wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin 1 (A0A1D8PN92)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mlc2p
- Mlc1p
- Actin
- Nuclear control of ATPase protein 2
- Ras GTPase-activating-like protein IQG1
- Formin-binding protein
- Centractin
- Calmodulin
- UNC-45/Cro1/She4 central domain-containing protein
- Myosin 2
Sequence:
MVTSSTANDNNNEDPIISKNWVWVPNQQDLFTKGYITDYLPDGKCKVNVVKGQESSHDSTIIVDQDKLENCNPVKFNKCEDMAELTHLNEPSVVYNLYLRYLDDLIYTYSGLFLVAINPYKSLPIYNQSILMKYHQYNNVTTNKNDYKSKNASNSNNNNKGQSPPHIFAVAESTFRNLLSNKKDQSILVTGESGAGKTENTKKIIQYLSSITSGSHTNKVDHNNSIDTKILQANPILESFGNAKTIKNNNSSRFGKFIQIYFSNTGEISGANINYYLLEKSRVISQSNQERNYHIFYQFLKGYENLPSLGLNKDMSTYNYLSGGKLTINNVDDFKEFNLLVEAFKIMGFTTNKMNFIYQVLAIILHLGNITFTSWKSEQANFTNDSPIDRICELLAVDKDLFVQNLLRPKVKAGREFITKSKKPNEVKFAIDAFAKYLYEKLFQFIITKINEKLDQSHNGDDNTANNNNDNNFFIGVLDIAGFEIFDINSFEQLCINYTNEKLQQFFNHHSFILEQSEYLRENINWEFIDFGQDLQPTIDLIETKQPMGILKLLDEECLMPKSSDASFMEKLSKNFSNTHKKFSENKFKNGFIIHHYAGKVEYNVENWLQKNTDPISESILNLLPDSQNELIADMFINDPHINRPQTNGGGNSKLKTASQKHKDQLKTLMDQLESTEPHFVRCILPNLEKRANKFDKNLVLGQLRCNGVLEGIRITRAGYPNRMMFDEFIQRYSIICDNELSSPQNKTNCEIILKFVKLNPEDFKVGLTKIFFKNGILGKLEIIRDLALKNIFTDLQKVIRGNLTRLVLKQKIKEIQSAQIISRTMVTLDEIKSNSPWMRLFFHVKPLLEDSAKVLDSKKLQENLQTLTVKLKDSEKLTKGLETDNEKLREQMNNLQDEMINITSIAKEKDDKLSQLRLTENKSKHRIETLEIKLKDFEKQNQDLINEHEKLTRRSLELHDKHNAKVEELNSLNKLHDSAQSELSNLKQQLKEITKLKQDHSKELLKFKQMHDKSIEDLNEKVSRLENLNKKLQADLNSSKDVISSEHGKLQNEIMKLKELCSDYERKQKDSQRTIDSLQIQLKKDEDYKSRYESKIEEAREKVTLLKGKVEKKSQEIDQYKSEIKKLKAELASSNTKITQLDQSTKELSSLKSNESKYVAEIESAKQQLSKKIEEYSSIEADYNRLQTELKQMKQTNTEYSTRITELSTKLNQVTEEAKSKEIEKENQPPNPQFMEEFTHMKLKVNEQTASLRKEKFENKKLSEELQMLKERIMNGSLTSMDLTPKRRSLAIGDKSMITNTVDSFNKEIENLKFQLQQEQGNFQRAENYAIELQKKLNKLLTTRGLNTNTDYEKKYNDSQKRITQLETKIGRLLANSGGDYEDHHLDDNDDDWESRSSNGGSGGGSTSSSARNSLVKSESITAFHNMRGVSQDYIQIYQDITKTLKSTREELNGSKTEILRLKALLRESEDELYQVKQENYKTSVHDYEQDLAQLKVKHETLLSRNKDINESLEIYKKRSDEYYKKLELAESAIAISKRHEEQATKEMKESRSQLLLVREELRTTQILIKDFRIKVGNLEATIEEKNHQLDANKEEIKQIQDKLNYHLKNFENKELNEKLKEEIKNLNRDLDFKTDIETKLIKENKKLQLDYEDVLLVKNNLQNEVEELILQEEKLQNKIDELTNNNRQLENEKLINERKIVNCTKQISGLKELVDEISIERDKLLKDKETLQNDLQIMTNKFDSTTTELKQAHGELNFLKKHLENQREDSEAIKTELNQSKMSTSFDIRDQQKLRNELLVTKEENFSLVKTNKELNLKVSDLEEKLYSNEQLKYWESKVDTLSKALDGALNEKHEADKTIKNLQRSIKQLEIRVENESQLSKRYNDENFDYQNKINHYKSTIDIIHNENIEKDLQLKSIQRENIEMKESMLMLQKEVLELRERLQV
Protein: Paired box protein Pax-4 (O88436)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that competes with PAX6 in binding to a common element in the glucagon, insulin and somatostatin promoters (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Neurogenin 3
- Neurogenic differentiation factor 1
- Mitochondrial import inner membrane translocase subunit Tim22
- NK2 homeobox 2
- Insulin gene enhancer protein ISL-1
- Pro-glucagon
- Regulatory factor X, 6
- Transcription factor MafB
- Insulin-1
- Insulin-2
Sequence:
MQQDGLSSVNQLGGLFVNGRPLPLDTRQQIVQLAIRGMRPCDISRSLKVSNGCVSKILGRYYRTGVLEPKGIGGSKPRLATPAVVARIAQLKDEYPALFAWEIQRQLCAEGLCTQDKAPSVSSINRVLRALQEDQRLHWTQLRSPAVLAPALPSPHSNCEAPRGPHPGTSHRNRTIFSPGQAEALEKEFQRGQYPDSVVRGKLAAATSLPEDTVRVWFSNRRAKWRRQEKLKWETQMPGASQDLMVPKDSPGIISAQQSPGSVPSAALPVLEQLNPSFCQLCWGAVPDRCSSDTTSQACLQPYWECHSLLPVASSSYMEFAWPCLTTHPVHHLIGGPGQAPSTYYLHWP
Protein: Riboflavin biosynthesis protein PYRR, chloroplastic [Includes: Inactive diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (Riboflavin-specific deaminase); 5-amino-6-(5-phosphoribosylamino)uracil reductase (EC 1.1.1.193) (HTP reductase); Riboflavin biosynthesis intermediates N-glycosidase (EC 3.2.2.-)] (K7WIZ6)
Organism: Zea mays (Maize)
Function: Pyrimidine reductase involved in the riboflavin biosynthesis pathway. Has also a non-functional N-terminal deaminase domain that lacks the catalytically essential zinc-binding residues. 39% activity when NADH replaces NADPH. No evidence for a phosphatase activity conferred by the N-terminal domain.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23150645}.
Interaction partners:
- Bifunctional riboflavin biosynthesis protein RIBA 1 chloroplastic
- Bifunctional riboflavin biosynthesis protein RIBA 1 chloroplastic
- Riboflavin biosynthesis protein PYRD, chloroplastic
- Genetic modifier superfamily protein)
- Inhibitor of striate1
- Cytidine/deoxycytidylate deaminase family protein.
- Cytidine/deoxycytidylate deaminase family protein
- Bifunctional riboflavin biosynthesis protein RIBA 1 chloroplastic
- GTP cyclohydrolase II
- GTP cyclohydrolase II
Sequence:
MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQRKLAMKGVEVVEFDMLNPRAVMSYCYDRGYLAVLWECGGTLAASAISASVIHKVYAFWAPKIIGGLNAPTPVGELGMSQMTQAINLIDVSYEQIDRDMLMSGFIEPIPDLSPVIPSVEEIPSIDPEVSPYETNIISFYKTWDIFGAFSNFSPHSIQMPDENGDYFTWPTVEHYYQAHKFVGVDNPQARDIVQEIKLAKSPEEAARIGRTRQKGFPELVRTDWESTKIDVMYRAIKCKFSTYPHLTNMLLSTAGSVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEILGTVPASAEVGEAD
Protein: Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (Q07806)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Subcellular location: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Peptidoglycan D,D-transpeptidase MrdA
- serine-type D-Ala-D-Ala carboxypeptidase
- Penicillin-binding protein 1B
- Peptidoglycan D,D-transpeptidase FtsI
- Peptidoglycan glycosyltransferase MrdB
- Probable peptidoglycan glycosyltransferase FtsW
- D-alanyl-D-alanine endopeptidase
- Cell division protein FtsZ
- Cell shape-determining protein MreB
- Beta-hexosaminidase
Sequence:
MRLLKFLWWTCVTLICGVLLSFSGAYLYLSPSLPSVEALRNVQLQIPLKVYSEDGKLISEFGEMRRTPIRFADIPQDFIHALLSAEDDNFANHYGVDVKSLMRAAAQLLKSGHIQTGGSTITMQVAKNYFLTNERSFSRKINEILLALQIERQLTKDEILELYVNKIYLGNRAYGIEAAAQVYYGKPIKDLSLAEMAMIAGLPKAPSRYNPLVNPTRSTERRNWILERMLKLGFIDQQRYQAAVEEPINASYHVQTPELNAPYIAEMARAEMVGRYGSEAYTEGYKVITTVRSDLQNAASQSVRDGLIDYDQRHGYRGPETRLPGQTRDAWLKHLGQQRSIGGLEPAIVTQVEKSGIMVMTRDGKEEAVTWDSMKWARPFLSNNSMGPMPRQPADVAQAGDQIRVQRQEDGTLRFVQIPAAQSALISLDPKDGAIRSLVGGFSFEQSNYNRAIQAKRQPGSSFKPFIYSAALDNGFTAASLVNDAPIVFVDEYLDKVWRPKNDTNTFLGPIPLREALYKSRNMVSIRVLQGLGIERAISYITKFGFQRDELPRNFSLALGTATVTPMEIAGAWSVFANGGYKVNPYVIERIESRDGQVLYQANPPRVPVEEQVAADAEDAGNPGDPEHPESAEGEGSIEAQQVAAKAQTTFEPTPAERIIDARTAYIMTSMLQDVIKRGTGRRALALKRTDLAGKTGTTNDSKDGWFSGYNSDYVTSVWVGFDQPETLGRREYGGTVALPIWIRYMGFALKDKPMHTMAEPPGIVSLRIDPVTGRSAAPGTPGAYFEMFKNEDTPPSVNELPPGSFPGSPLPDDEGAPIDLF
Protein: Presenilin-like protein At1g08700 (O64668)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nicastrin
- Gamma-secretase subunit APH1-like
- Probable gamma-secretase subunit PEN-2
- Protein DETOXIFICATION 23
- Signal peptide peptidase
- 3-oxo-5-alpha-steroid 4-dehydrogenase
- Lung seven transmembrane receptor family protein
- Probable protein S-acyltransferase 13
- Probable ADP-ribosylation factor GTPase-activating protein AGD14
- Protein RETICULATA-RELATED 2
Sequence:
MESSILDSLGVEIIGVMAPVSICMFLVVLLTYSLSVTSDPQIRSAANLIYIENPSDSTTVKLEGSLANAIVFVVLIAAVTFILVLLFYYNFTNFLKHYMRFSAFFVLGTMGGAIFLSIIQHFSIPVDSITCFILLFNFTILGTLSVFAGGIPIVLRQCYMVVMGIVVAAWFTKLPEWTTWFILVALALYDLVAVLAPGGPLKLLVELASSRDEELPAMVYEARPTVSSGNQRRNRGSSLRALVGGGGVSDSGSVELQAVRNHDVNQLGRENSHNMDYNAIAVRDIDNVDDGIGNGSRGGLERSPLVGSPSASEHSTSVGTRGNMEDRESVMDEEMSPLVELMGWGDNREEARGLEESDNVVDISNRGIKLGLGDFIFYSVLVGRAAMYDLMTVYACYLAIISGLGCTLILLSVYNRALPALPISIMLGVVFYFLTRLLMEPFVVGVTTNLMMF
Protein: S-layer protein 1 (102 KDa parasporal endotoxin) (P85122)
Organism: Bacillus thuringiensis subsp. konkukian
Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
Subcellular location: Secreted, cell wall, S-layer.
Interaction partners:
Sequence:
SATVELYSNLAAKGLAVEFTSTSLKAALLNILSVDGVPATTAK
Protein: ADF actin binding protein (Coactosin like F-actin binding protein 1) (C7G537)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MATKIDKEACREAYNLVRDDATEVNWVTFKYNGSTIVPGDQGVDYETFKRKCTDDVRLFGFVRFTTGDAMSKRVKFALITWIGEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDHKELDEDYIKNELKKAGGANYDAQTE
Protein: Gephyrin b (Gephyrin2) (D3KYL1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASDGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDPSLLGGTISAYKIVPDEIDEIKETLVDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLREAVVKVKEIPNELEDLPSPPPPLSPLPASSPHRQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAASIAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTAVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTHTVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVQKFPVIAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGINRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDMDGSRKLIFALPGNPVSAVVTCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: Chaperonin-like RBCX protein 1, chloroplastic (AtRBCX1) (Q94AU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone involved in RuBisCO assembly process.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21922322}. Note=Associated with the thylakoid membranes. {ECO:0000269|PubMed:21922322}.
Interaction partners:
- Chaperonin-like RbcX protein 2, chloroplastic
- 2-oxoglutarate
- Agamous-like MADS-box protein AGL97
- Appr-1-p processing enzyme family protein
- Casein kinase II subunit beta-2
- Defensin-like protein 81
- Protein LOW PHOTOSYNTHETIC EFFICIENCY 1
- Cytochrome P450 family protein
Sequence:
MESSSSLLHHSYLSYLNPKFGKRPLVSYPLMQSSRKCKQTRICSNKMYVPGFGEASPEAKAAKHLHDFFTYVAVRIVSAQLESYNPEAYMELREFLDTNSVSDGDKFCATLMRRSSRHMNLALRILEVRSAYCKNDFEWDNMKRLAFKNVDDSNTRLMREYVLETSHVETDSDK
Protein: CBL-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (SNF1-related kinase 3.2) (SOS2-like protein kinase PKS16) (Q9LYQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Interaction partners:
- Calcineurin B-like protein 1
- Calcineurin B-like protein 4
- Calcineurin B-like protein 2
- Calcineurin B-like protein 3
- Calcineurin B-like protein 9
- Zinc finger CCCH domain-containing protein 53
Sequence:
MENKPSVLTERYEVGRLLGQGTFAKVYFGRSNHTNESVAIKMIDKDKVMRVGLSQQIKREISVMRIAKHPNVVELYEVMATKSRIYFVIEYCKGGELFNKVAKGKLKEDVAWKYFYQLISAVDFCHSRGVYHRDIKPENLLLDDNDNLKVSDFGLSALADCKRQDGLLHTTCGTPAYVAPEVINRKGYEGTKADIWSCGVVLFVLLAGYLPFHDTNLMEMYRKIGKADFKCPSWFAPEVKRLLCKMLDPNHETRITIAKIKESSWFRKGLHLKQKKMEKMEKQQVREATNPMEAGGSGQNENGENHEPPRLATLNAFDIIALSTGFGLAGLFGDVYDKRESRFASQKPASEIISKLVEVAKCLKLKIRKQGAGLFKLERVKEGKNGILTMDAEIFQVTPTFHLVEVKKCNGDTMEYQKLVEEDLRPALADIVWVWQGEKEKEEQLLQDEQGEQEPS
Protein: AT-hook motif nuclear-localized protein 15 (AT-hook protein of GA feedback 2) (Q9M2S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Binds the DNA sequence GNFEI (GA-negative feedback element I) in the GA3OX1 promoter. Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered FRK1 expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VYJ2}.
Interaction partners:
- B3 domain-containing protein At3g17010
- B3 domain-containing protein At5g57720
- Gamma-interferon-responsive lysosomal thiol protein
Sequence:
MANPWWVGNVAIGGVESPVTSSAPSLHHRNSNNNNPPTMTRSDPRLDHDFTTNNSGSPNTQTQSQEEQNSRDEQPAVEPGSGSGSTGRRPRGRPPGSKNKPKSPVVVTKESPNSLQSHVLEIATGADVAESLNAFARRRGRGVSVLSGSGLVTNVTLRQPAASGGVVSLRGQFEILSMCGAFLPTSGSPAAAAGLTIYLAGAQGQVVGGGVAGPLIASGPVIVIAATFCNATYERLPIEEEQQQEQPLQLEDGKKQKEENDDNESGNNGNEGSMQPPMYNMPPNFIPNGHQMAQHDVYWGGPPPRAPPSY
Protein: Heparin-binding fibroblast growth factor receptor 2 (Q63239)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
CTDNISVQMGLTSTWRYGTGPGIGTVTMVSWGRFICLVLVTMATLSLARPSFSLVEDTTLEPEGAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEMDAGEYICKVSNYIGQANQSAWLTVLPKQQAPVREKEITASPDYLEIAIYCIGVFLIACMVVTVIFCRMKTTTKKPDFSSQPAVHKL
Protein: Serine/threonine-protein kinase D3 (EC 2.7.11.13) (Protein kinase C nu type) (Protein kinase EPK2) (nPKC-nu) (O94806)
Organism: Homo sapiens (Human)
Function: Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18076381}. Membrane {ECO:0000269|PubMed:18076381}. Note=Translocation to the cell membrane is required for kinase activation.
Interaction partners:
- Serine/threonine-protein kinase D1
- Serine/threonine-protein kinase D2
- Protein kinase C alpha type
- Protein kinase C beta type
- Ras-related protein Rap-1A
- Integrin beta-1
- Integrin beta-2
- Ras-related protein Rap-1b
- Integrin alpha-M
- Protein kinase C gamma type
Sequence:
MSANNSPPSAQKSVLPTAIPAVLPAASPCSSPKTGLSARLSNGSFSAPSLTNSRGSVHTVSFLLQIGLTRESVTIEAQELSLSAVKDLVCSIVYQKFPECGFFGMYDKILLFRHDMNSENILQLITSADEIHEGDLVEVVLSALATVEDFQIRPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPGPGLSVPRPLQPEYVALPSEESHVHQEPSKRIPSWSGRPIWMEKMVMCRVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCKFNCHKRCASKVPRDCLGEVTFNGEPSSLGTDTDIPMDIDNNDINSDSSRGLDDTEEPSPPEDKMFFLDPSDLDVERDEEAVKTISPSTSNNIPLMRVVQSIKHTKRKSSTMVKEGWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRISSPRDFTNISQGSNPHCFEIITDTMVYFVGENNGDSSHNPVLAATGVGLDVAQSWEKAIRQALMPVTPQASVCTSPGQGKDHKDLSTSISVSNCQIQENVDISTVYQIFADEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKMRFPTKQESQLRNEVAILQNLHHPGIVNLECMFETPERVFVVMEKLHGDMLEMILSSEKSRLPERITKFMVTQILVALRNLHFKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRSKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWREISGEAIDLINNLLQVKMRKRYSVDKSLSHPWLQDYQTWLDLREFETRIGERYITHESDDARWEIHAYTHNLVYPKHFIMAPNPDDMEEDP
Protein: Protein kinase (Q76PF3)
Organism: bovine alphaherpesvirus 1
Interaction partners:
Sequence:
MERAAERLARQRARGLWRSRFACCVAAEPSGEPARPERSRSRCGSARCAAAGSADLYLAVNNEGPEVAPPARTGPPDADGIEGGAAVGNEQGGVAAGNERRAAIGDKKKSASGGENESESESESESESGSESGADDGDWDDDDDAGPAGGVTREEAEGAARALNFRIIRRLTPGSEGRVFEATGPAPAQEHVVLKIGASASTLAEAMLLRTLDHANVVKLKAVLFHGELVCVVLARYREDLHTHLWRINRPLALPAALAVTRAVLRGLAYLHSRRIAHRDVKTENVFLNGPGDVCLGDFGAAHGPVTEPRYYGLAGTLETNSPELLARARYDCRTDVWSAGVVAYEMLAYPRALFDSPAGPQGEDAEASGPPTILGDRDCARQLLRVIRRLAVHAEEFPPSPTDRLTRNFKRHASTRREPHSPYRCLAVLRLPCDADRLLHQMLTFDFRARPTAAELLEHPVFGAASG
Protein: YjeF N-terminal domain-containing protein 3 (YjeF_N3) (hYjeF_N3) (ApoA-I-binding protein 2) (A6XGL0)
Organism: Homo sapiens (Human)
Function: May accelerate cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis. May orchestrate hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence (By similarity). May play a role in spermiogenesis and oogenesis.
Interaction partners:
- Pyridoxine-5'-phosphate oxidase
- ATP-dependent
- m7GpppN-mRNA hydrolase
Sequence:
MSSAAGPDPSEAPEERHFLRALELQPPLADMGRAELSSNATTSLVQRRKQAWGRQSWLEQIWNAGPVCQSTAEAAALERELLEDYRFGRQQLVELCGHASAVAVTKAFPLPALSRKQRTVLVVCGPEQNGAVGLVCARHLRVFEYEPTIFYPTRSLDLLHRDLTTQCEKMDIPFLSYLPTEVQLINEAYGLVVDAVLGPGVEPGEVGGPCTRALATLKLLSIPLVSLDIPSGWDAETGSDSEDGLRPDVLVSLAAPKRCAGRFSGRHHFVAGRFVPDDVRRKFALRLPGYTGTDCVAAL
Protein: Transcription factor GATA-5 (GATA-binding factor 5) (Q9BWX5)
Organism: Homo sapiens (Human)
Function: Transcription factor required during cardiovascular development. Plays an important role in the transcriptional program(s) that underlies smooth muscle cell diversity (By similarity). Binds to the functionally important CEF-1 nuclear protein binding site in the cardiac-specific slow/cardiac troponin C transcriptional enhancer.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Homeobox protein Nkx-2.5
- Lactase/phlorizin hydrolase
- Zinc finger protein ZFPM2
- T-box transcription factor TBX20
- Hepatocyte nuclear factor 1-alpha
Sequence:
MYQSLALAASPRQAAYADSGSFLHAPGAGSPMFVPPARVPSMLSYLSGCEPSPQPPELAARPGWAQTATADSSAFGPGSPHPPAAHPPGATAFPFAHSPSGPGSGGSAGGRDGSAYQGALLPREQFAAPLGRPVGTSYSATYPAYVSPDVAQSWTAGPFDGSVLHGLPGRRPTFVSDFLEEFPGEGRECVNCGALSTPLWRRDGTGHYLCNACGLYHKMNGVNRPLVRPQKRLSSSRRAGLCCTNCHTTNTTLWRRNSEGEPVCNACGLYMKLHGVPRPLAMKKESIQTRKRKPKTIAKARGSSGSTRNASASPSAVASTDSSAATSKAKPSLASPVCPGPSMAPQASGQEDDSLAPGHLEFKFEPEDFAFPSTAPSPQAGLRGALRQEAWCALALA
Protein: Chlorophyll a-b binding protein 2, chloroplastic (Chlorophyll a-b protein 165) (CAB-165) (LHCII type I CAB-2) (P0CJ48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Interaction partners:
- Chlorophyll a-b binding protein CP26, chloroplastic
- Photosystem II CP43 reaction center protein
- Chlorophyll a-b binding protein CP29.1, chloroplastic
- Chlorophyll a-b binding protein
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Chlorophyll a-b binding protein 3, chloroplastic
- Photosystem II protein D1
- Photosystem II CP47 reaction center protein
- Chlorophyll a-b binding protein 3, chloroplastic
- Photosystem II D2 protein
Sequence:
MAASTMALSSPAFAGKAVNLSPAASEVLGSGRVTMRKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK
Protein: Fibronectin type-III domain-containing protein (A0A060YX94)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Interferon/interleukin receptor domain-containing protein
- Uncharacterized protein
- Fibronectin type-III domain-containing protein
- Fibronectin type-III domain-containing protein
- Fibronectin type-III domain-containing protein
- Interferon alpha-2-like
- Fibronectin type-III domain-containing protein
- Uncharacterized protein
- Type I interferon b3
- Uncharacterized protein
Sequence:
MAWVRMVHISLILVLSQQVDSYVPPPVNVSVICHNFHNVIYWNYSEPSLQPQFNVEMTRKYSGAALVCSNTSLYHCDVSSFTKVIEEGYRFILTAVGQNTNSSEISFTYDDTVYPDLVDVQCSLDFPPVNISAVSDQIIKVQFIHPFHIYKYAIIKNERPDHKEFDYMVVTEDHLVRTAGKL
Protein: Aquaporin Z (Bacterial nodulin-like intrinsic protein) (Water channel AqpZ) (P60844)
Organism: Escherichia coli (strain K12)
Function: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10487750, ECO:0000269|PubMed:10518952}; Multi-pass membrane protein {ECO:0000269|PubMed:10487750, ECO:0000269|PubMed:10518952}.
Interaction partners:
- Ammonium transporter AmtB
- Large-conductance mechanosensitive channel
- Lysine exporter LysO
Sequence:
MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD
Protein: 5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog) (Q8IZH2)
Organism: Homo sapiens (Human)
Function: Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12515382, ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:9802570}. Note=Discrete foci at the inner surface of the cell membrane.
Interaction partners:
- m7GpppN-mRNA hydrolase
- Enhancer of mRNA-decapping protein 3
- mRNA-decapping enzyme 1A
- Protein PAT1 homolog 1
- U6 snRNA-associated Sm-like protein LSm1
- Protein PAT1 homolog 2
- Enhancer of mRNA-decapping protein 4
- mRNA-decapping enzyme 1B
- Probable ATP-dependent RNA helicase DDX6
- U6 snRNA-associated Sm-like protein LSm3
Sequence:
MGVPKFYRWISERYPCLSEVVKEHQIPEFDNLYLDMNGIIHQCSHPNDDDVHFRISDDKIFTDIFHYLEVLFRIIKPRKVFFMAVDGVAPRAKMNQQRGRRFRSAKEAEDKIKKAIEKGETLPTEARFDSNCITPGTEFMARLHEHLKYFVNMKISTDKSWQGVTIYFSGHETPGEGEHKIMEFIRSEKAKPDHDPNTRHCLYGLDADLIMLGLTSHEAHFSLLREEVRFGGKKTQRVCAPEETTFHLLHLSLMREYIDYEFSVLKEKITFKYDIERIIDDWILMGFLVGNDFIPHLPHLHINHDALPLLYGTYVTILPELGGYINESGHLNLPRFEKYLVKLSDFDREHFSEVFVDLKWFESKVGNKYLNEAAGVAAEEARNYKEKKKLKGQENSLCWTALDKNEGEMITSKDNLEDETEDDDLFETEFRQYKRTYYMTKMGVDVVSDDFLADQAACYVQAIQWILHYYYHGVQSWSWYYPYHYAPFLSDIHNISTLKIHFELGKPFKPFEQLLAVLPAASKNLLPACYQHLMTNEDSPIIEYYPPDFKTDLNGKQQEWEAVVLIPFIDEKRLLEAMETCNHSLKKEERKRNQHSECLMCWYDRDTEFIYPSPWPEKFPAIERCCTRYKIISLDAWRVDINKNKITRIDQKALYFCGFPTLKHIRHKFFLKKSGVQVFQQSSRGENMMLEILVDAESDELTVENVASSVLGKSVFVNWPHLEEARVVAVSDGETKFYLEEPPGTQKLYSGRTAPPSKVVHLGDKEQSNWAKEVQGISEHYLRRKGIIINETSAVVYAQLLTGRKYQINQNGEVRLEKQWSKQVVPFVYQTIVKDIRAFDSRFSNIKTLDDLFPLRSMVFMLGTPYYGCTGEVQDSGDVITEGRIRVIFSIPCEPNLDALIQNQHKYSIKYNPGYVLASRLGVSGYLVSRFTGSIFIGRGSRRNPHGDHKANVGLNLKFNKKNEEVPGYTKKVGSEWMYSSAAEQLLAEYLERAPELFSYIAKNSQEDVFYEDDIWPGENENGAEKVQEIITWLKGHPVSTLSRSSCDLQILDAAIVEKIEEEVEKCKQRKNNKKVRVTVKPHLLYRPLEQQHGVIPDRDAEFCLFDRVVNVRENFSVPVGLRGTIIGIKGANREADVLFEVLFDEEFPGGLTIRCSPGRGYRLPTSALVNLSHGSRSETGNQKLTAIVKPQPAVHQHSSSSSVSSGHLGALNHSPQSLFVPTQVPTKDDDEFCNIWQSLQGSGKMQYFQPTIQEKGAVLPQEISQVNQHHKSGFNDNSVKYQQRKHDPHRKFKEECKSPKAECWSQKMSNKQPNSGIENFLASLNISKENEVQSSHHGEPPSEEHLSPQSFAMGTRMLKEILKIDGSNTVDHKNEIKQIANEIPVSSNRRDEYGLPSQPKQNKKLASYMNKPHSANEYHNVQSMDNMCWPAPSQIPPVSTPVTELSRICSLVGMPQPDFSFLRMPQTMTVCQVKLSNGLLVHGPQCHSENEAKEKAALFALQQLGSLGMNFPLPSQVFANYPSAVPPGTIPPAFPPPTGWDHYGSNYALGAANIMPSSSHLFGSMPWGPSVPVPGKPFHHTLYSGTMPMAGGIPGGVHNQFIPLQVTKKRVANKKNFENKEAQSSQATPVQTSQPDSSNIVKVSPRESSSASLKSSPIAQPASSFQVETASQGHSISHHKSTPISSSRRKSRKLAVNFGVSKPSE