGSVISDKKLANTIASLMGVDAIVLESSLVSRQISTGQGARISTYSVPQTVEQAMYARDAFAKATYSKLFDFIVRKINQSIEVKTIGKVIGVLDIYGFEIFENNSFEQFCINYVNETLQQIFIDLTLKTEQEEYVQEGITWIPVQYINNKACVDLIEKKPIGILSLLDEECLFPEGNDQTMIDKLNKHFSNHTHYSKVERQKNSQFIINHYAGKVFYNIDGFLDKNRDTLFNDLVTLATSSSCSLLVEIFKYVPPLEVDPEQEKKNRDKFSKNGFANNAAKTFIPTDKKRPITAGFQFKNQVTSLLKSLYSCSPHYVRCIKPNSNMRALEWDQSKCAEQVAYLGLFENLLVRRAGYCYRQTFSKFMRRYYMIGKSTWPKWSGDAEKGVNLLMGELTQEINIKEEVQYGKTKIFIRNPQPLFLLEDKRNKRLNDLATKIGSVWKMYKQRKWYLRTLAAIKIQRTYRGWLLVRECVKLKNQSISIFQNNKERNRQSIKLSKAAFIGDFLSLTRDNYTTATLKREEGPNAVLQLSLNVSKVSRHHKIQKRSLLVTNETIFTITPHKPKKDGSWFAIKRKVPFSAIEKISFSKLSDDFFVIHIINEHDLCLETNKKTVLITLLSNLYSKHLNGKELVFEFKDSIQYRNQKGPSELKFVKVDSIHEKSSNSPQANSPSFTAKAEKNYLKVCVLPGLSSESKSILIEK
Protein: Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (Mitochondrial translation optimization protein 2) (Synthetic lethal with MSS4 3) (Q12093)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150}.
Interaction partners:
- Mitochondrial translation optimization protein 1
- Cysteine desulfurase, mitochondrial
- Cytoplasmic tRNA 2-thiolation protein 1
- tRNA modification GTPase MSS1
- Adenylyltransferase and sulfurtransferase UBA4
- Methionyl-tRNA formyltransferase, mitochondrial
- Putative oxidoreductase TDA3
- Trichothecene 3-O-acetyltransferase
Sequence:
MLARYLNLIGRRSASPYRPQRLPAKFDNVIVAMSSGVDSSVAAALFAGEFPNTRGVYMQNWSESQSLDDPGKEPCYERDWRDVNRVAKHLNIRVDKVNFEQDYWIDVFEPMLRGYSEGSTPNPDIGCNKFVKFGKLREWLDEKYGTGNYWLVTGHYARVMQEMNGKGLFHLLRSIYRPKDQSYYLSQINSTVLSSLLLPIGHLTKPEVRDLAKYAGLPTAEKPDSQGICFVNNSQHGKFKNFLKHYLPSSPGDIITVDPQSGAKTTWGRHDGLWSYTIGQKVGISMPQADPNYQGTWFVSEKLRDTNEILIVRGRDNPALYSDTMRIENFSSLGPREDTINAFQNTGALTLQFRSLQVPVQIKSCKLNRSADNLDITIHLASKQRAITPGQSCCLYIDDRVLGSGPISHVNNNDTHA
Protein: Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme) (Q8ZKF6)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine.
Interaction partners:
- Phosphate acetyltransferase
- Acetate kinase AckA
- Malate synthase
- Phosphate acetyltransferase EutD
- 2-methylcitrate synthase
- Citrate synthase
- Propionate kinase PduW
- Pyruvate-flavodoxin oxidoreductase
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
Sequence:
MSQTHKHAIPANIADRCLINPEQYETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIAMPS
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (A0A8I6GKW5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083}.
Interaction partners:
Sequence:
VTAINYEIIIIDDGSPDGTREVAEQLEKIYGPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFITQILLRPGASDLTGSFRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMDYTVGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT