wanglab/gogpt-training-data huggingface dataset:
Protein: BHLH protein (O18374)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPRKKRSSSPTEFFDDDFDEDASSQSSQPPVQRNAANARERMRMRVLSSAYGRLKTKLPNIPPDTKLSKLDTLRLATLYIKQLITAVETGSHSQNHPHNHNQHHSLNHSHSSTTSSEGLDTSHMADSSGGGNYHFHNNGHGMSWPFEFHQSSRSLAFAPSSSTTSSARMDWQTLHTQSYPKTTRGETHVSADLSYHQLPESHSHWYPAEVHQMEPAASCSYDSGMGQHQRGIAIATSHAHGI
Protein: Leukocyte cell-derived chemotaxin 1 (Chondromodulin) [Cleaved into: Chondrosurfactant protein (CH-SP); Chondromodulin-1 (Chondromodulin-I) (ChM-I)] (O70367)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization (By similarity).
Subcellular location: [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Accumulated in the inter-territorial matrix of cartilage. {ECO:0000250}.; SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTENSDKVPITMVGPEDVEFCSPPAYATVTVKPSGSPTRLLKVGAVVLISGAVLLLFGAIGAFYFWKGNDNHIYNVHYTMSINGRLQDASMEIDAANNLETFKMGSGAEEAIEVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVSTGTKQSISELEGKIMPVKYEENSLIWVAVDQPVKDNSFLSSKILEFCGDLPIFWLKPMYPKEIPRERREVVRSSAPSTTRRPHSEPRGNAGPGRLSNRTRPSVQDDEEPFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVVMPCSWWVARILGMV
Protein: Fallaxidin-3.2.1 (P86164)
Organism: Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax)
Function: Lacks antibacterial activity against Gram-positive or Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:18803332}.
Interaction partners:
Sequence:
LDFAKHVIGIASKL
Protein: LD02225p (LD05703p) (Utx histone demethylase, isoform A (EC 1.14.11.68)) (Q9VL07)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PAX-interacting protein 1
- Retinoblastoma-binding protein 5 homolog
- Histone-lysine N-methyltransferase trr
- GEO08286p1
- Protein will die slowly
- HL01030p
- Protein dpy-30 homolog
- Nuclear receptor coactivator 6, isoform F
- Host cell factor
- Set1/Ash2 histone methyltransferase complex subunit ASH2
Sequence:
MGQLTFEDDCLIRELDSRYYGFLDLSNSKNAELRNLVQQTITNLQNYIANGQVHESKNSSDNKNAIQKFEPSTQAGEHMENTSSRNNDDTKPFEQDAKEKVSIIEEKHQDEHYVNALCKLGHLHLLLGEYSEALSAYQKYLRFRENNYWTNHAFIYGIGVAYFKLRCFKWAIKSFQELLYLSPNFTCANEVHLRLGLMLKHCGEFHIALKHLQLALLYTYPSTFSELQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKNISLELKADVYRQLGWMYHCVECLGEKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQISFQKSSLIRKKQAIRMKKDTIGLSKGLSQRITFLEGQLSQAPLPSITSKRRQLCSIEEAWNLPISLEMNSRQQQTAQMLPRQVTKQSPVQGPPPPYPHSQLSQSPIPSKRIKEDGTSQQEVTQNNSQTSAQNLINISESLNQRNFNAMPESNKSSEQSVLDTFDDISNDIYKQNESIKLERLSQDALSNNEDSRHDFIGGDNADISTTFKIQMDSKQLMVAVKLLPIDEPPVHCTILQVNAPPPSPPDCPPQKLTRDQLLPPTPSVHLENKKHAFSPQLQEFCLKHPIAVVRGLAGVLKLDLGLFSTKTLVEANPDHSVEVRTQVHQSPDENWDTSQGKRVWACISHRSHTTIAKYAQYQASSFQDSLKLILPQDESDKGFPGSQAMSDSDSKDSVSNSNIVLKRKKHKINSKMLRFGTNVDLSDEKKWKPQLTELQKLPAFARVISAANMLSHVGHVILGMNTVQLYMKVPGSRTPGHQENNNFCSININIGPGDCEWFAVPDAYWGGVHNLCEKNNISYLHGSWWPVLEDLYKENIPVYRFIQKPGDLVWVNAGCVHWVQSIGWCNNIAWNVGPLTARQYSLAIERYEWNKVQAFKSIVPMVHLSWNLARNIKVSDTKLFELIKMCLLQTLKNVLHIQEYVKSKGVEIRFNGRGKNEASHYCGQCEVEVFNVLFIKEQEKRHVVHCLSCALKLSPSLQGIVCLEEYRLSELQRVYDSFTLHRTQGLAYTQ
Protein: Serine/threonine-protein kinase 24 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 3) (MST-3) (STE20-like kinase MST3) [Cleaved into: Serine/threonine-protein kinase 24 36 kDa subunit (Mammalian STE20-like protein kinase 3 N-terminal) (MST3/N); Serine/threonine-protein kinase 24 12 kDa subunit (Mammalian STE20-like protein kinase 3 C-terminal) (MST3/C)] (Q9Y6E0)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. Regulates also cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve.
Subcellular location: Cytoplasm. Nucleus. Membrane. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.
Interaction partners:
- Programmed cell death protein 10
- MOB-like protein phocein
- Striatin
- Serine/threonine-protein kinase 25
- Striatin-interacting protein 1
- Striatin-interacting protein 2
- Serine/threonine-protein kinase 26
- Striatin-3
- Striatin-4
- CTTNBP2 N-terminal-like protein
Sequence:
MDSRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH
Protein: Signal peptidase complex catalytic subunit SEC11 (PfSPC21) (EC 3.4.21.89) (Signal peptidase 21 kDa) (PfSP21) (Q8IE14)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18054093, ECO:0000269|PubMed:30127496}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P13679}. Note=Partially colocalizes with SPC25 in the endoplasmic reticulum. {ECO:0000269|PubMed:30127496}.
Interaction partners:
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MDFIKEQYNSLVLDLRKTFRNKRDGLSHILNVICLLLNALMIWKLLVVFTGCESPVVVVLSGSMEPGYYRGDTLALYHPPKIHAGDVVVYQINGRDIPIVHRILSLHTSKDNKFHLLSKGDNNNIDDRGLYDPHQYWLENEHVLGLSVGYTPYIGILTIWINEYPVVKWAIVSIMLIMILMGYE
Protein: Tumor necrosis factor alpha-induced protein 8 (TNF alpha-induced protein 8) (Q921Z5)
Organism: Mus musculus (Mouse)
Function: Acts as a negative mediator of apoptosis. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MLSEAEEPREVATDVFNSKNLAVQAQKKILGKMVSKSIATTLIDDTSSEVLDELYRVTKEYTQNKKEAERVIKNLIKTVIKLAVLHRNNQFNQDELALMEKFKKKVHQLAMTVVSFHQVEYTFDRNVLSRLLNECRELLHEIIQRHLTAKSHGRVNNVFDHFSDCDFLAALYNPFGKFKPHLQKLCDGINKMLDEENI
Protein: COP9 signalosome complex subunit 5 (Signalosome subunit 5) (EC 3.4.-.-) (JAB1 homolog) (P91001)
Organism: Caenorhabditis elegans
Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex (By similarity). The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-3/katanin targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3. May stabilize glh-1 protein levels by antagonizing kgb-1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus {ECO:0000269|PubMed:12781129}.
Interaction partners:
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 6
- Ubiquitin-like protein NEDD8
- COP9 signalosome complex subunit 3
- Cullin-4
- RING-box protein 1
- Cullin-1
- Cullin-3
Sequence:
MEVDNVKPSSSVPQRNWEKENNVQNVDSIFEYNNKQQVEIRNAKPWDKDPHYFKQIKISAIALLKMTMHAKRGGNLEIMGLLQGRIDANSFIILDVFALPVEGTETRVNAQAQAYEYMTVYSEMCDTEGRKEKVVGWYHSHPGYGCWLSGIDVSTQTLNQKFQEPWVAIVIDPLRTMSAGKVDIGAFRTYPEGYRPPDDVPSEYQSIPLAKIEDFGVHCKRYYSLDVSFFKSQLDAHILTSLWNSYWISTLSSSPLFSNVEFLNNQIQDINQKLSAVDKKLQLNDRSVDGHEALMKVVTDAKAVGDELETGRISHLVKQLLFARQAGGGCGCSHASAGSPMDIAVATEPEKAGPSPSAPEPAVEMADA
Protein: SERTA domain-containing protein 3 (Replication protein-binding trans-activator) (RPA-binding trans-activator) (Q9ERC3)
Organism: Mus musculus (Mouse)
Function: Strong transcriptional coactivator.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UJW9}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UJW9}.
Interaction partners:
- RING finger protein 208
Sequence:
MGGLKRKHSDLEEEEEEEKWDWSPTALRSYQQALLRISLDKVQRSLGPRAPSLRRHVLIHNTLQQLQAAIRLAPAPALPPEPLFLGEEDFSLSTTIGSILRELDTSMDEMEPPLNPAASSSPQNEIVSQADPVFLEALSSRYLGDSGLDDFFLDIDTSAVEKDVALPPPEPPHSLFCSPGSWEWNELDHIMEIILGS
Protein: DSC E3 ubiquitin ligase complex subunit C (Defective for SREBP cleavage protein C) (Q4WPW5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23104569}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTFPAFLSPDPTWDGDSTGGPLLLTVRFSASIPDFPLDIENPDITTAAGLKQLIRTHLPPNLSSHRLRLIYAGRGLEDATPLSVSLKLPPSPSRTPVVQEDATTVKGKGKAPIREQPRLYIHCSIGDIVLSDADLAAEAAIATTLQQEQADEDYTGRKKQQQPPPSTTSAPRGFDRLLSAGFTPSEVSALRSQFMAIQSVSRTPDTMPTGAELRELEDRWMDEGSSAMAAGVPGGGEGISFADDDGGFGAGSRGAMDDMLWGAVMGFFWPVGCAMWLRREEGVWSWRKGLAVFVGVVINVAFGAMRIMN
Protein: Potassium channel K2 (PfK2) (PfKch2) (Q8IKI3)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000269|PubMed:32957994}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel domain-containing protein
Sequence:
MKSGLFSMNDIFFLVNSIFKYFLILLNGSHLLKLLYSSKENIHIIEGLLCIITGVILKLSLIYIYCTYFMNIYIIKDYRRKNVLNIFNMNNNYKRNGNVIESDDFEYRKLIKKFFFKKVYYSIKKKHKRIELYMLKIYNSNFNYYFCNIRDMCYTIIWYISLYYWRRDTYNMIWGFNKIPTYIYNMLLILLSTSYIDLVMVIISYNKSKYYLMKSKLLIDIFFSAPCTYLFSKFIFVFEHQIDIYFMMGFLRNIKIFLNVSYVRIEHNSILTNTEIKIIRIVLGVLLLCNAFASTIYTIQAIHPYNLDNENFNYFLNSYLDYFYFSIISISTVGYGDIFPINKLSKVVCIIFIFWTFIWVPIQFNDLIISIFSKKKTYGKISMNNQKFILLIGDVEPQQLNVFLFESVAQGNKLKFHLLTTYPINIYDEQIKIADHFCISLYIKNFDLNEKENINLLYSINAQNAYYLFLFSNKFHNGHYNIDTKSFTRLLILKKFLHGKKNAVIELRSNCVSNIVRSIGCENFIIVNLKHSLIVKNIKYPGFITLILNLFTAYNYDISSYNFNDIASYPSLKYIGEFNRGSRTKIFSFIVHKNMVGLIFDKLFYKLYESLGIILVGIETNTTNYYINNKKHKNKNSYVDDNFTTMRKNNMKNKKKKSFKFIYLHLLKKYGHTNHYTQKKKKKKYDNIINHHGSKSKMEYSTQLRHNNKTIKIYDEYNTIETYQNYLNYETINNSRINIYNSDEKKKKYNDVSPTNNILTNYKNGKLHIEKRDDFDNNNNNNNNNIVKSRKKGRENKNDEIINVCININSDIKKKYNNNNNNNNNNDNDNNNIINDHDNYNIYNNLNSNLKCRCLPNTKKNKAQNVNNVTNNKDNDVSVKRIKTHLQDDNTIDNKKELKCYLNLLGKNYAIRDSDKCVVIANSRKVIKYLSKAKSLFWIFEIKSKKKDNISYDLKSVIKTKQTFNKYFTTNIKKKLPTTSIQNNVYVNKNAHIIAMNYHDLFNTYRISRIFTKNNYNYKRKNSRKKHLFRNLNGEFNETKLYHHCNNTHNIKTTDKKNMEKLDKLYFSTKLNSKSNTNIHIHNNNNNNNNNNEHYDDEIKTYYFNLTEKNSHLLLNYKKQLKKKNYINTCYSVNKSDESINKIKNMNSDNNNINSNNINSNINNNNNNNTKLNHTLKNRITFSYMEACEKYFPTENRNNKLLLIINCTCNIIQLIKMFNNKYKYNVIILTDEIPTMNIMDLFKYNVVFIKCKILDDYNLINSGLMNAEYILILPTEAKNINEINEIDMNTIIVTRKITHLLKKKKRTYYINNIITELINPSNVIFLEENKMIKLKDKKSSYDDFFPYVNSSQFYSSNIICETMLYNFMTHHKSFTDFSVCTNTLECLIKFLRIIYICDLSKYYDFSFKKIKTFRDLFYFLSKKNIITIGLYRKGDKKVPFYIYTKPNENCLLRFDDIVYIL
Protein: Contig An01c0080, genomic contig (A2Q831)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQIFVKTLTGKTITLDVESSDTIDNVKTKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCEKSICRKCYARLPPRATNCRKKKCGHTNQLRPKKKLK
Protein: Muc3 protein (Q80Y91)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VTVTSQEYSEKLQDRKSEEFSNFNKTFTKQMALIYAGIPEYEGVIIKNLSKGSIVVDYDVILKAKYTPGFENTLDTVVKNLETKIKNATEVQVQDVNNNCSALLCFNSTATKVQNSATVSVNPEETCKKEAGEDFAKFVTLGQKGDKWFCITPCSAGYSTSKNCSYGKCQLQRSGPQCLCLITDTHWYSGENCDWGIQKSLVYGLGGAGVAVLLVILVILLVFSIRFRKDAQRQRSRVSEMYKWGEEEGRASPGTFHNFGFDHNEERENYMPLDSVYNTFQPSLNHINPERKIQIQRPQVVMTSL
Protein: Auxin-responsive protein IAA15 (Indoleacetic acid-induced protein 15) (Q9C966)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 5
- Auxin response factor 7
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin-responsive protein IAA33
- Auxin response factor 19
- Auxin transporter protein 1
- Auxin response factor 3
- Putative auxin response factor 15
- Putative auxin response factor 14
- Auxin response factor 9
Sequence:
MSPEEYVRVWPDSGDLGGTELTLALPGTPTNASEGPKKFGNKRRFLETVDLKLGEAHENNYISSMVTNDQLVGWPPVATARKTVRRKYVKVALDGAAYLRKVDLGMYDCYGQLFTALENMFQGIITICRVTELERKGEFVATYEDKDGDLMLVGDVPWMMFVESCKRMRLMKTGDAIGL
Protein: Uracil phosphoribosyltransferase (UPRTase) (EC 2.4.2.9) (UMP pyrophosphorylase) (P18562)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate in the pyrimidine salvage pathway.
Interaction partners:
- Cytosine deaminase
- Orotidine 5'-phosphate decarboxylase
- Uridine kinase
- Uridylate kinase
- Uridine nucleosidase
- Thymidylate synthase
- Putative uridine kinase DAS2
- Purine nucleoside phosphorylase
- Golgi apyrase
- Zinc finger chaperone ZPR1
Sequence:
MSSEPFKNVYLLPQTNQLLGLYTIIRNKNTTRPDFIFYSDRIIRLLVEEGLNHLPVQKQIVETDTNENFEGVSFMGKICGVSIVRAGESMEQGLRDCCRSVRIGKILIQRDEETALPKLFYEKLPEDISERYVFLLDPMLATGGSAIMATEVLIKRGVKPERIYFLNLICSKEGIEKYHAAFPEVRIVTGALDRGLDENKYLVPGLGDFGDRYYCV
Protein: Neuromedin-U [Cleaved into: Neuromedin precursor-related peptide 36 (NURP36); Neuromedin precursor-related peptide 33 (NURP33); Neuromedin-U-23 (NmU-23)] (P12760)
Organism: Rattus norvegicus (Rat)
Function: Ligand for receptors NMUR1 and NMUR2. Receptor-binding is very tight if not irreversible and triggers an increase in the cytosolic Ca(2+) concentration. Stimulates muscle contractions of specific regions of the gastrointestinal tract. In rat, NMU stimulates contractions of stomach circular muscle.
Subcellular location: [Neuromedin-U-23]: Secreted {ECO:0000305|PubMed:28874765}.
Interaction partners:
- Neuromedin-U receptor 1
- Neuromedin-U receptor 2
- Neuromedin-S
- Neurotensin receptor type 1
- Neurotensin/neuromedin N
- Appetite-regulating hormone
Sequence:
MSRAANRRPGLSAGQLAAATASPLLSLLLLLACCADACRGTPISPQRLPPEQELQLWNEIPEACASFLSVDSQPQASVALRKLCRVLMEIFQKPQEQTEKDNAKRFLFHYSKTQKLGNSNVVSSVVHPLLQLVPQLHERRMKRYKVNEYQGPVAPSGGFFLFRPRNGKRSTSFI
Protein: EH domain-containing and endocytosis protein 1 (Bud site selection protein 15) (P34216)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18448668, ECO:0000269|PubMed:19713939, ECO:0000269|PubMed:19776351, ECO:0000269|PubMed:22190733}. Note=Localized to actin cortical patches concentrated in the developing bud tip in cells with small buds and at the mother-daughter neck in cells undergoing cytokinesis. Localization can be maintained in the absence of polymerized actin filaments.
Interaction partners:
- Suppressor of yeast profilin deletion
- Epsin-1
- Polyubiquitin
- Protein SLA2
- Clathrin heavy chain
- Clathrin light chain
- Autophagy-related protein 8
- AP-2 complex subunit alpha
- Clathrin coat assembly protein AP180B
- Actin cytoskeleton-regulatory complex protein SLA1
Sequence:
MASITFRTPLSSQEQAFYNQKFHQLDTEDLGVVTGEAVRPLFASSGLPGQLLSQVWATVDIDNKGFLNLNEFSAALRMIAQLQNAPNQPISAALYESTPTQLASFSINQNPAPMQSGSATGNTNNTDIPALSSNDIAKFSQLFDRTAKGAQTVAGDKAKDIFLKARLPNQTLGEIWALCDRDASGVLDKSEFIMAMYLIQLCMSHHPSMNTPPAVLPTQLWDSIRLEPVVVNQPNRTTPLSANSTGVSSLTRHSTISRLSTGAFSNAASDWSLSFEKKQQFDAIFDSLDKQHAGSLSSAVLVPFFLSSRLNQETLATIWDLADIHNNAEFTKLEFAIAMFLIQKKNAGVELPDVIPNELLQSPALGLYPPNPLPQQQSAPQIAIPSRASKPSLQDMPHQVSAPAVNTQPTVPQVLPQNSNNGSLNDLLALNPSFSSPSPTKAQTVVQNNTNNSFSYDNNNGQATLQQQQPQQPPPLTHSSSGLKKFTPTSNFGQSIIKEEPEEQEQLRESSDTFSAQPPPVPKHASSPVKRTASTTLPQVPNFSVFSMPAGAATSAATGAAVGAAVGAAALGASAFSRSSNNAFKNQDLFADGEASAQLSNATTEMANLSNQVNSLSKQASITNDKKSRATQELKRVTEMKNSIQIKLNNLRSTHDQNVKQTEQLEAQVLQVNKENETLAQQLAVSEANYHAAESKLNELTTDLQESQTKNAELKEQITNLNSMTASLQSQLNEKQQQVKQERSMVDVNSKQLELNQVTVANLQKEIDGLGEKISVYLTKQKELNDYQKTVEEQHAQLQAKYQDLSNKDTDLTDREKQLEERNRQIEEQENLYHQHVSKLQEMFDDLSQRKASFEKADQELKERNIEYANNVRELSERQMNLAMGQLPEDAKDIIAKSASNTDTTTKEATSRGNVHEDTVSKFVETTVENSNLNVNRVKDDEEKTERTESDVFDRDVPTLGSQSDSENANTNNGTQSGNETANPNLTETLSDRFDGDLNEYGIPRSQSLTSSVANNAPQSVRDDVELPETLEERDTINNTANRDNTGNLSHIPGEWEATPATASTDVLSNETTEVIEDGSTTKRANSNEDGESVSSIQESPKISAQPKAKTINEEFPPIQELHIDESDSSSSDDDEFEDTREIPSATVKTLQTPYNAQPTSSLEIHTEQVIKYPAPGTSPSHNEGNSKKASTNSILPVKDEFDDEFAGLEQAAVEEDNGADSESEFENVANAGSMEQFETIDHKDLDDELQMNAFTGTLTSSSNPTIPKPQVQQQSTSDPAQVSNDEWDEIFAGFGNSKAEPTKVATPSIPQQPIPLKNDPIVDASLSKGPIVNRGVATTPKSLAVEELSGMGFTEEEAHNALEKCNWDLEAATNFLLDSA
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (G3MU40)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHDYLSDLNVYVPYQRPNIVLHGSDFWLRTLDCHTEIPLAAIYFGNIQGGTYFNHWQVSFSRENISSRDMLHKIHAEFEFDKTDMITVQFQCFEEKKQKFEDSRKQKVRVNYQLTIRRDSIRRIIVDPRVEGCNTCVHFEVNCPPLIRKGYIDNDKSSFHKPFYERQKRFDCDWRNGNVNHGNPQDAAIADSPFFTIEFHKEISTKEMYRVLSRLRSRTKVLIEFANLPSIDVPMGSHYPYNRWNLKKSPTDSNAPIFREFLKEIFPPKYEIVDDKLIDVNEERKFSITYLIECLLSRGAIVKDQLLLNEQHWKNFLEIIIWYYRNDNQLCEAALEDLVHLIDGRKRIGSILKCLDKICQKREVMKLVNGLTEKESIEGYQRVRKVIFTPTRVIYIAPETIMGNRVLRKFDKDGTRVLRVTFRDDNNKKMRSNVTGKLLDRTANKYLEHGVRIANREYGFLGCSNSQMRDNGAYFMMRFTDKQLDRFYKCNPTASNINFKPKIDEVRFQLGRFSEIENVPKLMARLGQCFTQSRLTGVGLGRDDYCSTYDLTGGRATNGSEYTFSDGVGMMSYQFAQEVSQAMQFGKAVPSCFQIRFRGNKGVIAIEPFLDEIRKWALVNGVTSMKMAKCLFRPSQIKFQAKAISGDQIEMVKFSSAVLVALNKPFINILDQVSEMQSLDCHKRITSRIEELMDRQILSFAKQMNEETFCRNKLKEFPRRIDIDNLRTMWGFTLSSEPFFRSLIKASIKFSITKQLCKEQIQIPSELGRSMLGVVDETGRLQYGQIFVQYTKNYKKKLPPRDSNNKVHGSEIVTGTVLLTKNPCIVPGDVRIFEAVDIPELHHMCDVVVFPQHGPRPHPDEMAGSDLDGDEYSVIWDQELLLERNEEPFDFAVEKIKVPYDREKLDVLMREFYVTYLKLDSVGQISNSHLHNSDQYGLNSRVCMDLAKKNCQAVDFTKSGQPPDPLETKWRADPVTFEVIPPENPERIPDFHMGNERSPMYVSPRLCGKLFREFQAIDNVIKISEERDEQYNIELDETIFVTGFERYMESAQKQLSSYNGQLRSIMENYGIRSEGEIMSGCIVEMRNRISDKDQDDMSFYNTNQMIETKMTSLVCKFRETFFEEFGGFTVKCTLLPNAYDNGNCLNYRCEDPDQEVRKKAVAWYRACYECAQSTREVRKLSFAWIAYDVIAKVKETNVLNNERMQIGGANPMYTFLEEHRKQYLIDHDADFKNFCELDHLITGEKSKEAISILKIYLEMIPGLDSVFFMLMRWGESLRLFDGKPIKIYHFFLMFILFATRQLASADGNAEPFFKIIEKEEYEKQKRDSSRGNIDPLTEKKRSDMMVKFFQFMGCRKFRKMSTLSFCPLNFSSIFMRGEWRIFHESALKTYYNILFNLRFEELPVSSDPTITAETMDRECEPFVIELPENINVNDLINNMKKHTNVSTVKMRRQEKNPINDKAKPKTTVRYIVSVSGTLESIQMLKKLSAVTIPIKSHWEGEEVSQQMASLCYQKVMNGEF
Protein: MEQ protein (Marek's EcoRI Q-encoded bZIP protein) (Meq oncoprotein) (R-LORF7) (Q77Q71)
Organism: Gallid alphaherpesvirus 2
Interaction partners:
Sequence:
MSQEPEPGAMPYSPADDPSPLDLSLGSTSRRKKRKSHDIPNSPSKHPFPDGLSEEEKQKLERRRKRNRDAARRRRRKQTDYVDKLHEACEELQRANEHLRKEIRDLRTECTSLRVQLACHEPVCPMAVPLTVTLGLLTTPHDPVPEPPICTPPPPSPDEPNAPHCSGSQPPICTPPPPDTEELCAQLCSTPPPPISTPHIIYAPGPSPLQPPICTPPPPDAEELCAQLCSTPPPPICTPHSLFCPPQPPSPEGIFPALCPVTEPCTPPSPGTVYAQLCPVGQAPLFTPSPPHPAPEPERLYARLTEDPEQDSLYSGQIYIQFPSDTQSTVWWFPGDGRP
Protein: Apoptosis enhancing nuclease (H0YMJ6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVPREAPESAQCLCPSLTIPNAKDVLRKRHKRRSRQHQRFMARKALLQEQGLLSMPPEPGSSPLPTPFGAATATEAASSGKQCLRAGSGSAPCSRRPAPGKASGPLPSKCVAIDCEMVGTGPRGRVSELARCSIVSYHGNVLYDKYIRPEMPIADYRTRWSGITRQHMRKAVPFQVAQK
Protein: Probable eukaryotic initiation factor 4A (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A) (Q384F2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RRM domain-containing protein
- Mago nashi-like protein,putative
- MI domain-containing protein
- mRNA export factor MEX67
- RNA-binding protein, putative
- RNA helicase
- MI domain-containing protein
- PRP8 protein homologue
- RNA-binding protein, putative
- PinX1-related protein 1
Sequence:
MTATARSDEEERAGLHEETDMQANVPTIPTFEAMGLKKDLLHGMYGYGYKKPTAIQKRFVAPFLQSRDLVAQASSGSGKTSAFCICLLQASEPTLRETQGLVLSPTRELALQTQDLCNNIGHYMGISAYAAIGGKSIEDDLRRLESGVQIVSGTPGRVFDMIKRRHLRVNHLKTLVLDEADEMLGKGFKAQIHDIYRMIPPLQVVLVSATLPVDVLDMTEKFMTEPVRILVKRDEITVDSIMQYFVSVDEEKNKFDTLCDLYDTLTIAHAVIFCNTRKKVEQLAKKMTKEKFTVSFMHGDMPQAERDEIMRNFREGKSRVLISTDLWSRGIDVEQISLVLNYDLPFSREQYIHRIGRTGRMGRKGLAISFVKHDELRLLRDIEQFYATQIEELPANVGEQF
Protein: Isoamyl acetate-hydrolyzing esterase (A0A1D8PUB6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Pyridoxal 5'-phosphate synthase glutaminase subunit
- Medium-chain fatty acid ethyl ester synthase/esterase
Sequence:
MAWDKKKKKFSTIAIMEYGKFVLFGDSITQFSCTQYGFHPALQNVYIRKLDVINRGFSGYNSEHARQILPKILESETNIKLMTIFFGTNDAYDYINEIQTVELDRYKDNLSVMVQMVLDKNIKPIIIGPGLHDPKMAKAMLAERGRPIDKDPTTNQRLLKYSETAKKVAAQHNVAFIDTWNTLRQHQGWTKDQLFEVSATKDKWEIGESLAEIVSDGIHFTAKSYKILFEEIIRVIEEKYPELAPENLPSQLCDWKQINPNDLSSIFN
Protein: Drosocin antimicrobial peptides [Cleaved into: Drosocin; Buletin (DIM 7) (IM7)] (P36193)
Organism: Drosophila melanogaster (Fruit fly)
Function: Antibacterial peptide with strong anti-Gram-negative bacteria activity.
Subcellular location: [Drosocin]: Secreted {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}.; SUBCELLULAR LOCATION: [Buletin]: Secreted {ECO:0000269|PubMed:35730150, ECO:0000269|PubMed:9736738}.
Interaction partners:
- Diptericin B
- Metchnikowin
- Diptericin A
- Attacin-C
- Attacin-A
- Cecropin-C
- Cecropin-B
- Cecropin-A1
- Peptidoglycan-recognition protein SB1
- Defensin
Sequence:
MKFTIVFLLLACVFAMGVATPGKPRPYSPRPTSHPRPIRVRREALAIEDHLTQAAIRPPPILPA