wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase Arkadia (EC 2.3.2.27) (RING finger protein 111) (hRNF111) (RING-type E3 ubiquitin transferase Arkadia) (Q6ZNA4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP. In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL. Associates with UBE2D2 as an E2 enzyme. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates. Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair. Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:23751493}. Cytoplasm {ECO:0000269|PubMed:16601693}. Nucleus, PML body {ECO:0000250|UniProtKB:Q99ML9}. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol. {ECO:0000269|PubMed:16601693}.
Interaction partners:
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 3
- Ski-like protein
- Axin-1
- Mothers against decapentaplegic homolog 2
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Ski oncogene
- Axin-2
- E3 ubiquitin-protein ligase SMURF2
Sequence:
MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
Protein: Ras homolog family member C (Ras homolog gene family, member C) (B2RYP0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGCPIL
Protein: Nicotinic acetylcholine receptor alpha5, isoform B (Nicotinic acetylcholine receptor alpha5, isoform D) (Nicotinic acetylcholine receptor alpha5, isoform H) (Q7KT97)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MKNAQLKLTEVDDDELWLAVRLAHCSSNISSSSSTRTTSSNKRHNQQLTTLQPRSLSTKHHSNIASEQHNSQQQEPASKDEDVANHGRSNDQQTHLQQLDSSNMLSPKTAAAATAAGDEATTQQPTNIRLCARKRQRLRRRRKRKPATPNETDIKKQQQLSMPPFKTRKSTDTYSTPAAITSCPTATYMQCRASDNEFSIPISRHDRVSTATFAWVLHVLQVLLVSLQQWQLHVQQRSVLLFRRIAASTIAFISYLGSFAAQLRSSSSSSSNSSNSGNSSSTQILNGLNKHSWIFLLIYLNLSAKVCLAGYHEKRLLHDLLDPYNTLERPVLNESDPLQLSFGLTLMQIIDVDEKNQLLVTNVWLKLEWNDMNLRWNTSDYGGVKDLRIPPHRIWKPDVLMYNSADEGFDGTYQTNVVVRNNGSCLYVPPGIFKSTCKIDITWFPFDDQRCEMKFGSWTYDGFQLDLQLQDETGGDISSYVLNGEWELLGVPGKRNEIYYNCCPEPYIDITFAIIIRRRTLYYFFNLIIPCVLIASMALLGFTLPPDSGEKLSLGVTILLSLTVFLNMVAETMPATSDAVPLLGTYFNCIMFMVASSVVSTILILNYHHRNADTHEMSEWIRIVFLCWLPWILRMSRPGRPLILEFPTTPCSDTSSERKHQILSDVELKERSSKSLLANVLDIDDDFRHNCRPMTPGGTLPHNPAFYRTVYGQGDDGSIGPIGSTRMPDAVTHHTCIKSSTEYELGLILKEIRFITDQLRKDDECNDIANDWKFAAMVVDRLCLIIFTMFTILATIAVLLSAPHIIVS
Protein: Ubiquitin domain-containing protein (Q54JN7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Chloride channel protein D
- MAP kinase phosphatase
Sequence:
MMAHRNIAPKFSSLKLVSLNHLSDHFKQDVNNNNNNSGSSNNNNNIQSYDQESNIHQPLLLKLKFRDNEEFNYTIKVTTGETVQTTKKLISDKLSIKQSFISFYLEGKQMIDPLSYNDFHQIKNQKLDSIDIDILIIGEFNRDDVLKYIREENEGMDSITTSMSNTSISYTSGTTLTTPSTLTNNNNNNSNNNNNNNNNNTTTTCNNNNSNNNNNNNNNNNNNKKNEESVVTNSCSAPSSVNSMSPILNSASSSSDISLGGRVNGTNSKPIISLRRHSVNVHVEQEESSPSSQPQTVNSSPSSPYSTRKIVINGGGSPNTNSGNNNNNPSPSKQQPPHSFSLIPPICEETFESNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNNNNIASISPLSSSPNVSSLTPLSSSPNVSTSSSFSSPKQPLSPKSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTNNVNSNHISNSNSNSSGSLSISHHKKTHLRINSITADLSMTRERDSSFSSNHNVNNNNNNNNNNNNNNNNNNNNNNNNNNPSNVNSSNTTNNLLSPTTFSRLEIYDISNHNNNNDNNNNNTGHILINTNNNCNETINNGVIN
Protein: Secretoglobin, family 3A, member 1 (A0A8I6AB14)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPPQSARHSVAFFVESLAKPVVEPVAALAPAAEAVAGAVPSLPLSHLAILRFILASLGIPLDPLIDGSRKCVTELGPEAVGAVKSLLGALTTFG
Protein: Tax1-binding protein 3 (Glutaminase-interacting protein 3) (Tax interaction protein 1) (TIP-1) (Tax-interacting protein 1) (O14907)
Organism: Homo sapiens (Human)
Function: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6.
Subcellular location: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the cell membrane by interaction with membrane proteins.
Interaction partners:
- Catenin beta-1
- PDZ domain-containing protein GIPC1
- tRNA N
- Suppressor of cytokine signaling 1
- Transforming protein RhoA
- Inward rectifier potassium channel 4
- Rhotekin
Sequence:
MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS
Protein: Smox protein (B1H229)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAARALLEQGFTDVTVLEASSHIGGRVQSVKLGHATFELGATWIHGSHGNPIYQLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNRGRRIPKDVVEEFSDLYNEVYNLTQEFFRNGKPVNAESQNSVGVFTREKVRNRIRDDPDDTEATKRLKLAMIQQYLKVESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAKGIPPHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDAGEGGQSGENPQQGRWDEDEQWPVVVECEDCEVIPADHVIVTVSLGVLKRQYTSFFRPCLPTEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESCTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEALVMERCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKTAVSGL
Protein: Protein mesA (Q5BGR2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for the formation of actin cables at hyphal tips. Involved in establishment and maintenance of hyphal polarity axes. Stabilizes the localization of the formin sepA at sites of polarized growth.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:15155805}. Note=Localizes to hyphal tips and sites of branch emergence.
Interaction partners:
Sequence:
MSIPLPIRTSDGTGNLSSSPPKSNGLPRLSPSPSFVQKHSPRSSDTSGLRRSASHHNARQTFKQRRCKSQYPRDSPERHVEFILVASFHIDRGPIMEHQYPGPISSDEGMLAELMLPDQTHVRSQDWTIFFLPLDTGGEGEEDDLAGENNKRKGKRNRVRSSSGDEGTSADTNNESEVTEEEESSDEEDGGEGPPLMYVLNLVNTKQDNTVKRGAVVKAMAICTRHSFLHIYKPILLLALEDYFKNPYPETLETLYNAVNAMDLSPMPKLNLLERQILQATNSKDMFIEKFEQMVQQRAIEDGENDIDEDNPPSPRRGTAPRYTLPRDTHEFESKIIYNDIPIPVKVPTVIWPEIVGDFSLVKLIQIFSAPHAASPQPFPLHPHLTTSGPLTHPIIVLVNAMLTQKRVVFLGHNRPSGEVAEAVLAACALASGGILRGFTRHAFPYTDLTKIDDLLRVPGFIAGVTNPTFANHPEWWDVLCDLPTGRIKISNHIEPAPVTDGQLYFQQQSPVSASGPNADPTGDNLFMEDVLRSIANRYGENAIRAKWRAYITKFTRVAAAFEETVYGASNIYIIGPNEELSPDSPSGLQSDPGDPTTIRGHGYVWPDEASKQRELMASVSRIEGWRTTRSYYSFIQDIAAMYWPSRPIQKPDLHHHHDRLRTLKLSAYEAGAIYLAFAHAIKDYAGICQLLTVTPESQAGLFYLSMGLLHPDRNVREATADLLERIALHPAGRHFWAQLNRFAKTAYFRIKREKEAAGNSSPIVKSPSDSFGPQQSLVGVAISGVHSQGS
Protein: High osmolarity signaling protein SHO1 (Osmosensor SHO1) (Suppressor of SUA8-1 mutation) (Synthetic high osmolarity-sensitive protein 1) (P40073)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway.
Subcellular location: Cell membrane; Multi-pass membrane protein. Bud. Bud neck. Cell projection. Note=Localizes at the tip of the mating projection during conjugation.
Interaction partners:
- Serine/threonine-protein kinase STE11
- MAP kinase kinase PBS2
- Protein STE50
- Cell division control protein 42
- Signaling mucin MSB2
- Mitogen-activated protein kinase HOG1
- Osmolarity two-component system protein SSK1
- MAP kinase kinase kinase SSK2
- Cell division control protein 24
- Signaling mucin HKR1
Sequence:
MSISSKIRPTPRKPSRMATDHSFKMKKFYADPFAISSISLAIVSWVIAIGGSISSASTNESFPRFTWWGIVYQFLIICSLMLFYCFDLVDHYRIFITTSIAVAFVYNTNSATNLVYADGPKKAAASAGVILLSIINLIWILYYGGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGNRNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLHLNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDNFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDGPEEMHR
Protein: Cysteine proteinase inhibitor 1 (AtCYS-1) (Q945Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in suppression of hypersensitive cell death activated by either avirulent pathogen or oxidative stress.
Interaction partners:
- Cation/H
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Cation/H
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Cysteine proteinase inhibitor 2
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MADQQAGTIVGGVRDIDANANDLQVESLARFAVDEHNKNENLTLEYKRLLGAKTQVVAGTMHHLTVEVADGETNKVYEAKVLEKAWENLKQLESFNHLHDV
Protein: Probable cyclic nucleotide-gated ion channel 12 (Cyclic nucleotide- and calmodulin-regulated ion channel 12) (Q8GWD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclic nucleotide-gated ion channel.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nucleotide binding protein
- 11-beta-hydroxysteroid dehydrogenase-like 2
- rRNA biogenesis protein RRP36
Sequence:
MNHRRSKFARIDSMGVDGKLKSVRGRLKKVYGKMKTLENWRKTVLLACVVALAIDPLFLFIPLIDSQRFCFTFDKTLVAVVCVIRTFIDTFYVIHIIYYLITETIAPRSQASLRGEIVVHSKATLKTRLLFHFIVDIISVLPIPQVVVLTLIPLSASLVSERILKWIILSQYVPRIIRMYPLYKEVTRAFGTVAESKWAGAALNLFLYMLHSYVFGAFWYLSSIERKSKCWRAACARTSDCNLTVTDLLCKRAGSDNIRFLNTSCPLIDPAQITNSTDFDFGMYIDALKSGVLEVKPKDFPRKFVYCFWWGLRNISALGQNLETSNSAGEIFFAIIICVSGLLLFAVLIGNVQKYLQSSTTRVDEMEEKRRDTEKWMSYRVIPEYLKERIRRFEDYKWRETKGTEEEALLRSLPKDLRLETKRYLYLDMLKRVPWLNIMDDGWLLEAVCDRVKSVFYLANSFIVREGHPVEEMLIVTRGKLKSTTGSHEMGVRNNCCDLQDGDICGELLFNGSRLPTSTRTVMTLTEVEGFILLPDDIKFIASHLNVFQRQKLQRTFRLYSQQWRSWAAFFIQAAWRKHCKRKLSKTRDNENIPQGTQLNLASTLYVSRFVSKALQNRRKDTADCSSSPDMSPPVPHKPADLEFAKAEA
Protein: Mitochondrial hydrogenase maturation protein (M9PAS4)
Organism: Mastigamoeba balamuthi (Phreatamoeba balamuthi)
Interaction partners:
Sequence:
MLRSSAKFALPSRRQSGAFPKIASPRTSFPSIERVLGLPRGHVQPGQTLDLNRIQLTDLLSANDGSETEAELFDLAETIVNRVYGNKVYLRGIVEFSNVCEKNCNYCGIRREMPKQALPRYTMPDNEIVECALWAQKQRLGTVMLQSGEVSHPSRINWLIDVITQIRSRSIEADTVHKKGVAVALSVGEQSYDVYRRLFEAGGRRFLLRIESSNPLLYRSLHPADGMHTWEKRMSCLRDLGRVGFQLGTGVMIGLPQQSNWDLAGDILFFKEIDADMIGMGPYVVQADTPTGKVWTELHGREDREEYNRRLLALSSRMIALTRITLGDANIAATTALQAIHPTGRELCLRRGANLMMPILTPTKYREEYQLYEGKPSIHEAAEETHASLVRRVHVAGKEVADDVWGDPPHFTRKQAARADNLQT
Protein: ATP-dependent RNA helicase eIF4A (EC 3.6.4.13) (Eukaryotic initiation factor 4A) (eIF-4A) (Translation initiation factor 1) (Q6FQQ6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Eukaryotic translation initiation factor 3 subunit I
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Candida glabrata strain CBS138 chromosome L complete sequence
- Eukaryotic translation initiation factor 3 subunit B
- Candida glabrata strain CBS138 chromosome L complete sequence
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MSTDQMTQLDESQIETNYDKVVYEFDDMNLNEKLLRGVFGYGFNKPSAIQQRAIMPIIEGNDVLAQAQSGTGKTGTFSIAALQRIDPAIKAPQALMLAPTRELALQIQKVVMALGFHMDIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRKFKVDNIKMFILDEADEMLSTGFKEQIYQIFTMLPPTTQVVLLSATMPRDVLEVTAKFMQNPVRILVKKDELTLEGIKQFYVNVEEEQFKYDCLTDLYDSISVTQAVIFCNTRRKVEELTQRLTADNFTVSSIYSDLPQQERDTIMKEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPTNKENYIHRIGRGGRFGRKGVAINFIVNEDVQALRELEQFYSTQIEELPSDIGTLFT
Protein: Apelin (APJ endogenous ligand) [Cleaved into: Apelin-36; Apelin-31; Apelin-28; Apelin-13] (Q9R0R4)
Organism: Mus musculus (Mouse)
Function: Endogenous ligand for the apelin receptor (APLNR). Drives internalization of APLNR (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates. Plays a role in early coronary blood vessels formation. Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9TUI9}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9TUI9}. Note=Abundantly secreted in the colostrum. Lower level in milk. Decreases rapidly within several days after parturition in milk, but is still detectable even in commercial milk. {ECO:0000250|UniProtKB:Q9TUI9}.
Interaction partners:
- Apelin receptor
- Apelin receptor early endogenous ligand
- Angiotensinogen
- Angiotensin-converting enzyme 2
- Neuropeptide B
- Insulin-1
- Insulin-2
- Pro-neuropeptide Y
- Pro-opiomelanocortin
- Type-1 angiotensin II receptor A
Sequence:
MNLRLCVQALLLLWLSLTAVCGVPLMLPPDGTGLEEGSMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF
Protein: Photoactivated adenylate cyclase subunit beta-like protein ST- (P84743)
Organism: Euglena gracilis
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:16121285}.
Interaction partners:
Sequence:
MYILVWKKGQQIKTFHTLDEAAQFKAASNIDEAQMFSVTVASAISASGGSTEATNLRRLMYLSKSTNPEECNPQFLAEMARVAFIRNREIRVSGFLMYSSPFFIQVIVETDEDLDFLFAKISADPRHEMCIVLANGPGTGRMYGDWHMKDSHLDSITTHTAMKTILYQIARSFSSMWIYLQKSAANMLMLGKDPAAQPPERRSVVVTFIYLVEFCSIFSHPNLTEKTADVLSTFVYVCVKNVEGSGGNIAKFIPAICMTYWPIIRTKEALTAIQQISEDLAQLRSQQAQGSAVSLRYSQAGVHYGRGMQCNAGSRKSDFTLLGDCINTTSRIATLAKKLKTPLLFGFEVRCLLGDEKREEIEGAGIHQVKGRDKPVVVYQFPGPDLDVAMVRQKIEQFTPGRFRCQMPVVEYEALPISQRPPIFDDTPKSNPRPRTPGYGGRQRSDSLVDRLIRIANLSGFSESATGDTTLTTLTYISQATRPMSRLDLSAIMPTATRRNAQQSNIGTVLHENGLFVQTLEGPKDAVVNLYLRIRQDPRHTDVTTVHMAPLQERVYTSEWTLTLATEEMLATFPPVQDVLSQLAKSYTSLETYVPSTVVRYLTAGNNPRNLMPVSCGVVMLATDISSFTSLTEISSFTEVWMICNTFIDACTSAICQEGGEVIKLIGDCVTPYFPGNNADLAVAAAQELFIFCRQLREAFVDVLDVRGCVSCAVGMDYGQVVMAQCGLLRLSDYVAAGAVSAGVVEVEAITREVGYQFVVTVPDADRVQPQFRDYGIEPTPQAIGGLPCYGIVREVFDLPVESIKRGIKAMHAARSGEQPLTEPEQAKPDFRVSPGRDRHGVSGRRSNSSQGKGSIQVG
Protein: Uncharacterized protein (Q57X74)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPDPPLAAVPQPPMAAVPQPPKAAVPQPPMATVPQPPMAAVPQPPMAAVPQPPMAAVPQPPKAAVPQPPMAAVPQPPMAAVPQPPKAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMATVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMATVPQPPMAAVPQPPMATVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMATVPQPPKAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAVPQPPMAAGTVQATSPLFHQGVPLPKVCLLPSQYLPSGFHPAGGAARPPELSEEQKRELERAALRELASASGDHNREPEEVVKTLAGRLFFLSRCDVATMLTNVATSVQSLGRHDVGLLANEDGTTFTFIQSPHYGTDNFAEGLQHPSRHRRAVEDAKERINRSDCRSRERFLRAARAGTPSNVEERRSPNPPKSTKRSTSIAARDFPKSTYEQIQEVLQEQRRTSRHEKRGASASRKGQRRPSSADGGYLLWRYGGKYPQECLYENYRLRGMRGRQH
Protein: Methionine aminopeptidase 1 (MAP 1) (MetAP 1) (EC 3.4.11.18) (Peptidase M 1) (P53582)
Organism: Homo sapiens (Human)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}.
Interaction partners:
- Methionine aminopeptidase 2
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL23
- Zinc-regulated GTPase metalloprotein activator 1B
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS17
Sequence:
MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF
Protein: THO complex subunit 1 (Nuclear matrix protein p84) (p84N5) (hTREX84) (Q96FV9)
Organism: Homo sapiens (Human)
Function: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.
Subcellular location: [Isoform 1]: Nucleus speckle. Nucleus, nucleoplasm. Nucleus matrix. Cytoplasm. Note=Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Spliceosome RNA helicase DDX39B
- THO complex subunit 7
- THO complex subunit 4
- THO complex subunit 2
- THO complex subunit 3
- THO complex subunit 6
- THO complex subunit 5
- SAP domain-containing ribonucleoprotein
- Chromatin target of PRMT1 protein
- Ubiquitin carboxyl-terminal hydrolase CYLD
Sequence:
MSPTPPLFSLPEARTRFTKSTREALNNKNIKPLLSTFSQVPGSENEKKCTLDQAFRGILEEEIINHSSCENVLAIISLAIGGVTEGICTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDEEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERTSDTKPTRIIRKRTAPEDFLGKGPTKKILMGNEELTRLWNLCPDNMEACKSETREHMPTLEEFFEEAIEQADPENMVENEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPVTGEQIEVFANKLGEQWKILAPYLEMKDSEIRQIECDSEDMKMRAKQLLVAWQDQEGVHATPENLINALNKSGLSDLAESLTNDNETNS
Protein: phosphorylase kinase (EC 2.7.11.19) (X2JEJ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKDEEDDLLPDKDAAKGFYAKYEPKEILGRGISSTVRRCIEKETGKEFAAKIIDLGATTESGETNPYHMLEATRQEISILRQVMGHPYIIDLQDVFESDAFVFLVFELCPKGELFDYLTSVVTLSEKKTRTIMRQIFEGVEYIHAKSIVHRDLKPENILLDENHNVKITDFGFAKQLQEGEKLTNLCGTPGYLAPETLKCNMFEGSPGYSQEVDIWACGVIMFTLLVGCPPFWHRKQMVMLRNIMEGKYSFTSPEWADISEDPKDLIRKCLVVDPSQRITVKEVLRHPFFNQMLRKQSRFNARKKFQFAILVIRAIIRIRRLRFTAEPLHVEEAIRDPYRVKVLRKVIDGCAFRVYGHWVKKGEGQNRAALFENTPRTELHALYINNLSR
Protein: 1-hydroxy-2-naphthoate 1,2-dioxygenasee (EC 1.13.11.38) (1-hydroxy-2-naphthoate-degrading enzyme) (1-hydroxy-2-naphthoic acid dioxygenase) (O24721)
Organism: Nocardioides sp. (strain KP7)
Function: Dioxygenase involved in phenanthrene catabolism by mediating cleavage of 1-hydroxy-2-naphthoate.
Interaction partners:
Sequence:
MNSSNTGAPEAAQAATLEAFDRRAAEQYLRGQWIAEEHLMRAIGGPRPAGIPYRWEWKSVEVALDEATIALGPVDTARRHLTFVNPGLMDRGSATTHTISAGFQLVKPGEVCWSHRHTMSAVRFVTKGHPDAFTAVDGERLPMEDFDLLITPRFSWHDHHNSGDADVVWLDGLDIGLLQSLGAVFYEPYGDDSQNVRPSSSEGIGTRSHWLRPTWERGRESRLPIRYPWKEVNARLDVYDLDAGTPYDGLALRYANPVTGGPTMATMDCWVQRLAPGFDGKSHRRSSSAITYVISGSGTMVTEDETITFNRGDVISLPNWTNFRWTNDSEIEPVLLFSMHDIPALEAFGLLYEEPEAILNATPAPINPTPSLNPIYRPGAFYDQDEL
Protein: CDT1-like protein a, chloroplastic (AtCDT1a) (Q9SJW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Member of the pre-replication complex. Component of the plastid division machinery. Promotes polyloidization and regulates endoreduplication. Involved in the coordination of cell and plastid division.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15928083}.
Interaction partners:
- DNA replication licensing factor MCM5
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Cell division control protein 6 homolog B
- Origin of replication complex subunit 2
- Origin of replication complex subunit 1B
- Origin of replication complex subunit 3
- Origin of replication complex subunit 1A
Sequence:
MSTPGSSRSIPFKSKKRLVMDSPSSKSQTGNPNPSSVALPTPEKPLENMLSRSRNRSVALSVKEIRQAAGSRRRSEDPVASSAKSRLFFDSSSSSPSKRKSSNKNAEKEKLPEKYENLGKFFEALDNSMLLSKLRGSKPTFSNISKQIEHLTERRFCYSHLAQIKHILPEAIEIKRVLIHDETTCCMKPDLHVTLNADAVEYNDKSKSESKKIALRKVFRARLADFVKAHPQGDEVPEEPLPEPFNRRKPVENSNVEVKRVSSLMEEMASIPASKLFSSPITSTPVKTTSSLAKPTSSQINIAPTPTKPTSTPAKQTLSEINILPTPVKPVSTLAKFPSTPAIIDSTPVITATPPEFASTPARLMSTSLAARPLKRSNGHTNPDDISADPPTKLVRRSLSLNFDSYPEDERTMDFTDDIPIDQVPEEDVSSDDEILSILPDKLRHAIKEQERKAIEDQNPAISLAKRRRKMIACLPKLFNVIHYLIQSIRRWVITKEELVHKIIAGHSDITDRKEVEEQLILLQEIVPEWMSEKKSSSGDVLVCINKLASPLTIRSRLEEENKQEMAPLLS