wanglab/gogpt-training-data huggingface dataset:
Protein: Bruchpilot, isoform I (A0A0B4K843)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDNAYVYYKLDEFRLEIQRRDQEILAMAAKMKTLEEQHQRHIAVLKESLCAKEEHYNMLQTDVEEMRARLEEKNRLIEKKTQGTLQTVQERNRLTSELTELKDHMDIKDRKISVLQRKIENLEDLLKEKDNQVDMARARLSAMQAHHSSSEGALTSLEEAIGDKEKQMAQLRDQRDRAEHEKQEERDLHEREVADYKIKLRAAESEVEKLQTRLERAVTERERLEIKLEASQSELGKSKAELEKATCEMGRSSADWESTKQRIARLELENERLKHDLERSQMQLEEQTTLHKTTFGRTTMTTSQELDRAQERADKASAELRRTQAELRVTQSDAERAREEAAALQEKLEKSQGEVYRLKAKLENAQGEQESLRQELEKAQSGVSRIHADRDRAFSEVEKIKEEMERTQATLGKSQLQHEKLQNSLDKAQNEVDHLQDKLDKACTENRRLVLEKEKLTYDYDNLQSQLDKALGQAARMQKERETLSLDTDRIREKLEKTQMERDDAVTEVEILKEKLDKALYASQKLIDEKDTSNKEFEKMLEKYDRAQNEIYRLQSRCDTAEADRARLEVEAERSGLAASKAREDLRKLQDESTRLQEACDRAALQLSRAKECEDNARSELEHSRDRFDKLQTDIRRAQGEKEHFQSELERVTYELERAHAAQTKASASVEAAKEEAAHYAVELEKMRDRYEKSQVELRKLQDTDTFGRETRRLKEENERLREKLDKTLMELETIRGKSQYESESFEKYKDKYEKIEMEVQNMESKLHETSLQLELSKGEVAKMLANQEKQRSELERAHIEREKARDKHEKLLKEVDRLRLQQSSVSPGDPVRASTSSSSALSAGERQEIDRLRDRLEKALQSRDATELEAGRLAKELEKAQMHLAKQQENTESTRIEFERMGAELGRLHDRLEKAEAEREALRQANRSGGAGAAPHPQLEKHVQKLESDVKQLAMEREQLVLQLEKSQEILMNFQKELQNAEAELQKTREENRKLRNGHQVPPVAAPPAGPSPAEFQAMQKEIQTLQQKLQESERALQAAGPQQAQAAAAAGASREEIEQWRKVIEQEKSRADMADKAAQEMHKRIQLMDQHIKDQHAQMQKMQQQMQQQQQAAQQAVQQAAQQQQSAAGAGGADPKELEKVRGELQAACTERDRFQQQLELLVTELEKSKMSNQEQAKQLQTAQQQVQQLQQQVQQLQQQMQQLQQAASAGAGATDVQRQQLEQQQKQLEEVRKQIDNQAKATEGERKIIDEQRKQIDAKRKDIEEKEKKMAEFDVQLRKRKEQMDQLEKSLQTQGGGAAAAGELNKKLMDTQRQLEACVKELQNTKEEHKKAATETERLLQLVQMSQEEQNAKEKTIMDLQQALKIAQAKVKQAQTQQQQQQDAGPAGFLKSFF
Protein: Large ribosomal subunit protein uL15/eL18 domain-containing protein (Q57U68)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 50S ribosomal protein L17, putative
- KOW domain-containing protein
- 50S ribosomal protein L2, putative
- Ribosomal protein L11, putative
- 30S Ribosomal protein S17, putative
- Large ribosomal subunit protein uL3m
- 50S ribosomal protein L13, putative
- 40S ribosomal protein S5, putative
- Large ribosomal subunit protein bL21m
Sequence:
MLSVSPPLRRYRLFHPRREAIPMHMCPAKTIFPLINSNNLLVKTRNSWEDFTGRKEFDEDHPLPVVGSRLNGRTTQHKWNHWDQYLNPQITQSIKDLTPTPEYVGMRCGHNMIKMGWMKIGGSWKYSRGYNDRRRVFARGQWQERKMTPRFMLAPRVSAGGPRNRYEGKLVFSPLRLSKLLWAIDTGRINPNEVITLYHLRQANVVGEREIVWPGFVLISNGVRRVPYPIHIELQNASAESIRLIEEAGGSFTCVYMTHEGLYQELHPEEYPIFMDQELPERRGLESLATNPSKRGWLTRWYEDSSKYAHPAAGRRYSHYLKPPTERDFPATVEEYEMVKHHQKWHLNQPGTGTLLPWHSYNTADLVKRAAGRL
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) [Cleaved into: Ghrelin; Obestatin] (Q30DT1)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU368086}.
Interaction partners:
Sequence:
ILSLLLLSLLWMDLAMAGSSFLSPEHQKLQRKEPKKPSGRLKPRALEGQFDPDVGSQEEGAEDELEIRFNAPFNIGIKLSGAQSLQHGQTLGKFLQDILWEEAEETL
Protein: Sulfate adenylyltransferase subunit 2 (EC 2.7.7.4) (ATP-sulfurylase small subunit) (Sulfate adenylate transferase) (SAT) (P9WIK1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Interaction partners:
- Bifunctional enzyme CysN/CysC
- Probable sulfate-binding lipoprotein SubI
- Probable sulfate-transport integral membrane protein ABC transporter CysW
- Sulfate transport system permease protein CysT
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfite reductase [ferredoxin]
- 3'-phosphoadenosine 5'-phosphate phosphatase
- Adenosine 5'-phosphosulfate reductase
- uroporphyrinogen-III C-methyltransferase
- Bifunctional oligoribonuclease and PAP phosphatase NrnA
Sequence:
MTSDVTVGPAPGQYQLSHLRLLEAEAIHVIREVAAEFERPVLLFSGGKDSIVMLHLALKAFRPGRLPFPVMHVDTGHNFDEVIATRDELVAAAGVRLVVASVQDDIDAGRVVETIPSRNPIQTVTLLRAIRENQFDAAFGGARRDEEKARAKERVFSFRDEFGQWDPKAQRPELWNLYNGRHHKGEHIRVFPLSNWTEFDIWSYIGAEQVRLPSIYFAHRRKVFQRDGMLLAVHRHMQPRADEPVFEATVRFRTVGDVTCTGCVESSASTVAEVIAETAVARLTERGATRADDRISEAGMEDRKRQGYF
Protein: AT4g20760/F21C20_110 (NAD(P)-binding Rossmann-fold superfamily protein) (Q941A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNTLVRSGGAWLVSPSMAVAALKRMRVSGLATSSSSSVPNWKGGVSMVQGASRGIGLEFVRQLLENNKNGYVVATCRNPKEATSLSDLKNRFSERLFIQKLDVTDETTIEESAESVREKYGSLNLLINAAGILSIPGVLQPETTLNKVEKSSLMLAYEVNAVGPILVMKHMWPLLKAGGGSGTDREVAVVANLSARVGSIGDNRLGGWHSYRASKSALNQLTKNVSVELGRRKDPVACILLHPGTVDTDLSRPFQRNVPDGKLFTREYSVQKLLHIINNTKKQDSGKFFAWDGQEIPW
Protein: RNA polymerase I-specific transcription initiation factor rrn11 (O94332)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of a multiprotein complex essential for the initiation of rDNA transcription by RNA polymerase I. Binding to the DNA template is dependent on the initial binding of other factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C3B8.11
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- RNA polymerase I-specific transcription initiation factor rrn7
- Cytochrome b-c1 complex subunit 7
- Putative acyl carrier protein, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- RNA polymerase I-specific transcription initiation factor rrn3
Sequence:
MFSPCTVKEKRSTLRSVAPNPESSVIPPIPLPSRRYKTRHIDALCSLMHLCLLRKDYPRASRAFSLLLRSKSVDISKLWNIGLEILNKVNPEASSEYMERLIARYPARPSINNSYPNRNAEHFFPAYIMLLIQRQEYNKAMKLLDEYLLLPPYNQNPALHEYSGMLCFELAKEEASESERTKWIEKAKYNFSNAGIDVEL
Protein: Uncharacterized protein, isoform C (Uncharacterized protein, isoform D) (Q9VHY2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA polymerase II subunit M
- FI07206p
- Phosphoserine phosphatase
- Trifunctional purine biosynthetic protein adenosine-3
- Delta-1-pyrroline-5-carboxylate synthase
- Adenylosuccinate synthetase
Sequence:
MESSSPSDTTEIHKQSCSIQDQSSVPVPDSSGEINNWMEPEPVDSLELSGEYADNESAIFVSASEYNEKKAQIDQLVQKILTMEQQQRQLEENASETKELCDLKLHLEKLNARLEALGEFLDTLRLREDQQEIKIEDNSELVDHTEQPKWSNLYSGLNRYRQKANHTAAQFYQHKSNIIDSLKTLYEPIQPRPAIDDLEKQPALLLVRLLKHQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILASEETKNRKREEKKKALTLKWTQEFNRVYCKEIRKISMFDDEEESGKEEEQYEPPEKRTCHVKTKKINQFRILDDDDNDAGDKAVVEDEQKDLLAKTPEPEVFSSDEEEEHLSNGRYPSANTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLVVNELKRYGNTSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESMLGHRRLNFIIKPLMLRRTKQKLQASGDMPALPSLKIELICVQLSKTEMAVYQILSAISKKIFTQFLLQREKGNSDLNYYSLERTPQFIAGHMSDERYNEIYERFLKSLGYNPGEKILGIYILVLLLRLRQFCCHPGLMIGMLRGALTAEDVQNVKVDASDVEGQLKMDVLAELDKFDETDSEDDCCDEEDSTRRDGNFKLEVIKDEIKEENVPWDSGDDLPTASSFEDQLDSARALKLLNPQNPIFQFIRPSAKLKMVIDKLEELLTGTNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNANNEKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRIKSLQDCKLEIAKVVLPEEGGEVTKCVGGGLNLAELKKLFEM
Protein: T. brucei spp.-specific protein (Q38BF9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMEVGGWQNMRVEQHGGPLVLVDYRTFTHIPCCTFFFCFLLAFFFLRFTCVMLFSLLLLLLLLSFLFGCLSLSYLLNDTSLFDLCVVHLFCVCFVFVFIRINILLPTFFFLLFRFAVWLRGDLVFVFFCFFFSLLFVFFFPFPTVGIDACGFCVRASTAGLCESAFSLFALLTYICASPPLFFLFFLFLFLPFVCVLFAHEHGLLYVYLTPVFHPFMCLLVRY
Protein: NAD(P)H pyrophosphatase NUDT13, mitochondrial (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 13) (Nudix motif 13) (Q8JZU0)
Organism: Mus musculus (Mouse)
Function: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP. Has a marked preference for the reduced pyridine nucleotides. Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-end of some RNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28755312}.
Interaction partners:
- Nucleotide triphosphate diphosphatase NUDT15
Sequence:
MSLYCRTFFRRKSFGCYRLLSTYVTKARYLFELKEDEEACRKAQKTGVFYLFHDLDPLLQASGHRYLVPRLSRAELEGLLGKFGQDSQRIEDSVLVGCSEQQEAWFALDLGLKSASSSRASLPKSEMEAELGGSFIKLRQALFQLNSVDSSLLFTAQALLRWHDGHQFCSKSGQPTQKNVAGSKRVCPSSKIIYYPQMAPVVITLVSDGARCLLARQSSFPKGLYSALAGFCDIGESVEETVHREVAEEVGLEVENIQYSASQHWPFPNSSLMIACHATVKPGHTEIQVNLKELEAAAWFSLDEVTTALRRKGSLALQPSEASPLLLPPKLAIAHHLIKKWVETRSCSSLAA
Protein: GPI transamidase component PIG-S (Phosphatidylinositol-glycan biosynthesis class S protein) (Q96S52)
Organism: Homo sapiens (Human)
Function: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Multi-pass membrane protein {ECO:0000269|PubMed:11483512}.
Interaction partners:
- GPI-anchor transamidase
- GPI-anchor transamidase component PIGU
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component GPAA1
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase, stabilizing subunit
Sequence:
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLRLMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALSSGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFNIIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKSHDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSLPHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIMVYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMTWELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELASGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKIFLETRKSWRKPEKTD
Protein: Vasodilator-stimulated phosphoprotein (VASP) (P70460)
Organism: Mus musculus (Mouse)
Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10660044}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell junction, focal adhesion {ECO:0000269|PubMed:10660044}. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10660044}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10660044}. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions (By similarity). In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (By similarity). {ECO:0000250}.
Interaction partners:
- Zyxin
- Ena/VASP-like protein
- Profilin-1
- Vinculin
- Profilin-2
- Ras association
- Cell division control protein 42 homolog
- Profilin-4
- Filamin-binding LIM protein 1
- Actin, alpha skeletal muscle
Sequence:
MSETVICSSRATVMLYDDSNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIIRGVKYNQATPIFHQWRDARQVWGLNFGSKEDAIQFATGMANALEALEGGGPPPAPAPPAWSAQNGPSPEELEQQKRQPEHMERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPSSGVSGAGHGAGAAPPPAPPLPTAQGPNSGGSGAPGLAAAIAGAKLRKVSKQEEASGGPLAPKAENSRSTGGGLMEEMNAMLARRRKATQVGEKPPKDESASEESEARLPAQSEPVRRPWEKNSTTLPRMKSSSSVTTSEAHPSTPCSSDDSDLERVKQELLEEVRKELQKMKEEIIEVFVQELRKRGSP
Protein: TCEA2 protein (Transcription elongation factor A (SII), 2, isoform CRA_b) (Transcription elongation factor A2) (Q86VL0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
Sequence:
MMGKEEEIARIARRLDKMVTKKSAEGAMDLLRELKAMPITLHLLQSTRVGMSVNALRKQSSDEEVIALAKSLIKSWKKLLDASDAKARERGRGMPLPTSSRDASEAPDPSRKRPELPRAPSTPRITTFPPVPVTCDAVRNKCREMLTAALQTDHDHVAIGADCERLSAQIEEYILWVGAVGLGFWWSQEAAWPGALWWLLDATAQLSRGHLPGWSPAWVVRLSHLRRAPGPAEGLILSACGA
Protein: Prostaglandin E2 receptor EP3 subtype (PGE receptor EP3 subtype) (PGE2 receptor EP3 subtype) (Prostanoid EP3 receptor) (P34980)
Organism: Rattus norvegicus (Rat)
Function: Receptor for prostaglandin E2 (PGE2). Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11006128, ECO:0000269|PubMed:8393672}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Prostaglandin E synthase
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
Sequence:
MAGVWAPEHSVEAHSNQSSAADGCGSVSVAFPITMMVTGFVGNALAMLLVVRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTSPVVILVYLSQRRWEQLDPSGRLCTFFGLTMTVFGLSSLLVASAMAVERALAIRAPHWYASHMKTRATPVLLGVWLSVLAFALLPVLGVGRYSVQWPGTWCFISTGPAGNETDSAREPGSVAFASAFACLGLLALVVTFACNLATIKALVSRCRAKAAASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQMSVEQCKTQMGKEKECNSFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRDHTNYASSSTSLPCPGSSVLMWSDQLER
Protein: Lipopolysaccharide heptosyltransferase 1 (EC 2.4.99.23) (ADP-heptose:lipopolysaccharide heptosyltransferase I) (ADP-heptose:LPS heptosyltransferase I) (Heptosyltransferase I) (Q9HUF5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P24173}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24173}; Cytoplasmic side {ECO:0000250|UniProtKB:P24173}.
Interaction partners:
- UDP-glucose:
- Lipopolysaccharide core heptose
- lipopolysaccharide heptosyltransferase II
- 3-deoxy-D-manno-octulosonic acid transferase
- Bifunctional protein HldE
- Serine/threonine protein kinase
- Lipopolysaccharide kinase
- Phosphoheptose isomerase
- Heptose kinase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
Sequence:
MRVLLVKTSSLGDVIHTLPALTDAARAIPGIQFDWVVEEGFAEIPAWHPAVARVIPVAIRRWRKNLWQTLRNGEWRRFKQRLKEVDYDLVIDAQGLLKSAWLTRYVGKTPVAGLDRDSAREPLASRFYRRAYPVAWGQHAVERTRQLFAQALDYPLPESVGDYGLDREQLADADPGAPYLVFLHGTTWVTKHWPEAYWRELAERMCERGWSVRLPWGSAAERERAGRLAAGLENAAVLPRLSLAGMAKVLAGARACVAVDTGLGHLAAALDVPTLSLFGPTNPGFTGAYGRSQVHLGSDFPCAPCLKKTCTYQPTEEDRKLFDLKREQPLCFTRLNPQRVATQLEAMLLAPETLR
Protein: Acetyl-CoA carboxylase (Q9GZI3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVVNGQKPDIRTIVVSGNSLTNDAADQYESMEQFIHSHVADIEKRRPIKRLLVATNGIAAMRCLMTAKKFLHHTFRNDNLIHFVCMTTEDEIQSMSESLRMPNITLAESPSGTNKNNFANVDEILKHAIKYEVDAVWAGWGHASENPDLPRRLNDHNIAFIGPPASAMFSLGDKIASTIIAQTVGVPTVAWSGSGITMESIERSRGDFVVVPEDLLEQACVANYKEGLEALKTHNIGFPLMIKASEGGGGKGIRKCTKVEDFKSMFEEVAQEVQGSPIFLMKCVDGARHIEVQLLADRYENVISVYTRDCSIQRRCQKIIEEAPAIIASSHIRKSMQEDAVRLAKYVGYESAGTVEYLYLPASEGQEEHYYFLELNPRLQVEHPTTEMVSNISIPAIQLQIAMGLPLHKIKDIRKLYDLPIDGDSELPDEVLVDTKLHAIAARITCENPDDSFRPSTGKVYEINFPSSQDAWAYFSVGRGSSVHQFADSQFGHIFTRGTSRTEAMNTMCSTLKHMTIRSSFPTQVNYLVDLMHDADFINNAFNTQWLDKRIAMKIKQKCSLSMSVIIAVSAAVIGSSRVTGVFESFEESIDRGQVRPPNDLTETFIFDLVKDLNIYSLKVVRSAENTFVIILNGSKVTVGVKELQNGEFMVTHCEIVYRCAFEETKEAYKVTVNNEIITFEKDNDVSVLKSPYTGKLLQWKKEDGDWLNVGDVYATAESMKMVFQVEVAKAPGRLQRVVNEGDPIHPGSVLAKLVDQTESEADRAQPFHGTFLEWSWHSSKANEQSKFNDCLAQCQNLLAGSTPMDSACIITELFHHLNESHTAHASEVLNQLLRDYINVEKYFEGKVYDDSVGEIKEDHLSRKDVVRTIYSHTQIKSKNIVMKALLGALKQGSGSKFIPSLLDNLRQIGNLHHTEEISNLAREILLFYHSMCYKNNYSEITASGLRPTGQEVKAWLDGPLSRRPDSSGWKVIHEYFFDETIGSQCLDRYVAMHISAEEGSIGNTYPLPQMKCTIDHFTLTATPKSFNKVVLKGNKLIVVRLSLDSKTFNQQCFSSEKFLDCLKTNFRKYCKKTDVINVSIFVKITDDLEAHQDPSTLTEQEEQRVCYAQNAVVDMKTILEKEFRVNRVNTVLCLNDRPLPQLTIFEQVRLEKDRLPANSYPVLSKLSTVRVSQHDDPTSNFAKLFVRQQLIIPGNNAEEVQKKISQAVYLALDNACTAAQVAMAKKTKANKTFTSNHVFVFISCPGLPEKVIGSQEQLEFMKKCITDEVDSHKAILAKHQINEVEVVYESVDGHKRIVIRDETGVTTEVITEFSEASLGVYPVINTIEKKRLAARRVNSSYIYDFPIIFGMAAMNFWKSASSAMELPNEMAQALKEQRWREFFQIRELVLENGVLTEISDAEILKKRSANALNNCGMVAWIMTLYTPEKPRGFDLIVIGNDVTFQSGSFGTAEDDLFAAASTYSREHKLPRVNVSVNSGARIGLSTKISKLVKLQLENEDKPEQGFEYIYIDGEHKAQIEGEVVYEELGNGRLKILAVIGAKNEKIGVENLQGSGLIAGETARAYAEVPTYCYVTGRSVGIGAYTARLAHRIVQHKQSHLILTGYEALNTLLGKKVYTSNNQLGGPEVMFRNGVTHAVVDNDLEGIAKVIRWMSFLPTPTEEFPFFSKHGDDCSARDVVIPSDSEQNTYDVRDLIDSKNLSNQTGICDTMSFDEICGDWAKSIVAGRARLCGIPIGVVSSEFRNFSTIVPADPAIDGSQVQNTQRAGQVWYPDSAFKTAEAINDLNKENLPLMIIASLRGFSGGQKDMYDMVLKFGAQIVDALAVYNRPVIVYIPEAGELRGGAWAVLDSKIRPEFIHLVADEKSRGGILEPNAVVGIKFRKPMMMEMMKRSDPTYSKLSSSTEPEAREQLEERYEELSKTYRNASVEFADAHDRWQRMKSVGVVEHVTSLTNSRRLFSELLRNELAKVGMAEIYSSAPHTVKPCLATAMTWVETNLRSYVQPNSSMDEQYTQIEQYYETQFVDDLVIAINEDRKRYEQQLNTFMNKISSKRR
Protein: Probable tape measure protein (TMP) (Transglycosylase) (EC 4.2.2.n1) (O64046)
Organism: Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta)
Function: Serves as a base for tail tube protein polymerization and acts as a template for tail length determination. Exolysin involved in host peptidoglycan digestion necessary for viral DNA entry into the host cell.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MSQNLKIILTPQADTSSKTVEQLNQQIKSLEKKLNSLKLNTNIDSTTLKALQEFSSAIDTYQKNLKSYNQTVKETSTVIKNADGSVEKLTQQYKKNGEILQRETKIINNRNTALKQETQEVNKLTQATEKLGQVQKKTVQRNLQGQPTKVVQKNRHGFDDIVYTTDPKTNSTSSKTTTNYDQQRRAIEQLKQDLEKLRQQGIVTDTTISSLGRKINTAQSAQQIEALQNRIRMLDDKSAAVAKNNELKKTIELYQRQAQVNVQNLNTRYGSSMGSSNRQAVQDYLNAVNSLNVSTGSNNIRSQIQSLNMQFRELASNAQTAANQASSFGAELTQTFKSMSTYLISGSLFYGAISGLKEMVSQAIEIDTLMTNIRRVMNEPDYKYNELLQESIDLGDTLSNKITDILQMTGDFGRMGFDESELSTLTKTAQVLQNVSDLTPDDTVNTLTAAMLNFNIAANDSISIADKLNEVDNNYAVTTLDLANSIRKAGSTASTFGVELNDLIGYTTAIASTTRESGNIVGNSLKTIFARIGNNQSSIKALEQIGISVKTAGGEAKSASDLISEVAGKWDTLSDAQKQNTSIGVAGIYQLSRFNAMMNNFSIAQNAAKTAANSTGSAWSEQQKYADSLQARVNKLQNNFTEFAIAASDAFISDGLIEFTQAAGSLLNASTGVIKSVGFLPPLLAAVSTATLLLSKNTRTLASSLILGTRAMGQETLATAGLEAGMTRAAVASRVLKTALRGLLVSTLVGGAFAALGWALESLISSFAEAKKAKDDFEQSQQTNVEAITTNKDSTDKLIQQYKELQKVKESRSLTSDEEQEYLQVTQQLAQTFPALVKGYDSQGNAILKTNKELEKAIENTKEYLALKKQETRDSAKKTFEDASKEIKKSKDELKQYKQIADYNDKGRPKWDLIADDDDYKVAADKAKQSMLKAQSDIESGNAKVKDSVLSIANAYSSIDISNTLKTSISDVVNKLNLKDDLDPEELEKFSSSLGKLQEKMQKALDSGDEKAFDNAKKDLQSLLETYSKSDSSIDVFKMSFDKAQKNIKDGDKSLSSVKSEVGDLGETLAEAGNEAEDFGKKLKEALDANSVDDIKAAIKEMSDAMQFDSVQDVLNGDIFNNTKDQVAPLNDLLEKMAEGKSISANEANTLIQKDKELAQAISIENGVVKINRDEVIKQRKVKLDAYNDMVTYSNKLMKTEVNNAIKTLNADTLRIDSLKKLRKERKLDMSEAELSDLEVKSINNVADAKKELKKLEEKMLQPGGYSNSQIEAMQSVKSALESYISASEEATSTQEMNKQALVEAGTSLENWTDQQEKANEETKTSMYVVDKYKEALEKVNAEIDKYNKQVNDYPKYSQKYRDAIKKEIKALQQKKKLMQEQAKLLKDQIKSGNITQYGIVTSTTSSGGTPSSTGGSYSGKYSSYINSAASKYNVDPALIAAVIQQESGFNAKARSGVGAMGLMQLMPATAKSLGVNNAYDPYQNVMGGTKYLAQQLEKFGGNVEKALAAYNAGPGNVIKYGGIPPFKETQNYVKKIMANYSKSLSSATSSIASYYTNNSAFRVSSKYGQQESGLRSSPHKGTDFAAKAGTAIKSLQSGKVQIAGYSKTAGNWVVIKQDDGTVAKYMHMLNTPSVKAGQSVKAGQTIGKVGSTGNSTGNHLHLQIEQNGKTIDPEKYMQGIGTSISDASQAEAERQQGIAQAKSDLLSLQGDISSVNDQIQELQYELVQSKLDEFDKRIGDFDVRIAKDESMANRYTSDSKEFRKYTSDQKKAVAEQAKIQQQKVNWIQKEIKTNKALNSAQRAQLQEELKQAKLDLISVQDQVRELQKQLVQSKVDETLKSIEKSSSKTQGKIKDVDNKISMTEEDEDKVKYYSKQIKLIQQQQKEAKKYIKQLEEQKKAAKGFPDIQEQITEEMQNWKDKQKDFNLELYNTKKSIKDIYKSLADEVVSIYKEMYEKMRDIELEAHQKATQDLIDEIDKTDDEAKFQKELKERQDSIQKLTDQINQYSLDDSEFGKSKVKELTEQLQKEQLDLDDFLKDRESNKRKEALQDQLEKDEESINNKYDNLVNDERAFKKLEDKIMNGKITDIAKQLNEFSKFINTNMESIGKSISNNLIDKLKEASNALNTAVKGNTTGKKVSSFASGGYTGTGLGAGKLAFLHDKELILNKTDTANILDTVKAVRETAVDDSPKWGQGVKLADLIKKGITSIPSLVPNVNQSMLTNSLIPNLKKIEIPSKTIASSGDKTINLTNTFHIDKLIGGESGARSMFESIKNEVVKLNGSM
Protein: Pygopus 2 (Q80V76)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- B-cell CLL/lymphoma 9 protein
- Catenin beta-1
- B-cell CLL/lymphoma 9-like protein
- LIM domain-binding protein 1
- Lymphoid enhancer-binding factor 1
- Transducin-like enhancer protein 1
- Transcription factor 7-like 2
- Transducin-like enhancer protein 4
- Transducin-like enhancer protein 3
- Transcription factor 4
Sequence:
MAASAPPPPDKLEGGSGPAPPPAPPSTGRKQGKAGLQMKSPEKKRRKSNTQGPAYSHLTEFAPPPTPMVDHLVASNPFEDDFGAPKVGGAGPPFLGSPVPFGGFRVQGGMAGQVPPGYGTGGGGGPQPLRRQPPPFPPNPMGPAFNMPPQGPGYPPPGNMNFPSQPFNQSLGQNFSPPGGQVMPGPVGGFGPMISPTMGQPPRGELGPPPLPQRFTQPGAPFGPSLQRPGQGLPSLPPNTSPFPGPDPGFPGPGGEDGGKPLNPPAPTAFPQEPHSGSPAAAVNGNQPSFPPSSSGRGGGTPDANSLAPPGKAGGGSGPQPPPGLVYPCGACRSEVNDDQDAILCEASCQKWFHRECTGMTESAYGLLTTEASAVWACDLCLKTKEIQSVYIREGMGQLVAANDG
Protein: DNA-binding death effector domain-containing protein 2 (DED-containing protein FLAME-3) (FADD-like anti-apoptotic molecule 3) (Q8WXF8)
Organism: Homo sapiens (Human)
Function: May play a critical role in death receptor-induced apoptosis and may target CASP8 and CASP10 to the nucleus. May regulate degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11965497}. Note=Nuclear, accumulated in subnuclear structures resembling nucleoli.
Interaction partners:
- CASP8 and FADD-like apoptosis regulator
Sequence:
MALSGSTPAPCWEEDECLDYYGMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHLARKRRRPVSPERYSYGTSSSSKRTEGSCRRRRQSSSSANSQQGQWETGSPPTKRQRRSRGRPSGGARRRRRGAPAAPQQQSEPARPSSEGKVTCDIRLRVRAEYCEHGPALEQGVASRRPQALARQLDVFGQATAVLRSRDLGSVVCDIKFSELSYLDAFWGDYLSGALLQALRGVFLTEALREAVGREAVRLLVSVDEADYEAGRRRLLLMEEEGGRRPTEAS
Protein: Actin-4 (EC 3.6.4.-) (P10986)
Organism: Caenorhabditis elegans
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:2795655}.
Interaction partners:
- Tropomyosin isoforms a/b/d/f
- LRRCT domain-containing protein
- Actin-related protein 2
- Actin-depolymerizing factor 2, isoform c
- Actin-related protein 3
- Probable actin-related protein 2/3 complex subunit 3
- Menorin
- Myosin, essential light chain
- DH domain-containing protein
- Leukocyte cell-derived chemotaxin-2 homolog
Sequence:
MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF