wanglab/gogpt-training-data huggingface dataset:
Protein: histone acetyltransferase (EC 2.3.1.48) (A0A0R4IPF2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cellular tumor antigen p53
- E1A-binding protein p300 b.
- Interferon regulatory factor 3
- Forkhead box protein O1-A
- Creb1 protein
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1-A
- Transcription factor 7-like 2
- Transcription factor 7.
- Transcriptional activator Myb isoform 1
Sequence:
MAENVLDVGPPNAKRAKLTAPAPDAPELGSLSWDDLENDLPDELIPNGDLGLMSLPSNGGAAGTGAHGPMVPDAAAKHKQLSELLRPGSSAGMNSVSPQPGGIGPQLGGLGKSPLGQGSPSHPSQTQKPGGTPGTQGNNAGSAGMGFNQGMLNSGMMGQNAGAQGGQVINGALGTVGRGRGVQGMYQGAAMQVASSVGAGGGVGAAAPGGAGSVLAETLTQGAQQMGINAQQAKMGMAGGNSPFGQYQAGGQQLGTNAQNKGALPNSLPPFPTDLKGATVTSVPNMPQQQQVSVGMVAGQGVSTGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGDVRACALPHCRTMKNVLNHMTHCQAGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASENANKHNQQPMLSPPNASLQTPIGSVGTGQQTAPALPSSTPIDPSSMRRAYAALGLPYSNQNPTQTQSPTQTQGPGQTTAQTPHQQPMRSINALGGGQLNPIGVPTSEQAKLLPDGTMPSTLNNPVMPDGSTVGNLSNLPTAAPLSATGVRKAWHEHVTQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANSRDEYYHFLAEKIYKIQKELEEKRRSRLQKQIINQTSMTATGQQPSALNQPNVMGPRPQNGPVPMPNVPNQILNRMQVSQGMNPFSAMSNVPMSQAPMGTRAASPINHQQINMNQVPTMNMSPTRIAPTQGMLGAHGGNMVTQTPNQTQFMTQPPFPATTNTMNVNMGQPNSQTPVSQQPNANLPLNALGPLGPALGCPTPPQAPLRATPPPNATAASTTNLPAALQPSTPTPAPAQATPPHMQTQAELPIPGQQHPGTPTGENRVPTPASAASTELHSQHAVPDVPPNDTKTEEQDYDMAVKTEPSTETEEDTGSLLVKKEEQEGSEAKQEPMETEDKKTDLKTETKEEDESKTNGTASSSPSQSRRKIFKPEELRQALMPTLESLYRQDPESLPFRQPVDPILLGIPDYFDIVKNPIDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKYCSKLAEVFEQEIDPVMQGLGYCCGRKYEFSPQTLCCYGKQLCTIPRDGTYYSYQNRYHFCEKCFNEIQGDSVTLGDDPAQPQTMISKDQFERKKNDTLDPEPFVECKDCGRKMHQICVLHYEVIWPSGFICDNCLKKSAKSRKENKFTAKRLQSTRLGTYIEDRVNKYLKRQNHPEAGEVFVRVVASSDKTVEVKPGMKAKFVDTGEMMEAFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPFPNTRRVYISYLDSIHFFKPRMLRTAVYHEILIGYLEYVKKLGYVTAHIWACPPSEGDDYIFHCHPADQKIPKPKRLQEWYRKMLDKAFAERILHDYKDIFKQATEDRLTSANELPYFEGDFWPNVLEESIKELEQEEEERKKEENTAACETPEGTPGDSKNAKKKNNKKTNKNKSSLSRANKKKPGMPNVANDLSQKLYATMEKHKEVFFVIHLHSGPIVNSLLPILDSDPLLNCDLMDGRDAFLTLARDKHWEFSSLRRCKWSTMCMLVELHNQGQDRFVYTCNECKHHVETRWHCTVCEDFDLCINCYNAKGHEHQMVKWGLGLDDDSSSQSGEASKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQLQHRLQQAQMMRRRMATMQGRAMPQSLPSPPASTAPSTPTSHQQPNTPQTPQPLPNQPTTPNAVVMSPTYPNTPRNGQPLPQASQGKPGPQASPLHQQQSPLPQPPQQQPPPQQPPQQQQQPPPMAVKMARHIEMVAQAQQNYRMTMNGLPMNHQQPRMPGAMQPPMQLVGPRGQQVMQPMPQGQWPGGAQPSMPAAQQQVAQQTPQGPQSTLPIQRPAMPQQVAQPRMMVPTQGPRPQAPQRAAGIAPNALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYHASQPQQQQPQQGIHAAQPAMQNMAAMQAVPRPGMAPQQQQQQPTPQGMAALGPQGQLMNPAPANNPQLQEMYRRQLLRHQQQQQQQQQQGGMPQAHGQFPQAQGTATNYTQLRMQQQQLAMQGTGGPMGQLPPMAQMAMDGTPNLLHQRNNLLLQQQQLPQQQVVLKPPMGSQAQPSPMSPQTHLLSGQPQGAHLPGQPMANALSNQVCSPGPVQSPRPPSQQPPPHSSPSPHVQPQPSPQHVPSHTGSPHPGLTTPMPGSMDQGHLGTPEQSAMLPQLNTPNRGGLPSDLNMVGDTTGDTLEKFVEGL
Protein: Dynein light chain 2B, cytoplasmic, putative (Q57YQ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain, putative
- Dynein light chain, putative
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Uncharacterized protein
Sequence:
MEFNASTTNERERRIKSVEEVLLRIAKHEGVVGYLVLNPADGRVMRYSGFSSDERKVKKYADKINGFTALAASTIRTIDWKDDLTFLRMGLGLTEILIAPDVNKQYVLIVVQEIRS
Protein: Regulator of G protein Signaling 21 variant 1 (Regulator of G-protein signalling 21) (V9GXQ3)
Organism: Mus musculus (Mouse)
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MPVKCCFYRSPTTETLAWSENMDSLLANQAGLDAFRTFLKSEYSEENVEFWLACEDFKKTECREKIATKAKTIYSEFIVADAPKEINIDFSTRDLISRNIAEPTPKCFDEAQKLIYSLMAKDSFPRFLKSEIYKKLVNSQQVGNHKRWLPFL
Protein: Dynamin-B (Q9U1M9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Enzyme hydrolyzing GTP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Mitochondrial division protein fszB
- Dynamin-like protein B
- Mitochondrial division protein fszA
Sequence:
MLSSTAILKASGDVAINYQQYIYPIIINKLSTLNYTIKNKKYYSQYKYSIQFQNEFQKNLKIYNNSNNNNNNNNNNKINKNNNNNNNNISKFFIQNNNIDKKVLRHFYSSTKLNYAKQQQQLFKNNETFNETVGASLLPIINKLQENAALIGSEITLPQIIVVGSQSSGKSSVLENLVGRDFLPRGSGLVTRRPLVLQLYQTTTTSRNNVNENEDEDEDDNYYDNDNDDNSLEEWGEFGHTGTNRFNFQEIKEEIERETERIAGPNKDISSEPIVLKIYSPKVVPLTLVDLPGLTRVAIEDQPPDIEEKIKSMIIDYISNPNSIILAITPANQDIVTSDALKLAQQVDPLGKRTIGVLTKLDLMDKGTDAIDILLGNSIPLSLGFVGVVNRSQQDINNRKPIEQMLADEWKWFDQHPVYHRITNQLGTKYLAQKCNKILTKHIRDTFPSVKNQIRQLIKKYESDLEKYGEPIPLRSAEKSRLLLDILNEFSRKYRADLDGTNEELILNEFNGGARIRYIFSKAFQSTTAAAATTSTDNSGGGEPFGWLSDQQLKIALRNSGSTMFIPQKIFDSLIRKQLERVREPLIQTSEIILDELIRILTQADYSHVLSRFPILKERIVEVSNNALRKLVKECNQSISQMVDAEMSFINTNHPNYLYQLNNLLFSSSSSSFVVPQGAFQSTSSTSSSPTSSSSSLPLPQNSNPYNDALNPYNIDRSYPIDNQIKQQQQQQQQQQQQSYQQQQQQQQKQQSGFLSRIFGSSSSPPSPPSPPQPKQQQSHEIQIQQQQQQQQQQHLKKQNLIFDDKFKLEQYGLNDITEDEKKQIYLLRRLLLAYNDIAQFNLQQNTMKLVSLLLIDKSKDILQKELIDSLYDQSSVDQLLRENELVVAKRNECIYKLDLLKKAKKSLSQSENSDLLHLY
Protein: Polycomb protein mes-6 (ESC homolog) (Maternal-effect sterile protein 6) (Q9GYS1)
Organism: Caenorhabditis elegans
Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. In association with the nfya-1-NF-Y complex, may play a role in repressing the expression of the homeobox protein egl-5 in tissues such as the head. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. The mes-2/mes-3/mes-6 complex may participate in the global inactivation of the X chromosomes in germline cells. The complex may act via methylation of histone H3 'Lys-27', rendering chromatin heritably changed in its expressibility. This complex is required to exclude mes-4 from the inactivated X-chromosomes in germline cells. Required for small-RNA-induced H3K27 trimethylation.
Subcellular location: Nucleus.
Interaction partners:
- Histone-lysine N-methyltransferase mes-2
- Polycomb protein mes-3
- Probable histone-binding protein lin-53
- Probable histone-binding protein rba-1
- E3 ubiquitin-protein ligase RING2 homolog spat-3
- Histone-lysine N-methyltransferase mes-4
- JmjC domain-containing protein
- PHD-type domain-containing protein
- Polycomb group RING finger protein 3 homolog mig-32
- Transcription factor che-1
Sequence:
MEHTKKFKSLNLHGFDRSTEDYGKRPFVLTAKLLEDQKKAIYGCAFNQYAGIDEEQAVATVGGSFLHMYSVPIDINNIELQWSCNFPTDKSSKVEREESLFTVTWCYDTYEAENDRNPFKVVTGGTLGHIYVIDYVSRKLSNRLRSVGWEINDIRTCPANSNLIVCASSDQSIRIHHIRNEACLIVIGGLECHAGTILSVDWSTDGDFILSCGFDHQLMEWDLSVKQVKEHLERACKALHQDKINVLTQSQDIPYVSKGTMRKSAVSRNIPDKEEDQLLELHRELIPRPSCLLPIYTPSSVSTDMHSDYVDCIRFLIGTNYALSKGCGNEKAIHFWRFGPPKGEVENRIHGNVLRPKSCTTKFRTMNVPSGSAWFIKFAVDPRRRWLVCGGAGGSVMFFDLRNNEETNPTHTCSVGSRTVRQASFSTCGRFLVLVTDEGFVCRFDRVSASVDAKDLAKF
Protein: Serine/threonine-protein kinase AGC1-7 (EC 2.7.11.1) (AGC serine/threonine-protein kinase subfamily 1 member 7) (Q1PFB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions redudantly with AGC1-5 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16973627}.
Interaction partners:
- Probable protein kinase At2g41970
- Serine/threonine-protein kinase-like protein At5g23170
- Rho guanine nucleotide exchange factor 8
- Serine/threonine-protein kinase-like protein At1g28390
- Probable LRR receptor-like serine/threonine-protein kinase At4g31250
- Rop guanine nucleotide exchange factor 2
Sequence:
MLTKPGKKLDSSESTHHTTSSNYPPLDIVHQTPQPRKEMQQKPLFDPKKMDNLIKPEPAGFTNHHRPNPSPKIPSSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPHTGGDIRWDAVNTLTSKGVQLGISDFRLLKRLGYGDIGSVYLVELRGTITYFAMKVMDKASLASRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCGGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVSPTLVKSSSVHAAGGGSGSSRPVGLIDEDAAVQGCIQPSTFFPRILQSSKKNRKAKSDFGLFVNGSMPELMAEPTNVKSMSFVGTHEYLAPEIIRGEGHGSAVDWWTFGIFIYELLYGATPFKGQGNRATLHNVIGQALRFPEVPHVSSAARDLIKGLLVKEPQKRIAYKRGATEIKQHPFFEGVNWALIRSATPPHVPEPVDFSCYASKDKESMAAVDGGGKKNNNGAGGGCSTGGGDNKPNGDCNDPDYIDFEYF
Protein: BTB/POZ domain-containing protein KCTD3 (Q8BFX3)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3) up-regulating its cell-surface expression and current density without affecting its voltage dependence and kinetics.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23382386}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
Sequence:
MAGGHCGSFAASAASSGEIVQLNVGGTRFSTSRQTLMWIPDSFFSSLLSGRISTLRDETGAIFIDRDPAAFAPILNFLRTKELDLRGVSINVLRHEAEFYGITPLVRRLLLCEELERSSCGSVLFHGYLPPPGIPSRKVTNTARSSVDARNGLNSMEGEARGNGTQPVLAGNGEDTIRLGVPVDPRKVLIVAGHHNWIVAAYAHFAVCYRIKESSGWQQVFTSPYLDWTIERVALNAKVVGGPHGDKDKMVAVASESSIILWSVQDGGSGSEIGVFSLGVPVDALFFIGNQLVATSHTGKVGVWNAVTQHWQVQDVVPITSYDTAGSFLLLGCNNGSIYYIDMQKFPLRMKDNDLLVTELYHDPSNDAVTALSVYLTPKTSVSGNWIEIAYGTSSGAVRVIVQHPETVGSGPQLFQTFTVHRSPVTKIMLSEKHLVSVCADNNHVRTWTVTRFRGMISTQPGSTPLASFKILSLEETESHGSYSSGNDIGPFGERDDQQVFIQKVVPITNKLFVRLSSTGKRICEIQAVDCTTISSFTVRECEGSSRMGSRPRRYLFTGHTNGSIQMWDLTTAMDMVNKTEDKDAGGPTEEELLKLLDQCDLSTSRCATPNISPATSVLQHSRLRESSSSLQLQHHETIHEAATYGATRPYRESPLLARARRTESFHSYRDFQTLNLNRSIERPVPENGHMGPAQTEVKGAAGECAMSERRSPGTEVRCGRESDGGLEVHRTAEGLSEPKKRSAEDENEHKVEFRKKGFEAGGFLGRKKVPYLASSPSTSDGGTDSPGTASPSPTKTTPSPRHKKSDSSGQEYSL
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial (Glu-AdT subunit C) (EC 6.3.5.-) (Protein 15E1.2) (O43716)
Organism: Homo sapiens (Human)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Cytochrome c oxidase subunit 5A, mitochondrial
- Asparaginyl-tRNA synthetase
- Cytochrome c oxidase subunit 7C, mitochondrial
- Glutamine--tRNA ligase
- Cytochrome b-c1 complex subunit 7
- Asparagine--tRNA ligase, cytoplasmic
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 9
Sequence:
MWSRLVWLGLRAPLGGRQGFTSKADPQGSGRITAAVIEHLERLALVDFGSREAVARLEKAIAFADRLRAVDTDGVEPMESVLEDRCLYLRSDNVVEGNCADELLQNSHRVVEEYFVAPPGNISLPKLDEQEPFPHS
Protein: SMN complex subunit yip11/gem2 (Gem-associated protein 2) (Survival of motor neuron protein-interacting protein yip11) (SMN-interacting protein yip11) (Yab8-interacting protein 1-a) (P0CU08)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins smb1, smd1, smd2, smd3, sme1, smf1 and smg1 that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (By similarity). In the cytosol, the Sm proteins smd1, smd2, sme1, smf1 and smg1 (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone saf5 (By similarity). To complete assembly of core snRNPs, the SMN complex accepts 5Sm from saf5 (By similarity). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of smd3 and smb1 to complete assembly of the core snRNP (By similarity). Within the SMN complex, yip11/gem2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound.
Subcellular location: Nucleus {ECO:0000269|PubMed:10749973}.
Interaction partners:
- SMN complex subunit smn1
- Small nuclear ribonucleoprotein Sm D1
- Uncharacterized protein new12
- Gem-associated protein 7 homolog
- Uncharacterized protein C16H5.15
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein E
- U2 small nuclear ribonucleoprotein A'
Sequence:
MPSKRKRNPLQYQTSGSLDEETNQRSAFPQIDNNSASESLEYDIPLDGLDYLATVREEARKLVPFVAARREPETRETIPLRKLEIEAGKKSFDPFLRYLLNIIDKEGERLEQYMESSSLDASILPKNLQQWRVYIEHKAPCWAILAVVDLATVLEILESLSSWLEKDAIDLQSQWIFCFCYKLPELLNGEDISTLRSVLKSLRSTHTSFPALQMSASALQAVLVYRYGQKDLFQT
Protein: C5a anaphylatoxin chemotactic receptor 2 (Complement component 5a receptor 2) (G-protein coupled receptor 77) (Q695P6)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Complement C5
- Complement C3
Sequence:
MLNDTTSKDYEYEYDQEQYSDLLNVPVDCPAGNCFSNDAYLIVLLGLYSVIFLVGVPGNTLLAWVTWKESRHRLGASWFLHLTMADLLCCVSLPFLAVPIAQKGHWPYGTAGCWLLSSITVLSMYASVLLLTGLSGDLFLLAFRPSWKNADQRTCGVRVVQVSSWMLALLLTVPGAVYRKLLQEHYPPRLVCGTNYGGSVTAEVTITTVRFLFGFLVPLVFMASCHGILQRQMARRHWPLGTAVVVGFFICWTPFHLLRVIIAVASSHSPLLAWALEAEPLVTGLALAHSALNPIMFLYFGRKQLCKSLQAACHWALRDLQDEEESAVTKVSTSQEMVSEMPV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (D3ZZQ0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHGQRPATEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLANKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQEREQRRHYEEQMRREEERRRAEHEQEYKRKQLEEQRQAERLQRQLKQERDYLVSLQHQRQEQRPLEKKPLYHYKEGMSPSEKPAWAKEVEERSRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPQLVAVKSQGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSSWLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPVLESSLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERTRVRANSKSEGSPVLPHEPSKVKPEESRDIPRPSRPADLTALAKELRELRIEETNRPLKKVTDYSSSSEESESSEEEEEDGESETHDGTVAVSDIPRLIPTGAPGKNEQYNMGMVGTHGLETSHADTFGGSISREGTLMIRETAEEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDTGAEYGMGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAAALFTSELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGDLEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVEEGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVGIFCIRAIWRK
Protein: Sex-determination protein fem-3 (Ce-FEM-3) (Feminization of XX and XO animals protein 3) (P34691)
Organism: Caenorhabditis elegans
Function: Required for male development. In XO (male) animals, fem-3 directs male differentiation in all tissues. In XX (hermaphrodite) animals, it specifies the first 80 or so germ cells to be sperm. Negatively regulates male development when bound to tra-2. Together with fem-2 associates with the CBC(fem-1) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of tra-1.
Interaction partners:
- Protein phosphatase fem-2
- Sex-determining protein fem-1
- Sex-determining transformer protein 2
- Fem-3 mRNA-binding factor 2
- Sex-determining transformer protein 1
- F-box domain-containing protein
- Cullin-2
- Anti-proliferative protein domain-containing protein
- Female germline-specific tumor suppressor gld-1
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-1
Sequence:
MEVDPGSDDVEADRETRAQKLKLKRNVKFRAQMRRFDEYCGVTNLTVDDLNWPLISGIPLQRQRLTGATYYDDSLLDQNPWDEFSIDRFLEITSIQLITAGAGYERNDEITRFVFQRTMKTIVTYCNFMYDLARRNGKVQITRFELQDLIHRDEFRFYMYFRQFLPNPDPNCTAFSNHYTSLLHTLYFNIPGMPQFWNNSQMYNYAATRGQRLVQNIAAFYPPEYFWNEDESKYHTTFVVPRGTEFSKFYARRFHEALGMPPLENEIITVLDWLAKLCILEIVYHTTIWCDITGFGGLPRIEHYRLAMENVEDIIFDLAIDDFSISRLQLQISPFEISRYSPLDVSGYYETIKRKKDIEEYQNRFYEVHYSDDVRIMNVYATDCSRKR
Protein: Isoleucine--tRNA ligase, putative (EC 6.1.1.5) (Q8I5G6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Proline--tRNA ligase
- Proline--tRNA ligase, putative
- leucine--tRNA ligase
- leucine--tRNA ligase
- glutamate--tRNA ligase
- glutamine--tRNA ligase
- glutamate--tRNA ligase
- tRNA import protein tRIP
- Phenylalanine--tRNA ligase beta subunit
- arginine--tRNA ligase
Sequence:
MFKYGNFIVIIFLIFLSLIIELYLSLHIQKKHIPLDNKNNSFLQFINSEHYKYKHNNKYQLNQHKKNIKDVIKESINLPLQFLPTTYNSLDRQKFIQQFWNCKEIYEKRNFENIKKHIYNNGNNTKQSKYIQHNNTQSCNEHNILNKKKKKEKETYSDVMETKNSHLIKELIEKKKKLISKIDDNNNNNNRKHIFKYIKTKDYINCHNGNHLINKFENIIYEKIKNEKYLKKNKKEILLKLYNKILNKIKIIHDGPPYANNDIHIGHILNKVIKDIYLKYFLFQNYFVLLIHGFDTHGLPIEYNVMKLLKINHIQDLNLNSSYIHNQNESLKNEHVFFKSYINLLNKLKNQHKKKKQISFLSNIFEKNNIISKDTIEQQKISTFKNLCKSYASYFVNEQFMSLVSYGIWGYWNYTYITFYKFYEQIQNKVFRDLLKNKYIYMSNRPIYHSYATKTVLSDSEIIYKKRVCNSFYFFYTFFKISDTFLLHLLKEFKENKAINEILEFNQDDVTYFLENYSLVINEIIKNNKENNEGKNILNGNDLFNETNSNDSYLEGQHISNYILKLKNQIIEKIIKKVKILVLTTQMHTIFNNKCLLIHEKYLYRIIHLKYEDEKENQFFIICDKSYNSFSDNLTKYYSKKSPIKEIKNICTFQGNSFMSCTYKNFTNNEENNFIFVSDNEIKESFGTGIVHVAPSHGFTDYNFYYKNNKLKKIYLDISNYQEIEEKKQTRDNNKINISCNDMKAEVSKKIFNENYFIKNNSLSLDVINENVMDENDDLKDEYTELVYKNLEKNIHFIKKYETPSNAQSLLNSLDIMKKKTKKLNINEKDIHSLFFYSFYENILFYFPYEHSYTYDWRSHTTVQIKSLLQIYVDIDKIKNNIPFYQSIKNIHFINKHVKNNLIKTIKDRNEWCISRQKYWGVNIPLKDIELDQNQKIIFNNQIMDVWFDSSVSYIYVLYMCKHILFHTYFNKIWKSVKNYNNTYQKGKGKYKNKINYNNKNENKLSFNIYDVYDQIMNHDEYNIRSMENKDNILLKNILQKKKIFDTSKMYKWINKQIQKGQQKKYYSFQWNSIKDIVFSKNNKKEFFKKHFNIFLCCEGIDQIRGWFQSFFFVFFCLNWINQRKKTRSQLLKNTDKIIDKKGVVIIKREQIKNNIKHYTLNNNNNNDNNNNNNNSIFSDDSLCFNNTSSIETNSKRLPSHSYLPIKNVIVHNYVVDSNNIKMSKSLNNVISPRELFFEKEKDDIPTTSKRKDTQKPDDLNKNTDINNKGNINNNVNNNNDILMKTGKQIDLIKKKNKNKDLNKRFNADIVRLWVCCYNFVNRNISISYEILENINKYIYLKLYNTFKFIMNNIYDLNFDGTKDNMKIKWDNIQMIDKFILYKKDNLIKHCTKAYKNFQLQLLIKYIMNFIYTDLAIYIDYSKDRLYIHEKNSLNRTNCQKILYKILRDLIILLGPIVPHLSEDIYYNLQLLKNKTKRKYMTTHNNNNNNISINEGKIKSLFLRPFPKFKNYKQVNLDTLFLIKYYIHKQISPYFSNSLQAIVYIFSNNDNIINLIKSFLRTPDPLEQFNNYDDLRFLFNVSNIFICDNICQVEEKDKNYKTYKIPLPNINEKNQIKNKNKNKKKNLNDFFQPNQKPIVDHMLNFDENIEHAIISIGINKTESKRCSRCWMYGTVYSFEGEYFCPRCLNVIKSHYN
Protein: Pleckstrin homology domain containing A1 (Q5RGS4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPYVDRQNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIKITVPKQSDSQPNSDNLSRHGECGKKQVSYRTDIVGGVPIITPTQKEEVNECGESIDRNNLKRSQSHLPYFTPKPPQDSAVIKAGYCVKQGAVMKNWKRRYFQLDENTIGYFKSELEKEPLRVIPLKEVHKVQECKQSDIMMRDNLFEIVTTSRTFYVQADSPEEMHSWIKAVSGAIVAQRGPGRSASSMRQARRLSNPCIQRSIPPVLQNPNTLSVLPTQPPPPHIPQPLAATLWSQPLPWRSEDFTSLLPRSSQGTSRSRLSLQENQLPK
Protein: Multiplexin, isoform U (X2JCL0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVLQGVMFALAMICTLLVPVLGSFELVGQSIKDALAEYTLTDIMNNNQFAGIEFGEAEDGFPAFRFLQTADVKSPYRMLLPEKLYEFAILITFRQSSLKGGYLFSVVNPLDTVVQLGVHLSPVVKNSYNVSLVYTQADQNIGRKLASFGVAHVPDKWNSIALQVLSDKVSFYYDCELRNTTLVTREPIELVFDSASTLYIGQAGSIIGGKFEGYLEKINVYGNPDAINVTCMPPPKATIAPTTAATDIFDASGMQPPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNESLRESLRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGPPGLPENYDESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: CapZ-interacting protein (Protein kinase substrate CapZIP) (RCSD domain-containing protein 1) (Q6JBY9)
Organism: Homo sapiens (Human)
Function: Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly.
Interaction partners:
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit beta
- MAP kinase-activated protein kinase 2
- MAP kinase-activated protein kinase 3
- F-actin-capping protein subunit alpha-2
- Mitogen-activated protein kinase 12
Sequence:
MEERPAETNANVDNSASPSVAQLAGRFREQAAAAKETPASKPTRRKPPCSLPLFPPKVDLGQNGEEKSPPNASHPPKFKVKSSPLIEKLQANLTFDPAALLPGASPKSPGLKAMVSPFHSPPSTPSSPGVRSRPSEAEEVPVSFDQPPEGSHLPCYNKVRTRGSIKRRPPSRRFRRSQSDCGELGDFRAVESSQQNGAKEEDGDEVLPSKSKAPGSPLSSEGAAGEGVRTLGPAEKPPLRRSPSRTEKQEEDRATEEAKNGEKARRSSEEVDGQHPAQEEVPESPQTSGPEAENRCGSPREEKPAGEEAEMEKATEVKGERVQNEEVGPEHDSQETKKLEEGAAVKETPHSPPGGVKGGDVPKQEKGKEKQQEGAVLEPGCSPQTGPAQLETSSEVQSEPAVPKPEDDTPVQDTKM
Protein: Protein unc-13 homolog (Protein PROTON ATPASE TRANSLOCATION CONTROL 1) (Q8RX56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Controls the tethering of the proton ATPase AHA1 to the plasma membrane. Is essential for stomatal opening in response to low concentration of carbon dioxide and light.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23896897}. Cell membrane {ECO:0000269|PubMed:23896897}; Peripheral membrane protein {ECO:0000305}. Note=Translocates reversibly between the cytoplasm and the plasma membrane depending on environmental conditions. {ECO:0000269|PubMed:23896897}.
Interaction partners:
- Kinetochore protein SPC24 homolog
- Protein CELLULOSE SYNTHASE INTERACTIVE 1
- Serine/threonine/tyrosine-protein kinase HT1
- Protein DETOXIFICATION 56
- ATPase 1, plasma membrane-type
- Guard cell S-type anion channel SLAC1
- Exocyst complex component SEC5B
- Exocyst complex component SEC6
- Exocyst complex component SEC10a
Sequence:
MEEENAVEILQRYRRDRRKLLDFMLAGSLIKKVIMPPGAVTLDDVDLDQVSVDYVINCAKKGGMLELAEAIRDYHDHIGLPYMNSVGTADEFFLATIPESSGSPPKRAPPPIPVLISSSSPMVTNPEWCESPSAPPLMRSESFDSPKAQELTVDDIDDFEDDDDLDEVGNFRISRRTANDAADLVPRLPSFATGITDDDLRETAFEILLACAGASGGLIVPSKEKKKEKSRSRLIKKLGRKSESVSQSQSSSGLVSLLEMMRGQMEISEAMDIRTRQGLLNALAGKVGKRMDSLLVPLELLCCVSRTEFSDKKAYLRWQKRQLNMLAEGLINNPVVGFGESGRKATDLKSLLLRIEESESLPSSAGEVQRAECLKSLREVAISLAERPARGDLTGEVCHWADGYHLNVRLYEKLLLCVFDILNDGKLTEEVEEILELLKSTWRVLGITETIHYTCYAWVLFRQYVITSERGLLRHAIQQLKKIPLKEQRGPQERLHLKTLKCRVDNEEISFLESFLSPIRSWADKQLGDYHLHFAEGSLVMEDTVTVAMITWRLLLEESDRAMHSNSSDREQIESYVLSSIKNTFTRMSLAIDRSDRNNEHHLALLAEETKKLMKKDSTIFMPILSQRHPQAIAFSASLIHKLYGNKLKPFLDGAEHLTEDAVSVFPAADSLEQYLLELMTSVCGEDTSGPYFKKLIPYEVESLSGTLVLRWINSQLGRILSWVERAYKQEHWDPISPQQRYGSSIVEVFRIVEETVDQFFALKVPMRSIELSALFRGIDNAFQVYTNHVMEKLASKDDLVPPVPVLTRYKKETAIKVFVKKELFDSKHLDERRSINIDVPATAMLCVQLNTLHYAVSQLSKLEDSMWLRWIAKKPREKIVIRKSMVEKSKSFNQKESFEGSRKDINAALDRICEFTGTKIIFCDLREPFIENLYKPNVSQSRLEGLIEALDTELGQLCSVIMEPLRDRIVTSLLQASLDGLLRVLLDGGASRVFHPSESKLLEEDVEVLKEFFISGGDGLPRGVVENQVARVRLVVKLHGYETRELIDDLRSRSSLEMQQGGKGKLGADTQTLVRVLCHRNDSEASQFLKKQYKIPRSHG