wanglab/gogpt-training-data huggingface dataset:
Protein: PRRC2A (A0A1U9X974)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDRSGPTAKGKDGKKYSSLNLFDTYKGKSLEIQKPAVAPRHGLQSLGKVAIARRMPPPANLPSLKAENKGNDPNVSLVPKDGTGWASKQEQSDPKSSDASTAQPPESQPLPASQTPASNQPKRPPAAPENTPLVPSGVKSWAQASVTHGAHGDGGRASSLLSRFSREEFPTLQAAGDQDKAAKERESAEQSSGPGPSLRPQNSTTWRDGGGRGPDELEGPDSKLHHGHDPRGGLQPSGPPQFPPYRGMMPPFMYPPYLPFPPPYGPQGPYRYPTPDGPSRFPRVAGPRGSGPPMRLVEPVGRPSILKEDNLKEFDQLDQENDDGWAGAHEEVDYTEKLKFSDEEDGRDSDEEGAEGHRDSQSASGEERPPEADGKKGNSPNSEPPTPKTAWAETSRPPETEPGPPAPKPPLPPPHRGPAGNWGPPGDYPDRGGPPCKPPAPEDEDEAWRQRRKQSSSEISLAVERARRRREEEERRMQEERRAACAEKLKRLDEKFGAPDKRLKAEPAAPPAAPSTPAPPPAVPKELPAPPAPPPASAPTPETEPEEPAQAPPAQSTPTPGVAAAPTLVSGGGSTSSTSSGSFEASPVEPQLPSKEGPEPPEEVPPPTTPPVPKVEPKGDGIGPTRQPPSQGLGYPKYQKSLPPRFQRQQQEQLLKQQQQHQWQQHQQGSAPPTPVPPSPPQPVTLGAVPAPQAPPPPPKALYPGALGRPPPMPPMNFDPRWMMIPPYVDPRLLQGRPPLDFYPPGVHPSGLVPRERSDSGGSSSEPFDRHAPAMLRERGTPPVDPKLAWVGDVFTATPAEPRPLTSPLRQAADEDDKGMRSETPPVPPPPPYLASYPGFPENGAPGPPISRFPLEEPGPRPLPWPPGSDEVAKIQTPPPKKEPPKEETAQLTGPEAGRKPARGVGSGGQGPPPPRRESRTETRWGPRPGSSRRGIPPEEPGAPPRRAGPIKKPPPPTKVEELPPKPLEQGDETPKPPKPDPLKITKGKLGGPKETPPNGNLSPAPRLRRDYSYERVGPTSCRGRGRGEYFARGRGFRGTYGGRGRGARSREFRSYREFRGDDGRGGGTGGPNHPPAPRGRTASETRSEGSEYEEIPKRRRQRGSETGSETHESDLAPSDKEAPTPKEGTLTQVPLAPPPPGAPPSPAPARFTARGGRVFTPRGVPSRRGRGGGRPPPQVCPGWSPPAKSLAPKKPPTGPLPPSKEPLKEKLIPGPLSPVARGGSNGGSNVGMEDGERPRRRRHGRAQQQDKPPRFRRLKQERENAARGSEGKPSLTLPASAPGPEEALTTVTVAPAPRRAAAKSPDLSNQNSDQANEEWETASESSDFTSERRGDKEAPPPVLLTPKAVGTPGGGGGGAVPGISAMSRGDLSQRAKDLSKRSFSSQRPGMERQNRRPGPGGKAGSSGSSSGGGGGGPGGRTGPGRGDKRSWPSPKNRSRPPEERPPGLPLPPPPPSSSAVFRLDQVIHSNPAGIQQALAQLSSRQGSVTAPGGHPRHKPGLPQAPQGPSPRPPTRYEPQRVNSGLSSDPHFEEPGPMVRGVGGTPRDSAGVSPFPPKRRERPPRKPELLQEESLPPPHSSGFLGSKPEGPGPQAESRDTGTEALTPHIWNRLHTATSRKSYRPSSMEPWMEPLSPFEDVAGTEMSQSDSGVDLSGDSQVSSGPCSQRSSPDGGLKGAAEGPPKRPGGSSPLNAVPCEGPPGSEPPRRPPPAPHDGDRKELPREQPLPPGPIGTERSQRTDRGTEPGPIRPSHRPGPPVQFGTSDKDSDLRLVVGDSLKAEKELTASVTEAIPVSRDWELLPSAAASAEPQSKNLDSGHCVPEPSSSGQRLYPEVFYGSAGPSSSQISGGAMDSQLHPNSGGFRPGTPSLHPYRSQPLYLPPGPAPPSALLSGLALKGQFLDFSTMQATELGKLPAGGVLYPPPSFLYSPAFCPSPLPDTSLLQVRQDLPSPSDFYSTPLQPGGQSGFLPSGAPAQQMLLPMVDSQLPVVNFGSLPPAPPPAPPPLSLLPVGPALQPPSLAVRPPPAPATRVLPSPARPFPASLGRAELHPVELKPFQDYQKLSSNLGGPGSSRTPPTGRSFSGLNSRLKATPSTYSGVFRTQRVDLYQQASPPDALRWIPKPWERTGPPPREGPSRRAEEPGSRGDKEPGLPPPR
Protein: DNA mismatch repair protein (Q9N3T8)
Organism: Caenorhabditis elegans
Interaction partners:
- DNA mismatch repair proteins mutS family domain-containing protein
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein S5 domain-containing protein
- Proliferating cell nuclear antigen
- Exonuclease 1
- Flap endonuclease 1
- ERCC1-like central domain-containing protein
- DNA ligase 1
- DNA polymerase
- DNA ligase IV
Sequence:
MSKRQSSLMSFFTKTPKSEKPEEEVKEKSVEEPKSLKNDTPKISNDSEKKVLKRSNSKTVSSPVKTPRNASKRPKVVVCSSSEGEDDDGDEDFEMKEAEEHESSDESEADENASDCEVVESPESTPQSTPKRGGKKKISKPLLAENTPKSVKMAGKSKKVIPDGEAVSMAGVLDKMDKIMDGEGERKRIVEKTTGAKNKAVELEPAERFDHESFDFLKPDKIRDGFKRPMSDPEYDPKTLWVPPDFHQKQTPGHRQWWTMKSQHFDTILLFKVGKFYETYHMDAVEVVRALNIAFMRGSYAHAGFPEHAASKFADQLMNHGYKVARIEQTETPQMLEERNQKTKTKEKVVRREVCRVTSNGTRTYGVLDGVDLGSASSTLDPTAKHLLAIKEFHNPETGKSSYGVCMIDTTTAHIRIGQFEDDDYRSQLRTLLANVIVVQAIVERGSISSTTKSIINGILFSVPVEHLLPKKQFMTAEDVVRIVSNEDYYGSDASEWPEVLKGMLEDSSILPKPSTDWQLALSAFGAIFWYLRDSLIDVDMLSMRNVTIYNSNSMENDQKKEKIDWNGKNLILDGTALENLNIVPNGRDSHLTSLYYVINKCSTPFGRRLLRSWLLQPTCDPKKLEQRQKAIKWLVSPDASSFMTTATATLKKIPDLDRLLQKIHTIGLKYRSEKHPDSRAIFFDTIKTNQKKIAELLAAIDGFKLCNKLRKEYIKVQKEGEGCELLDELLGNEQEMEEVDENIYFFEKMFDRSTAMKDGKIVPNAGCDEEYDEALNRVKEALNELNDYKDSVAKKYSCSIKFVDSGKVKYLLEMPENTKVSSSFELKSRRKGFIRYSTPDSEQLVAALDAVEKEKSKLGDDATRRVFEQFGHKNPIWLETVKLVSSFDVLTSLALFAKSSPFEMCMPEFDFNATDPYLIVDKGVHPCLALQSRNEVTQTTSFIANSTTMGASEAAVMLLTGPNMGGKSTLMRQTAVLAILAHIGSMVPAFSMRLTPIDRIFTRIGANDRIMCGESTFFIELKETDIMLKNATKHSLLLVDELGRGTSTFDGTAIASAVLQKISDDLACRTFFSTHYHSICDSFTNHPNVRLAHMKCVVDKENNEDPTMEDVTFLYELESGICPKSYGFYAAKLAGIDHQVVRNAYLESNKFASNLIIDPKIRHLVECARDDNFDVGELKRMIEAI
Protein: Protein YOP1 (YIP1 partner protein 1) (YPT-interacting protein 2) (Q12402)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole. Induces high curvature in membranes and causes membrane tubule formation (Probable). Involved in membrane/vesicle trafficking.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11278413, ECO:0000269|PubMed:18442980}; Multi-pass membrane protein {ECO:0000269|PubMed:25646439}. Golgi apparatus membrane {ECO:0000269|PubMed:11278413}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein SEY1
- Reticulon-like protein 1
- Reticulon-like protein 2
- Peroxisomal membrane protein PEX30
- Protein transport protein YIP1
- Endoplasmic reticulum junction formation protein lunapark
- Nucleoporin POM152
- Peroxisomal membrane protein PEX29
- Nucleoporin POM34
- Nucleoporin NDC1
Sequence:
MSEYASSIHSQMKQFDTKYSGNRILQQLENKTNLPKSYLVAGLGFAYLLLIFINVGGVGEILSNFAGFVLPAYLSLVALKTPTSTDDTQLLTYWIVFSFLSVIEFWSKAILYLIPFYWFLKTVFLIYIALPQTGGARMIYQKIVAPLTDRYILRDVSKTEKDEIRASVNEASKATGASVH
Protein: Nr5a5 protein (Nuclear receptor subfamily 5, group A, member 5) (B3DKN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Rh50-like protein
Sequence:
MNISSYPLDPPQPSVHLAAEFTQDHASQERPSTSQELKPDPESSATQEEGCPVCGDRVSGYHYGLLTCESCKGFFKRSVQNNKRYTCAEAQNCPMDLAQRKRCPYCRFQKCVAVGMKKEAVRADRMRGGRNKFGPLYRRDRQLKQQRGTYHQANIAPYRVKIEGPQQLVPALPHDFHVINPNPASLGTDHYHPTQHFHPNMSQSEFPVLLDCTMPRDRTFSDPSLPIHTVCYPGIHGYPPDKREIPFNYNPASVTPPGPMSPTVLSTPAPTLTPASTPSSTPTPSQSLTPTSTTAPSSFFLNQLLQAEPDEKQLCMRVLASLQREQACRGKHDRLNTFSIMCKMADQTLFGLVEWARNCELFKELKVDDQMVLLQSCWSELLVLDHLCRQVAYGRDGSICLITGQQIEASTILSQAGMTLSSLVSRAQDLVTKLRSLQLDREEFVCLKYLVLFNPDVKSVQNRRQVEQTQERVNKALMDHTMQTHPGHSDKFGQLLLRLPEVRSISLQVEEYLYQRHLLGDLPCNSLLTEMLHAKHT
Protein: Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT 1) (TAT 1) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog 1) (Q9VSY4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
Interaction partners:
Sequence:
MVEFRFDIKPLFAQPIIKVTSNLLPNTFRGDRRQCLDATSKMTEIIDQLGQLSATSQGLSKPVTTAQRLRMSDNQTIYLLADNEAGHNGAVLGLLKVGTKNLYLFDEAGKTRMVEQTPSILDFYVHESRQRAGLGKRLFQTMLNEEQWTARKCSVDRPSEKLLSFLSKHYGLKRIIPQANNFVLYEGFFNDGESGNGGGNGHANGTPNGLHITNSPNTHLFGATYLGEDSNQRRGSQQQTTPNARLQQITQISPSGRYGAKRPTCSMAEIIHAGNSKGGNGNGSAEANSGNGNHDIPEIAEQLQRQSLADLEANSYEPEPEVEPEPEPEPEPEPEPEVITPPSPPPKSHTPTPPSVRSPEVAESIVGDNRRAPAFQLSKQHTGMKNRSFGVGMAVMPSSKMEFDQMEREDFGVVKINRPPGHEVTSPGQDNTDAMSTVSSGGGGLTDQGYYDLKFYHNKLW
Protein: Nuclear pore complex protein (A1YK58)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
Sequence:
MADSPFPRSSRSGLLRTTLNSSMAPQNLSHSLLILEKSNAEQNERSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQEAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARERESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTLGGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAPVREKRPLHALDEEDNLRLSRAIFELIRAGRVYDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRRDIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNGRMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRLAHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYGSVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVKEQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLNWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADEISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
Protein: Tryprostatin B 6-hydroxylase (EC 1.14.14.118) (Cytochrome P450 monooxygenase ftmP450-1) (Fumitremorgin biosynthesis protein C) (B9WZX1)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKPSHSDTPLMMPSVMKCGYLATAGLIGICTHLSYFRYGEHHLYPWRYVRFHLCLTMGVAALLYAKKPPQYTLCSMDLVKDVSLLMATYLVGLFASLLLYRTLFHPLRQIRGPWAAKISSFWLSFRLRRGPSFRILHELHEEYGPVVRVGPSEVSIIHPEAVRMIYGPNSRCSKNTFYDNGHPMMSLHSYRDRIAHDQRRRVWSAGFGDRALRGYEQRMRVYRQKLFQRLEARAVAESAINISQWFNFYSYDTMGDLAFARSFDMLDASRNHWAVDMLMHGMIGYRYLFPSWFFRLLATMPSLSSDWHKFIGFATDTMLRRVGEQVDVPDIFASLLAPLNGREPTEDERNMLMGDAMLIITAGSDTTATSLTSIVYELARHLDEVDKLRAELDPIEADSDGEYQHDTLAKLPHLNGFINETLRLHPPIPGVIPRKTPPEGIHVKDVFIPGNMTVFSPQWSMGRSEAAYIDPEIFNPERWYKHMDLVKDPSAFAPFSIGPYSCIGKPLALMNIRTTVARLIMSFDVRFPEGEDGIRWMDAADEHFAMGIHQMPVVLTRRH
Protein: Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Q389H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Ras-related protein Rab-7b
- Small GTP-binding protein RAB6, putative
- Small GTPase, putative
- Ras-related protein rab-5
- Small GTP-binding protein Rab18
Sequence:
MFNYRREVLLDLWRKMPEAAACETVAPPEAVKGEEKRQQSVVKTQLDWLSEELKLSSSIIQSDYKVYAAFVHRRWVFMQLRRLAESALGNVGKRSKPAAPAGCQLGECAAAGEFDLPEEVLFWAKALLKEKRQGDALLAMDERNFHAWEFRRWVMYQLGQMEDLFVQSSIQFGPAVVGIKEREFASYMNGSAKSDRPRDLFFTPTEVKELNFTSAAVRRNFSNYSAWHQRGFIMQGALRRLQQRQWREEEADNNLRDGMLSQAWGQLEEDLTLLTTAIYCDPLDQSAWYYAKFLIHASKQLTALPFASTAVPIDITAKLDEVCLDLVGEERRLGEDMETYWPYLHLATSLLTSIKKSNDGNSSDVISDRQSALKLAREVWAALQPQGRHVNGDDDCIKCLQELCAHLTTADPLRAGMYKYFLSEVTTA
Protein: Protocadherin 7 (E9Q2S0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLRMRTTGWARGWCLGCCLLLPLCFSLAAAKQLLRYRLAEEGPADVRIGNVASDLGIVTGSGEVTFSLESGSEYLKIDNLTGELSTSERRIDREKLPQCQMIFDENECFLDFEVSVIGPSQSWVDLFEGRVIVLDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELLQEPGGGGGSGEGRRLGPADSAPYPGGGGNSASGGGSGGSKRRLDAPEGGGGTSPSGRSSVFELQVADTPDGEKQPQLIVKGALDREQRDSYELTLRVRDGGDPPRSSQAILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRATDLDVGVNGQIEYVFGAATESVRRLLRLDETSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPSIEIRKIGRIPLKDGVANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDTEGDQNKKKYFLHTSAPLDYETTREFNVVIVAVDSGSPSLSSNNSLVVKVGDTNDNPPVFGQSVVEVYFPENNIPGERVATVLATDADSGKNAEIAYSLDSSVMGTFAIDPDSGDILVNTVLDREQTDRYEFKVNAKDKGIPVLQGSTTVIVQVADKNDNDPKFMQDVFTFYVKENLQPNSPVGMVTVMDADKGRNAEMSLYIEENSNIFSIENDTGTIYSTMSFDREHQTTYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPTVTLPRNISYTLLPPSSNVRTVVATVLATDSDDGINADLNYSIVGGNPFKLFEIDSTSGVVSLVGKLTQKHYGLHRLVVQVNDSGQPSQSTTTLVHVFVNESVSNATVIDSQIVRSLHTPLTQDIAGDPSYEISKQRLSIVIGVVAGIMTVILIILIVMMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQPFRRVTFSVVSQPQDPHQGSLQSCYDSGLEESETPSSKSSSGPRLGALPLPEDNYERTTPDGSVDSRPLPDVALTGKCTRECDEYGHSDSCWMPVRTSPERKKSQPKLSTFMPVDERGSQEKLANGEAAIMGDRNRNLLNKKLTSSYETFSAASFSKNEEANPEDIPLTKTGEYKPSPVNTLTRREVYL
Protein: SMP-30/Gluconolactonase/LRE-like region domain-containing protein (Q5ARV3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Gluconokinase
Sequence:
MLFKNASFLFPLVLPLGALASSGPGNGTSGFMTFQPGFKAILGEHPKLELLHENRTYPFAHEAPVYIPDTGDLFIVGNYQTPTGGQAIQISRMVPQKNGSYVREIIHPDIPMANGAINYNGGILFCDQGTKERPSSLIFMNATAPYETKVLLDSFYGRHFNSLNDLDVHSDGSIWFTDPTYGYDQGFSMKPDLPNQVYRFNPKTGDVRVVADQIGQPNGIAFSPDESIVYVTDTDAVWGNGDNDSTRPATIYAFDVKYYSGSPFLMNRRVFAYTDNGIPDGVKTDTEGNVYAGCGDGVHVWSPAGVLLGKIQLPGTSANLAFAKPGEMFALNEYRLWKVTLSQNVQGTILNEL
Protein: Proliferating cell nuclear antigen (PCNA) (P15873)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase delta small subunit
- Replication factor C subunit 4
- DNA polymerase eta
- Replication factor C subunit 2
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- DNA polymerase delta catalytic subunit
- DNA ligase 1
- ATP-dependent DNA helicase SRS2
- DNA repair protein REV1
- Replication factor C subunit 3
Sequence:
MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE
Protein: CBS domain-containing protein CBSX6 (Q8GZA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- CBS domain-containing protein CBSX3
- CBS domain-containing protein CBSX2, chloroplastic
- CBS domain-containing protein CBSX1, chloroplastic
- SNF1-related protein kinase regulatory subunit gamma-like PV42a
- CBS domain-containing protein CBSCBSPB3
- SNF1-related protein kinase regulatory subunit beta-3
- DUF21 domain-containing protein At4g14240
- CBS domain-containing protein CBSCBSPB4
- Putative DUF21 domain-containing protein At3g13070, chloroplastic
- Protein ILITYHIA
Sequence:
MASVFLYHVVGDLTVGKPEMVEFYETETVESAIRAIGESTECGIPVWRKRTTPSLPGFVENSEMRQQRFVGILNSLDIVAFLAKTECLQEEKAMKIPVSEVVSPDNTLLKQVDPGTRLIDALEMMKQGVRRLLVPKSVVWRGMSKRFSILYNGKWLKNSENSSSSSGLSADSTNRPTTSMTSSRDKFCCLSREDVIRFLIGVLGALAPLPLTSISTLGIINQNYNFIEASLPAIEATRRPLCDPSAIAVLEQTENEQQFKIIGEISASKLWKCDYLAAAWALANLYAGQFVMGVEDNMSSRSFSDFLQTSFPGGEQNGTATNAKKFSSRSIGFNPTSPTRLSIGRSMYRGRSAPLTCKTSSSLAAVMAQMLSHRATHVWVTEADSDDVLVGVVGYGEILTAVTKQPSAFVPSNRSYEGFGNENQS
Protein: Extracellular signal-regulated kinase 1 (ERK1) (EC 2.7.11.24) (MAP kinase 1) (MAPK 1) (Q5A1D3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcription factor CPH1
- Serine/threonine-protein kinase STE7 homolog
- Dual specificity protein tyrosine phosphatase CCP1
- Cyclin-dependent protein serine/threonine kinase inhibiting protein
- Tyrosine protein phosphatase
- Mitogen-activated protein kinase
- protein-tyrosine-phosphatase
- Cst5p
- Formin BNI1
- Rlm1p
Sequence:
MNIDQHHQLQQQHQQQMLQQQAQAQAQAQAQAQQQQQQQQQAAAAAAAANAAATTSSSPRQVSFNVSDHYQILEIVGEGAYGIVCSAIHKPSQQKVAIKKIEPFERSMLCLRTLRELKLLKHFNHENIISILAIQRPINYESFNEIYLIQELMETDLHRVIRTQNLSDDHIQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNSNCDLKICDFGLARSIASQEDNYGFMTEYVATRWYRAPEIMLTFQEYTTAIDVWSVGCILAEMLSGRPLFPGRDYHNQLWLIMEVLGTPNMEDYYNIKSKRAREYIRSLPFCKKIPFSELFANTNNNTSTSTSNTGGRTNINPLALDLLEKLLIFNPAKRITVEDALKHPYLQLYHDPNDEPISDKIPEDFFDFDKMKDQLTIEDLKKLLYEEIMKPL
Protein: PML nuclear body scaffold (A0A8I6ACX4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
VPSLTSLSLVHQQAIKEEFQFLRCPGCQTQAKCPKLLPCLHTLCSGCLEAPGLQCPICQAPGSANANAEALDNVFFESLQRRLAVFRQIVDAQAACTRCKELADFWCFECEQLMCGKCFDAHQWYLKHEARPLAELRDNSVREFLDSTRKSNIFCSNTNHRTPAQTNIYCRGCAKPLCCECALLDRNHSHLQCEIGKEIQQLHEELGTMTQALEEQGRTFDSAHAQMHSAIGQLDDARSDTEKQIRARVRQVIEHVQAQERELLEAVNVRYQRDYQEIAGQLGHLEAVLQRIRTGGALVKRMKLYASEQEVLDMHGFLRKALCRLRQEEPQNHKVQLRTSGFEEFKLCLQDLVSFITQRTDVAVAGRASPEAASTHPEAASAQPEAASTHPEAASAQPEAASAHPESASTPGNSTDLEQPKEVQRAQAQAMELSKTQPVAMVKSVPGAHPVPVYAFSMQGPTYREEASQTVSPMKRKCCHIDCCRKIIKMESTDENEDRLSTSSPEQPRPSTSKAISPPHPDGTSSTESTIPEKETPLPNNNHVASDAGETEERIVVISSSEDSDAENLPSHELDDSSSESSSIQLEGPNSLKALDESLAEPHLEDRTLVFFDLKIDNETQKISQLAAVNRESKFRVLIQPEAFSVYSKAVSLESGLQHFLSFLNSMHRPLLACPRLWGPGLPIFFQALNDINKLWEFQDAISGFLAVLPLIQERIPSASSFKLRNLAKTYLARNMSERSALAAVLAMRDLCCLLEVSPGLQLAQHIYSFSSLQCFASLQPLIQAQVLPQPEARLLALHNVSFLELLTAYRSNRQEGLKKYVHYLSLQTTPSSASTQIAQFLQALSAYMDGQLEGHIPAGAEGTALSLSGRAENKGCLA
Protein: N-acetyl-D-glucosamine kinase (EC 2.7.1.59) (GlcNAc kinase) (P75959)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Has also low level glucokinase activity in vitro.
Interaction partners:
- N-acetylglucosamine-6-phosphate deacetylase
- Putative N-acetylmannosamine-6-phosphate 2-epimerase
- PTS system N-acetylglucosamine-specific EIICBA component
- N-acetylmuramic acid 6-phosphate etherase
- Beta-hexosaminidase
- Probable bifunctional chitinase/lysozyme
- NAD-dependent protein deacylase
- Lipoprotein-releasing system transmembrane protein LolE
- Ribonuclease E
- RNA polymerase sigma-54 factor
Sequence:
MYYGFDIGGTKIALGVFDSGRQLQWEKRVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANVPAASGKPLRADLSARLDRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLIFNGKPITGKSYITGEFGHMRLPVDALTMMGLDFPLRRCGCGQHGCIENYLSGRGFAWLYQHYYHQPLQAPEIIALYDQGDEQARAHVERYLDLLAVCLGNILTIVDPDLVVIGGGLSNFPAITTQLADRLPRHLLPVARVPRIERARHGDAGGMRGAAFLHLTD
Protein: 5'-adenylylsulfate reductase 2, chloroplastic (EC 1.8.4.9) (3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43) (PAPS reductase homolog 43) (Prh-43) (Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 2) (APS sulfotransferase 2) (Thioredoxin-independent APS reductase 2) (P92981)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Assimilatory sulfite reductase
- Adenylyl-sulfate kinase 2, chloroplastic
- Adenylyl-sulfate kinase 1, chloroplastic
- ATP-sulfurylase 3, chloroplastic
- ATP sulfurylase 4, chloroplastic
- Adenylyl-sulfate kinase 4, chloroplastic
- ATP sulfurylase 2
- ATP sulfurylase 1, chloroplastic
- Adenylyl-sulfate kinase 3
- Sulfite oxidase
Sequence:
MALAVTSSSTAISGSSFSRSGASSESKALQICSIRLSDRTHLSQRRYSMKPLNAESHSRSESWVTRASTLIAPEVEEKGGEVEDFEQLAKKLEDASPLEIMDKALERFGDQIAIAFSGAEDVALIEYARLTGKPFRVFSLDTGRLNPETYRLFDAVEKQYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPIVQVDPVFEGLDGGVGSLVKWNPLANVEGADVWNFLRTMDVPVNALHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDGAADSKPAAVQEIFESNNVVALSKGGVENLLKLENRKEAWLVVLYAPWCPFCQAMEASYIELAEKLAGKGVKVAKFRADGEQKEFAKQELQLGSFPTILLFPKRAPRAIKYPSEHRDVDSLMSFVNLLR
Protein: Bax inhibitor 1 (BI-1) (Testis-enhanced gene transcript protein) (Transmembrane BAX inhibitor motif-containing protein 6) (P55062)
Organism: Rattus norvegicus (Rat)
Function: Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55061}.
Interaction partners:
- Desumoylating isopeptidase 1
- Bcl-2-like protein 1
- Serine/threonine-protein kinase/endoribonuclease IRE1
Sequence:
MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTRFIQAGLLSALGALALMICLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAINPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMFVSSLGNLFFGSIWLFQANLYMGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCIDLFLDFVTLFRKLMLILAFNEKDKKKEKK
Protein: Serine/threonine-protein kinase (EC 2.7.11.21) (Q5ABG0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mitosis inhibitor protein kinase SWE1
- Oxidant-induced cell-cycle arrest protein 5
- separase
- M-phase inducer phosphatase
- Kleisin alpha
- Tyrosine-protein phosphatase CDC14
- Cdh1p
- Rad21/Rec8-like protein N-terminal domain-containing protein
- Ras family GTPase
- Structural maintenance of chromosomes protein
Sequence:
MSALRSQPLQPLNSGQLNARANNITPVKSIRRPKENVQPTDQKQKKKKEKLSALCKTPPSIVRTRNGRDYRRGNFLGEGGFARCFQMKDASGQIYAAKTVAKASIKNEKTKTKLLSEIKIHKSLRHPNIVNFVDCFEDDVNVYILLEICPNQSLMELLKTRKRVSEPEVRFFMVQIVGAIKYLHSRRVIHRDLKLGNIFFDPEMNLKIGDFGLASVLPSTDSRKYTICGTPNYIAPEVLGGKNTGHSFEVDIWAIGIMMYALLVGKPPFQAKDVNVIYERIKKTEYYFPEDKPISESAKQLIKDLLSLNPLHRPTIDEILSYDWFKGPFPDKTYEVSLQTLPPGLDQITRAQSSANFKYAKDSAGIYTPKNKNPVEILRADLHSEQPRTLLPSSLSPNDTRNKYQEVDPGQLGRPRRVNFSSNFSTAIKRLNQVCFETYQTMRRLEHSRHDEVDASEFPNCENPTLISKWVDYSNKYGFSYQLNNDDIGVLFNDENTLLKRHNSDRFLELIYHENEGWTCIENSLANPPAQAKRQLEIVDFFAKYMNSNLSKVSEIEERKETVFLRRYTRTPDYIMFEMTNGNFQFNFKDHHKICISKTGLAITHISPGRLTQTQPLISVLKQGNFQHENVPDCMEKIMVIKEAIKKKAFKEA
Protein: DnaJ homolog shv (Protein shriveled) (Q9VPQ2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Maintains stem cell niche architecture in the testes. Activates an extracellular integrin beta-PS pathway which regulates DE-cadherin (shg) levels in somatic hub cells, and is essential for maintaining the number of germline stem cells and the structure and localization of hub cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:27191715}. Cell membrane {ECO:0000269|PubMed:27191715}. Secreted {ECO:0000269|PubMed:27191715}. Note=Secreted by somatic cells of the testes. Detected at the cell borders between the hub and germline stem cells, and between the germ and cyst stem cells. {ECO:0000269|PubMed:27191715}.
Interaction partners:
- Heat shock protein 83
- LD25575p
- Endoplasmic reticulum chaperone BiP
- GH07340p
- GEO10507p1
- Mesencephalic astrocyte-derived neurotrophic factor homolog
- Protein disulfide-isomerase A6 homolog
- GH21273p
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum protein 44, isoform A
Sequence:
MQLIKCLVIIQLSLLLVEESFAGRDFYKILNVKKNANTNEVKKAYRRLAKELHPDKNKDDPDASTKFQDLGAAYEVLSNPDKRKTYDRCGEECLKKEGMMDHGGDPFSSFFGDFGFHFGGDGQQQDAPRGADIVMDLYVSLEELYSGNFVEIVRNKPVTKPASGTRKCNCRQEMVTRNLGPGRFQMIQQTVCDECPNVKLVNEERTLEIEVEQGMVDGQETRFVAEGEPHIDGEPGDLIVRVQQMPHPRFLRKNDDLYTNVTISLQDALVGFSMEIKHLDGHLVPVTREKVTWPGARIRKKGEGMPNFENNNLTGNLYITFDVEFPKKDLTEEDKEALKKILDQSSINRIYNGL
Protein: PAR domain protein 1-epislon (PAR domain protein 1-epsilon) (Q9TVS7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPQSNAAAAAQLLXPVAMLPLLQRCSCKWQPGIEWECQWNGNAVVAATGNGNGGNPGQNNNNNNGNNSGNSNNNSNNNVSSVQHVANAVAAAVIANEHHNHLNSLKARFQPASSGKSTSNSKEIICPDDKYKEEGDIWNVEAQTAFLGPNLWDKTLPYDADLKVTQYADLDEFLSENNIPDGLPGTHLGHSSGLGHRSDSLGHAAGLSLGLGHITTKRERSPSPSDCISPDTLNPPSPAESTFSFASSGRDFDPRTRAFSDEELKPQPMIKKSRKQFVPDELKDDKYWARRRKNNIAAKRSRDARRQKENQIAMRARYLEKENATLHQEVEQLKQENMDLRARLSKFQDV