wanglab/gogpt-training-data huggingface dataset:
Protein: cDNA clone:J023066J03, full insert sequence (Q69WX7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELLKELVPGCSKVSGTALVLDEIINHVQSLQRQVEYLSMRLAAVNPRVDFGGLDNFLTTECGRITGLNYKNGMDLEQVTWPDMGVHGARNLMQLQQQFWHGDLAHPLQPPSQWEKRTDTNPPVFSNSSSSLFGYDLASSGAPAQTGNKLKTEL
Protein: Rho guanine nucleotide exchange factor 19 (Ephexin-2) (Weakly similar to Rho GEF 5) (Q8BWA8)
Organism: Mus musculus (Mouse)
Function: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase.
Interaction partners:
- Disheveled-associated activator of morphogenesis 1
Sequence:
MDCGPPATLQPHLAGPPGTARRPVAVCQQESLSFVELPPSRLCVDLFPIAPEELQAPGSRWSLATPAPLQGLLWPTSPGGPDTHIASTSGGMRPGRAGSWPHCPGAQPPTLVEPWSSQHMQPQRRASHSGSEKSAWRKMQVYHNEEATGTETPTGLLETGQAAQEQALCALEPGPQELSGNARGGLEAPERRRFSASELMTRLHSSLRLGRSTATRVLTSGSGAGAIREGKLPVRESRRAETRADSVSLPGPVDLNEVHGGLVEPRLDTQDKPTQDPSSATERRQSRFLLNSVLYQEYSDVASARELRRQQREEEGPGDGAEGAEEGPGPPRANLSPSSSFRAQRSTRGSTFSLWQDIPDVRGSGVLATLSLRDCKLQEAKFELITSEASYIHSLSVAVGHFLGSVELSECLGTQDKQWLFSKLPEVKSTSERFLHDLEQRLEADVLRFSVCDVVLHHCPAFRRVYLPYVTNQAYQERTYQRLLLENPKFPGILARLEESPVCQRLPLTSFLILPFQRVTRLKMLVENILKRTAPGSQDEDMATKAFSALKELVQECNASVQSMKRTEELIHLSKKIHFEGKIFPLISQARWLVRHGELVELAPLPAAPPAKLKLSSKAVYLHLFNDCLLLSRRKELGKFAVFVHANMAELQVRDLSLKLQGIPGHVFLLRLLHGQRARHQLLLRARTESEKQRWISALRPSSPQEDKEITCDGEDRPQVQCVRTYKALQPDELTLEKTDILAVKTRTSDGWLEGVRLADGEKGWVPQAHVVEISSLSARLRNLREYKRVSNASSKLGDPPA
Protein: Frizzled-8 (Fz-8) (hFz8) (Q9H461)
Organism: Homo sapiens (Human)
Function: Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1.
Subcellular location: Membrane; Multi-pass membrane protein. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalizes with GOPC at the Golgi apparatus. {ECO:0000250}.
Interaction partners:
- Proto-oncogene Wnt-3
- Proto-oncogene Wnt-1
- Low-density lipoprotein receptor-related protein 6
- Protein Wnt-11
- Protein Wnt-3a
- Low-density lipoprotein receptor-related protein 5
- Protein Wnt-2
- Tyrosine-protein kinase RYK
- Protein Wnt-5b
- Protein Wnt-4
Sequence:
MEWGYLLEVTSLLAALALLQRSSGAAAASAKELACQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERAKAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYNRTDLTTAAPSPPRRLPPPPPGEQPPSGSGHGRPPGARPPHRGGGRGGGGGDAAAPPARGGGGGGKARPPGGGAAPCEPGCQCRAPMVSVSSERHPLYNRVKTGQIANCALPCHNPFFSQDERAFTVFWIGLWSVLCFVSTFATVSTFLIDMERFKYPERPIIFLSACYLFVSVGYLVRLVAGHEKVACSGGAPGAGGAGGAGGAAAGAGAAGAGAGGPGGRGEYEELGAVEQHVRYETTGPALCTVVFLLVYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYSQYFHLAAWLVPSVKSIAVLALSSVDGDPVAGICYVGNQSLDNLRGFVLAPLVIYLFIGTMFLLAGFVSLFRIRSVIKQQDGPTKTHKLEKLMIRLGLFTVLYTVPAAVVVACLFYEQHNRPRWEATHNCPCLRDLQPDQARRPDYAVFMLKYFMCLVVGITSGVWVWSGKTLESWRSLCTRCCWASKGAAVGGGAGATAAGGGGGPGGGGGGGPGGGGGPGGGGGSLYSDVSTGLTWRSGTASSVSYPKQMPLSQV
Protein: Retinoic acid receptor beta (RAR-beta) (Nuclear receptor subfamily 1 group B member 2) (P22605)
Organism: Mus musculus (Mouse)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (By similarity). The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10826}. Cytoplasm {ECO:0000250|UniProtKB:P10826}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Retinoic acid receptor RXR-beta
- Mediator of RNA polymerase II transcription subunit 1
- Retinoic acid receptor RXR-gamma
- Retinoic acid receptor alpha
- Nuclear receptor coactivator 1
- Cellular retinoic acid-binding protein 2
- Arginine--tRNA ligase, cytoplasmic
- Nuclear receptor corepressor 2
- Retinoic acid receptor gamma
Sequence:
MSTSSHACPVPAVRGHMTHYPAAPYPLLFPPVIRGLSLPPLHGLHGHPPPSGCSTPSPASVGQACQRTTGGSQFAASTKWTPSLNAAIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNIAEHSPSVSPSSVENSGVSQSPLLQ
Protein: ribonuclease III (EC 3.1.26.3) (A0A0B4LFK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDMTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSKPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHYYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA
Protein: X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (Q6P7P8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
Interaction partners:
Sequence:
MAWSGNKAAVVLCMDVGVAMGNSFPGEESPLEQAKKVMTMFVQRQVFSESKDEIALVLYGTESTDNALAGKDQYQNITVHRHLMLPDFDLLEDIGNKIQPSSQQADFLDALIVCMDLIQRETIGKKFGKKHIEVFTDLSSPFSQDQLDIIICNLKKSGISLQFFLPFPIDKNGEPGETEDHDSSFDHCAPSFPQKGLTEQQKEGIHMVTRVMLSLEGKDGLDEIYSFSESLQQLCIFKKIERRSLPWPCQLTIGPNLSIRIVAYKSIVQEKFKKSWVVVDARTLKKEDIQKETVYCLNDDDETEVSKEDTIQGFRYGSDIIPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVHRRFFMGHQVLKVFAAKDDEAAAVALSSLVHALDELNMVAIVRYAYDKRANPQVGVAFPFIKDAYECLVYVQLPFMEDLRQYMFSSLKNNKKCTPTEAQLSAIDDLIDSMSLVKKNEEEDIIEDLFPTSKIPNPEFQRLYQCLLHRALHLQERLPPIQQHILNMLDPPTEMKAKCEIPLSKVKTLFPLTEVVKKKDQVTAQDVFQDNIEEGPAAKKYKTEKEEGHISISSLAEGNVTKVGSVNPVENFRVLVRQKIASFEEASLQLMSHIEQFLDTNETLYFMKSMDRIKALREEAIQFSEEQRFNSFLEGLREKVEIKQLNHFWEIVVQDGITLITKDESPGSSVTAEEATKFLTPKDKAKEDTTGLEEGGDVDDLLDMI
Protein: Proline dehydrogenase (EC 1.5.5.2) (A0A0G2K2S1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDLKWCLGSRVYFKAASPACVCPPFSVTRLFQVARKLLGQRMFERLMKMTFYGHFVAGEDQESIRPLIRHNKAFGVGFILDYGVEEDLSPEEAERKEMESCTSEAERDGSGANKREKQYQVHPAFGDRRDGVISARTYFYASEAKCDNYMENLLQCIEASGGASDGGFSAIKLTALGRPQFLLQFSDVLTRWRQFFHQMAAEQGQAGRPAVDTKLEVAVLQESIAKMGISSRAEIERWFTPETLGVSGTVDLLDWNSLIDSRTQLSRHLVVPNVQTGQLEPLLSRFTEEEEQQMKRMLQRMDVLAKRAREAGVRLMIDAEQSYFQPAISRLTLEMQRRFNVDKPFIFNTFQCYLKDAYDNVTIDMELSRREGWCFGAKLVRGAYMAQERARAVEIGYEDPINPTYEATNAMYHRCLNYVLEELKHSTKAEVMVASHNEDTVSFTLCRMKELGLHPADGQVCFGQLLGMCDQISFPLGQAGFPVYKYVPYGPVMEVLPYLSRRALENSSIMKGAQRERQLLWQELCRRLRTGSLFHHPA
Protein: At1g52420 (F6D8.36 protein) (Glycosyl transferase, putative) (Glycosyltransferase) (Putative glycosyl transferase) (Q9SSP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEEIRLSPLRQTSVKSSLSGRSTPRGTPRVYSGRTPRRGHGGGGAFQWFRSSRLVYWLLLITLWTYLGFYVQSRWAHDNESKVEFLRFGGRPRKDELYMEKIKGLDVVANENSEALVNITGKDDAGSNKRTDVSLIKKDDGVSRRSLSSKQKTRKTVRTSRSKIRVKQKVIKEVLETKDLDDEQDPQLPLTNATYGKLLGPFGSLEDKVLEWSPHRRSGTCDRKSDFKRLVWSRRFVLLFHELSMTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKTAMKADLIIAGSAVCTSWIDQYMNHHPAGGSQIAWWIMENRREYFDRAKPVLDRVKMLIFLSESQSRQWLTWCEEEHIKLRSQPVIVPLSVNDELAFVAGIPSSLNTPTLSPEKMRVKRQILRESVRTELGITDSDMLVMSLSSINPTKGQLLLLESIALALSERGQESQRNHKGIIRKEKVSLSSKHRLRGSSRQMKSVSLTLDNGLRREKQELKVLLGSVGSKSNKVGYVKEMLSFLSNSGNLSKSVMWTPATTRVASLYSAADVYVTNSQGVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSGNKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFVDVLVKCMRP
Protein: Galectin (J3KT17)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFSGCQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSCSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGTWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQTQTVIHTVQSASGQMFSTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRCGSCVKLTASRWPWMVSTCLNTTIA
Protein: CDK5 regulatory subunit-associated protein 3 (Q6IQA6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MENIQNLPIDIQTSKLLDWLVDRRHCTLKWQSAVMTIREKINAAIQDMPENEEIKQLLSGSYIHHFHCLQIIEVLKGTEASTKNIFGRYSSQRMKDWQEIVSMYEKDNVYLAEMASILVRNVSYEGPALRKQVSKAQQLQQELSRRELECQSGSADMRERYYAACKQYGIKGENVARELQAQVKDLPVVLEETGKKAACLKDAIEFYTAFTKFVSDWSEEVLPLLRFVQKKGNTTVYERKTGNVPKVVERPVMEEAPPDVVTEETIDWGDLGSGAGTGSEEVNFGISVEDGVDWGIGLESGTEETSGGGINWGDSESAPLEIEVVDVGTDCPDGVARGEDALSLLENSQTRSQFINELKELEMFLCQRLSEMREEGDLVAMSQFQLAPSVIQAQTPQRVQVMLADVRELLNGLTSVRMQHLFMIQASPRYVERVSELLRQKLKQADIMVLKRGTLAEKRQEALEEQAKLEPRIDLLAARTKELQKLIEADISKRYNNRPVNLMGVHV
Protein: Acyl-CoA thioesterase YbgC (EC 3.1.2.-) (P94842)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Thioesterase that may be involved in phospholipid metabolism. Displays acyl-CoA thioesterase activity with lauroyl-CoA (C12:0), myristoyl-CoA (C14:0), palmitoyl-CoA (C16:0), stearoyl-CoA (C18:0) and benzoyl-CoA, catalyzing the hydrolysis of the thioester bond. Has low activity with butyryl-CoA and octanoyl-CoA.
Interaction partners:
- Cytotoxicity-associated immunodominant antigen
- Uncharacterized protein HP_0495
- Malonyl CoA-acyl carrier protein transacylase
Sequence:
MRCRVYYEDTDSEGVVYHANYLKYCERARSEFFFKQNVLPENEEGVFVIRSIKADFFTPASLGQVLEIRTQIKELRKVFVVLFQEIYCIQNASLEPMKPFKVFASEIKFGFVNRSTYSPIAIPKLFKELLNAI
Protein: E3 ubiquitin-protein ligase RMA (EC 2.3.2.27) (Protein RING membrane-anchor) (RING-type E3 ubiquitin transferase RMA) (Q6NLR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein {ECO:0000256|RuleBase:RU369090}.
Interaction partners:
- At3g29270
- Probable E3 ubiquitin-protein ligase WAVH2
- SBP family protein
- E3 ubiquitin-protein ligase CSU1
- E3 ubiquitin-protein ligase RFI2
- Probable E3 ubiquitin-protein ligase RHA1A
- At5g18300
Sequence:
MSTSVQGETMDLDLNQEPSSDSESPGGLMTALSPMLEELESAQERIQERIRQLEVIVSRIREREITTTTTPALVSPNEHRDSTAGVIHERSRERLVENGENKTYLIAKALNMEKTSSVPGGFFDCNICLEKAEDPILTCCGHLFCWGCFYQLPLIYLNIKECPVCDGEVTDAEVIPIYGNGDDCDGTKPKLEDCGISLPPRPNAKRVESVRQKIINRGNPFFPGHENEAIEHIRRTIDSIGLQALAQGDEFGLTNIINNGGDNGGQQQQQQHHHHHHPPFGPLRLLPPYATFPGLLVDTSDIPAPFDDDAFDVDSFVDTTSLRRNRRRPSPAVRASYQRNRSNNASQTISFRLGSSASSAPREFAVPSSSIMTRSQTVNPTEVVTSSTSASSSRRRTEDVNNGPRTRSRRRLR
Protein: Uncharacterized protein (Q3USW8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAEMESAVEGRTASVLFAGFRALGLFSNEVPHVVRYSALKRRFYVTTCVGKSFHTYDVQKLSLVAVSNSVPQDICCMAADGRLVFAAYGNVFSAFARNKEIVHTFKGHKAEIHLLQPFGDHVISVDTDSVLIIWHIYSEEEYLQLTFDKSVFKISTILHPSTYLNKVLLGSEQGSLQLWNIKSNKLLYTFPGWKVGVTALQQAPAVDVVAIGLVSGQVVIHNIKYDETLMKFHQDWGPITSISFRTDGHPIMAAGSPCGHIGLWDLEDKKLINQMRNAHSTAISGLTFLHREPLLVTNGADNALRIWIFDGPAGEGRLLRFRMGHSASLTKIRYYGQNGQQILSASQDGTLQSFSTVH
Protein: Arylsulfatase I (ASI) (EC 3.1.6.-) (Q5FYB1)
Organism: Homo sapiens (Human)
Function: Displays arylsulfatase activity at neutral pH, when co-expressed with SUMF1; arylsulfatase activity is measured in the secretion medium of retinal cell line, but no activity is recorded when measured in cell extracts. Lacks arylsulfatase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:19262745}. Endoplasmic reticulum {ECO:0000269|PubMed:19262745}. Note=Localized in the intracellular granular structures.
Interaction partners:
- Arylsulfatase K
- Formylglycine-generating enzyme
- Arylsulfatase H
Sequence:
MHTLTGFSLVSLLSFGYLSWDWAKPSFVADGPGEAGEQPSAAPPQPPHIIFILTDDQGYHDVGYHGSDIETPTLDRLAAKGVKLENYYIQPICTPSRSQLLTGRYQIHTGLQHSIIRPQQPNCLPLDQVTLPQKLQEAGYSTHMVGKWHLGFYRKECLPTRRGFDTFLGSLTGNVDYYTYDNCDGPGVCGFDLHEGENVAWGLSGQYSTMLYAQRASHILASHSPQRPLFLYVAFQAVHTPLQSPREYLYRYRTMGNVARRKYAAMVTCMDEAVRNITWALKRYGFYNNSVIIFSSDNGGQTFSGGSNWPLRGRKGTYWEGGVRGLGFVHSPLLKRKQRTSRALMHITDWYPTLVGLAGGTTSAADGLDGYDVWPAISEGRASPRTEILHNIDPLYNHAQHGSLEGGFGIWNTAVQAAIRVGEWKLLTGDPGYGDWIPPQTLATFPGSWWNLERMASVRQAVWLFNISADPYEREDLAGQRPDVVRTLLARLAEYNRTAIPVRYPAENPRAHPDFNGGAWGPWASDEEEEEEEGRARSFSRGRRKKKCKICKLRSFFRKLNTRLMSQRI
Protein: Pcdh9 protein (B2RY66)
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:
MDLRDFYLLAALIACLRLDSAIAQELIYTIREELPENVPIGNIPKDLNISHINAATGTSASLVYRLVSKAGDAPLVKVSSSTGEIFTTSNRIDREKLCAGASYAEENECFFELEVVILPNDFFRLIKIKIIVKDTNDNAPMFPSPVINISIPENTLINSRFPIPSATDPDTGFNGVQHYELLNGQSVFGLDIVETPEGEKWPQLIVQQNLDREQKDTYVMKIKVEDGGTPQKSSTAILQVTVSDVNDNRPVFKEGQVEVHIPENAPVGTSVIQLHATDADIGSNAEIRYIFGAQVAPATKRLFALNNTTGLITVQRSLDREETAIHKVTVLASDGSSTPARATVTINVTDVNDNPPNIDLRYIISPINGTVYLSEKDPVNTKIALITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPKALHTLVLVFLYVNDTAGNTSYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQGIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQSQRRVTFHLPDGSQESYSDSGLGDHEPVGSGTLISHPLPLVQPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFNNGGHMADIPLANLKSYKQAGGTIESPKEHQL
Protein: Membrane cofactor protein (A0A024CBD6)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000256|PIRNR:PIRNR037971}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTSSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDTLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASPPKDAESLDGGIIAAIVVGVLAAIAVIAGGVYFFHHKYNKKRSK
Protein: Iron-sulfur cluster assembly transcription factor IscR (B7J5W8)
Organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Interaction partners:
- Iron-sulfur cluster assembly scaffold protein IscU
- 2Fe-2S ferredoxin
- Cysteine desulfurase IscS
- Co-chaperone protein HscB homolog
- Serine acetyltransferase
- Iron-binding protein IscA
Sequence:
MKLTTKGRYAVTAMLDLALNQRGGVVTVADISQRQQISVAYLEQLFGRLRRFGLVESVRGPGGGYRLAMPDSEIPLTRIVEAVNESISTTQCGGDPHLCCKGDGQQCLTHDLWEELGNRIAEFLGGITLGQLVQKQLHKELMQAAPIAMTDKTPLRETHDTA
Protein: Myocyte-specific enhancer factor 2D (Q14814)
Organism: Homo sapiens (Human)
Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15743823}. Note=Translocated by HDAC4 to nuclear dots.
Interaction partners:
- Myocyte-specific enhancer factor 2A
- Myocyte-specific enhancer factor 2B
- Histone deacetylase 4
- Nuclear factor of activated T-cells, cytoplasmic 2
- Calcineurin-binding protein cabin-1
- Histone deacetylase 5
- Nuclear factor of activated T-cells, cytoplasmic 1
- Nuclear factor of activated T-cells, cytoplasmic 3
- Myogenin
- Histone acetyltransferase p300
Sequence:
MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLTSAELSSLPAFSSPGGLSLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK
Protein: TLC domain-containing protein 1 (Calfacilitin) (Q96CP7)
Organism: Homo sapiens (Human)
Function: Regulates the composition and fluidity of the plasma membrane. Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity. Does not appear to have any effect on LCPUFA synthesis.
Subcellular location: Cell membrane {ECO:0000305|PubMed:30509349}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F1NZP5}.
Interaction partners:
Sequence:
MPRLLHPALPLLLGATLTFRALRRALCRLPLPVHVRADPLRTWRWHNLLVSFAHSIVSGIWALLCVWQTPDMLVEIETAWSLSGYLLVCFSAGYFIHDTVDIVASGQTRASWEYLVHHVMAMGAFFSGIFWSSFVGGGVLTLLVEVSNIFLTIRMMMKISNAQDHLLYRVNKYVNLVMYFLFRLAPQAYLTHFFLRYVNQRTLGTFLLGILLMLDVMIIIYFSRLLRSDFCPEHVPKKQHKDKFLTE
Protein: Cleavage and polyadenylation specificity factor subunit 5 (Cleavage and polyadenylation specificity factor 25 kDa subunit) (CPSF 25 kDa subunit) (Cleavage factor Im complex 25 kDa subunit) (CFIm25) (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) (Pre-mRNA cleavage factor Im 68 kDa subunit) (O43809)
Organism: Homo sapiens (Human)
Function: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides.
Subcellular location: Nucleus {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:9659921}. Cytoplasm {ECO:0000269|PubMed:19864460}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles (PubMed:15169763). {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 6
- Cleavage and polyadenylation specificity factor subunit 7
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage stimulation factor subunit 2
- Pre-mRNA 3'-end-processing factor FIP1
- Protein virilizer homolog
- Pre-mRNA cleavage complex 2 protein Pcf11
Sequence:
MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN
Protein: GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (Q51366)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Interaction partners:
- Alginate biosynthesis protein AlgA
- GDP-6-deoxy-D-mannose reductase
- Alginate biosynthesis protein AlgA
- Alginate biosynthesis protein AlgA
- Glycosyltransferase WbpX
- PslA
- Glycosyltransferase WbpY
- ABC subunit of A-band LPS efflux transporter
- D-rhamnosyltransferase WbpZ
- GDP-mannose 6-dehydrogenase
Sequence:
MTRSALVTGITGQDGAYLAKLLLEKGYRVHGLVARRSSDTRWRLRELGIEGDIQYEDGDMADACSVQRAVIKAQPQEVYNLAAQSFVGASWNQPVTTGVVDGLGVTHLLEAIRQFSPETRFYQASTSEMFGLIQAERQDENTPFYPRSPYGVAKLYGHWITVNYRESFGLHASSGILFNHESPLRGIEFVTRKVTDAVARIKLGKQQELRLGNVDAKRDWGFAGDYVEAMWLMLQQDKADDYVVATGVTTTVRDMCQIAFEHVGLDYRDFLKIDPAFFRPAEVDVLLGNPAKAQRVLGWKPRTSLDELIRMMVEADLRRVSRE