wanglab/gogpt-training-data huggingface dataset:
Protein: Sperm antigen with calponin homology and coiled-coil domains 1 (J3QS22)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSAAKPWNPAIRAGGHGPDRVRPLPAASSGMKSSKSSTSLAFESRLSRLKRASSEDTLNKPGSTAASGVVRLKKTATAGAISELTESRLRSGTGAFTTTKRTGIPAPREFSVTVSRERSVPRGPSNPRKSVSSPTSSNTPTPTKHLRTPSTKPKQENEGGEKAALESQVRELLAEAKAKDSEINRLRSELKKYKEKRTLNAEGTDALGPNVDGTSVSPGDTEPMIRALEEKNKNFQKELSDLEEENRVLKEKLIYLEHSPNSEGAASHTGDSSCPTSITQESSFGSPTGNQMSSDIDEYKKNIHGNALRTSGSSSSDVTKASLSPDASDFEHITAETPSRPLSSTSNPFKSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAP
Protein: Macrophage-expressed gene 1 protein (Perforin-2) (Q7SXE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004265}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004265}.
Interaction partners:
Sequence:
MKSRAFHLLMLCCFISVCNLHPLIRPNNGLRLCRKNSSLTALEVLPGGGWDNLRNIDMGRVMNLSYSQCQTTEDGVYLIPDEVFVIPQKVSGVETNSEIIMSWLEQKSSTSSSVNADVSFFSVLNAKFSTENQRMKTHQVKEGSVTARVQVRNHLYTVKAYPDFTLDSRFAKQAEEIADAIENNQTRHANYLSEKLVLDYGTHVITSVDAGATLVQEDYLKMSYISNSQSDKSSVSASAGANFFDKVKFDIGGNTSQGSSQSSSYQGNITYSLIQSHGGALFYPGITLQKWQQSTLNNLAAIDRSGLPLHYFLNPSTFPDLPTPTVNKLASTVRKAAERYYKVNTIPGCVNVDSPNFNFQANVDDASCEGPITNLSFGGIYQKCTPLTPDGNIICDETAQKNPATGGYSCPQHYNTTLLHSEVVEKGFNHYECHTHCHSCGFLGLSTCCDKTCGDSYHVRRAKLETLWCSSTHKTPENSGYLFGGLFGPGIQNPLTKSSSCPPSYFTQRFLSNGMMICMSNDYEIGTRFSVPFAGFFSCQSGNPLSNGQSRCPPQFSQHLAAISDGCQVLYCVQSGVFSGGHLKPVRLPPFTRPPVVGMIATNTVAVMTEGERSWVRVGETKMWRLAKPGDIKQMQSILDASEMSGGKKAGVAIGIIVLVALVVAGTVVIMKRRNRFSSLKLNRGYEEISEERNESSVEIEQEQNEAANENPNQQLLS
Protein: Brevinin-2JD (B3A0M3)
Organism: Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis)
Function: Has antibacterial activity against E.coli ATCC 25992 (MIC=38 uM), E.coli CIB 84492 (MIC=38 uM), S.aureus ATCC 25923 (MIC=19 uM) and S.aureus CIB 85462 (MIC=19 uM). Has antifungal activity against C.albicans (MIC=19 uM). Has weak hemolytic activity against rabbit erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:22917879}.
Interaction partners:
Sequence:
GLLDTFKNLALNAAKSAGVSVLNSLSCKLSKTC
Protein: DUF1279 domain-containing protein (E9AC21)
Organism: Leishmania major
Interaction partners:
Sequence:
MLFRCIRVVRPPALHTRRMSMRTVVMEHGVPLSLYYFITNELLVCLLTCLLHYGYFGQEDLIGFLKSVGASKYVDLNSIEGKSWSLFGGQLVVSARLVANFTAASLFMSLWTPVQLPICIATYPYLKRSRQLLMKRDSVSKPI
Protein: Acid-sensing ion channel 1 (ASIC1) (Acid-sensing ion channel) (Amiloride-sensitive cation channel 2, neuronal) (Brain sodium channel 2) (Q6NXK8)
Organism: Mus musculus (Mouse)
Function: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11988176}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P78348}. Postsynaptic cell membrane {ECO:0000305|PubMed:11988176}. Cell projection, dendrite {ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:17060608}. Note=Isolated in synaptosomes from the dendritic synapses of neurons. {ECO:0000269|PubMed:11988176}.
Interaction partners:
- Acid-sensing ion channel 2
- PRKCA-binding protein
- Acid-sensing ion channel 4
- Stomatin
- Acid-sensing ion channel 3
- Stomatin-like protein 3
- Transient receptor potential cation channel subfamily V member 1
- Bile acid-sensitive ion channel
Sequence:
MELKTEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFCYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEACSAEDFKVVFTRYGKCYTFNSGQDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLIYLPSPWGTCNAVTMDSDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCQKEAKRNSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
Protein: C-CAP/cofactor C-like domain-containing protein (Q388J8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTYQAKEVVTEEFLRKKLEVSGELARMRAMIVDTALKTLSEDPNIKSRLFSPTPRLKAEKESAKGRQSLSVVMEYLEHMGLNYTLSVLKQEAALTECALQSRQDIVRELGLPEGSGPILTTIMGAPGAAGANSGVSKDNIGLPTTTPESAPVPRAPVAQTKTEDGEDTTYFISKWSGRTFYRSGGQVSGQQVQLEYLTNCTVYVLDPLDSITVDDCEGGELIIAACEGSVFLRNCKNMTVHVACKQLRTRDCEYITLHIFATTDPVVESSHHINFKPFYIRLPGLQASFKSARLDPKTNRFVHVYDFTEDDPKLPKPHFTVTYKGHGLCMKDLCGEKGKPDCPQEIEDFLAGRLGPAASSESGHNKSYNIKTGAEEWTGNKESSSPERGKEATPPESASRSDSSAPTTPHSRKDDAVPAPAAATGDALDGSYSSFDDDEDEDENDSQSDKKSEDDDDDDSDDF
Protein: Splicing factor YJU2 (P28320)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role (via N-terminus) in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates. Further stabilizes spliceosome conformation for 3'-splice site docking (via C-terminus) promoting exon ligation.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor SNT309
- Pre-mRNA-splicing factor CLF1
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ISY1
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor PRP46
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-processing protein 45
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-splicing factor CWC2
Sequence:
MSERKAINKYYPPDYNPLEAEKLSRKMAKKLKTMNKSHASIRLMTPFSMRCLECNEYIPKSRKFNGKKELLKEKYLDSIKIYRLTISCPRCANSIAFRTDPGNSDYVMEVGGVRNYVPQKPNDDLNAKTAVESIDETLQRLVREKEMEQNEKMGIKEQADDKMDLLEKRLAKIQQEQEDDEELENLRKKNLEMSQRAEMINRSKHAQQEKAVTTDDLDNLVDQVFDNHRQRTNKPGNNNDEKRTPLFNPTSTKGKIQKKSSVRTNPLGIVIKRGKSLK
Protein: Large ribosomal subunit protein uL15 (60S ribosomal protein L28) (L27a) (L29) (RP44) (RP62) (YL24) (P02406)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS13A
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS12A
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL15A
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS4B
- Large ribosomal subunit protein uL30A
- Large ribosomal subunit protein eL13B
- Large ribosomal subunit protein eL36B
Sequence:
MPSRFTKTRKHRGHVSAGKGRIGKHRKHPGGRGMAGGQHHHRINMDKYHPGYFGKVGMRYFHKQQAHFWKPVLNLDKLWTLIPEDKRDQYLKSASKETAPVIDTLAAGYGKILGKGRIPNVPVIVKARFVSKLAEEKIRAAGGVVELIA
Protein: Proline-rich protein 7 (Synaptic proline-rich membrane protein) (P0C6T3)
Organism: Rattus norvegicus (Rat)
Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner. Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN. Might play a redundant role in the regulation of T cell receptor signaling (By similarity). Might promote apoptosis in T cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8TB68}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000269|PubMed:15629447}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Synapse {ECO:0000269|PubMed:27458189}. Cell projection, dendrite {ECO:0000269|PubMed:27458189}. Nucleus {ECO:0000269|PubMed:27458189}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD) (PubMed:15629447, PubMed:27458189). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern (PubMed:15629447). Translocates from synapses to nuclei following NMDA receptor activity (PubMed:27458189). {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}.
Interaction partners:
- Proline rich 9
Sequence:
MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPPPPHRSRLEAPVHAHSHVHVHPLLHHGPAQPHAHPHPHHHALPHPPPSHLSVPPRPWSYPRQAESDMSKPPCYEEAVLMAEPPPPYSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAAPCPALCLQADRSRRVFPSWTDSELSSREPLEHGAWRLPVSIPLFGRTTAV
Protein: GSH-induced LITAF domain protein (AtGILP) (Q94CD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a membrane anchor, bringing other regulators of programmed cell death (PCD) to the plasma membrane. Negatively regulates hypersensitive cell death.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21526181}; Peripheral membrane protein {ECO:0000269|PubMed:21526181}; Cytoplasmic side {ECO:0000269|PubMed:21526181}.
Interaction partners:
- Protein LSD1
- Protein FATTY ACID EXPORT 5
- Probable calcium-binding protein CML16
- At5g57910
- At4g27652
- Expressed protein
- AT5g23340/MKD15_20
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- At4g27654
- At1g66080
Sequence:
MAKEGTTVIGVPYYAGQNPYQAGIVPPNAIYGDPLGAPIQQTIYRDTPAPFNCLYCGNTGLTNLRSKPGVAAVVACMMPFMLGFCFLCPSMDCLWNKQHHCPQCGNKVADFEKSDPCLVMDPPQWKQPSFALPA
Protein: Solute carrier family 15 member 1 (Intestinal H(+)/peptide cotransporter) (Oligopeptide transporter, small intestine isoform) (Peptide transporter 1) (Proton-coupled dipeptide cotransporter) (P51574)
Organism: Rattus norvegicus (Rat)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P46059}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the apical membrane of enterocytes. {ECO:0000250|UniProtKB:P46059}.
Interaction partners:
- Sodium/glucose cotransporter 1
- Solute carrier family 22 member 6
- ATP-binding cassette sub-family C member 2
- Solute carrier family 2, facilitated glucose transporter member 2
- Organic anion transporter 3
- Neutral amino acid transporter B
- Organic cation/carnitine transporter 2
- G-protein coupled receptor family C group 6 member A
- Solute carrier organic anion transporter family member 2B1
- Solute carrier family 22 member 4
Sequence:
MGMSKSRGCFGYPLSIFFIVVNEFCERFSYYGMRALLVLYFRNFLGWDDDLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVISVSSINDLTDHDHDGSPNNLPLHVALSMIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPILRVQQCGIHSQQACYPLAFGVPAALMAVALIVFVLGSGMYKKFQPQGNIMGKVAKCIRFAIKNRFRHRSKAFPKRNHWLDWAKEKYDERLISQIKIMTKVMFLYIPLPMFWALFDQQGSRWTLQATTMTGKIGTIEIQPDQMQTVNAILIVIMVPIVDAVVYPLIAKCGFNFTSLKKMTVGMFLASMAFVVAAIVQVEIDKTLPVFPSGNQVQIKVLNIGNNDMAVYFPGKNVTVAQMSQTDTFMTFDVDQLTSINVSSPGSPGVTTVAHEFEPGHRHTLLVWGPNLYRVVKDGLNQKPEKGENGIRFVSTLNEMITIKMSGKVYENVTSHSASNYQFFPSGQKDYTINTTEIAPNCSSDFKSSNLDFGSAYTYVIRSRASDGCLEVKEFEDIPPNTVNMALQIPQYFLLTCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAIGNIIVLIVAEAGHFDKQWAEYVLFASLLLVVCIIFAIMARFYTYINPAEIEAQFDEDEKKKGVGKENPYSSLEPVSQTNM
Protein: Fused isobutyryl-CoA mutase [Includes: Isobutyryl-CoA mutase (ICM) (EC 5.4.99.13); P-loop GTPase (EC 3.6.5.-) (G-protein chaperone)] (Q1LRY0)
Organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Function: Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, and to a much lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. The G-domain of IcmF has also a role in its cofactor repair. Does not display ATPase activity.
Interaction partners:
- Periplasmic metal ion binding protein
- Methionine aminopeptidase
- Triosephosphate isomerase
- Triosephosphate isomerase
- 3-hydroxyacyl-coa dehydrogenase oxidoreductase protein
Sequence:
MTDLSDVSRTAAAKPPAVPGRGPANKVRFVTAASLFDGHDASINIMRRILQSQGCEVIHLGHNRSVQEVVTAALQEDVQGIAISSYQGGHVEYFKYMIDLLREHGGEHIQVFGGGGGVIVPDEIRELQAYGVARIYSPEDGQRMGLAGMITDMAQRCDIDLTRYAPTTLDTVVAGDRRALAQLITALENGKADPELVSALHAQAKAAAVPVLGITGTGGAGKSSLTDELIRRFRLDQDDALSIAVISIDPSRRKSGGALLGDRIRMNAINHPNIFMRSLATREAGSEISQALPDVIAACKAARFDLVIVETSGIGQGDAAIVPHVDLSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGAQDAWRDVAKQVQRNREQWHSRAEDMPVYGTQASRFNDDGVTMLYQGLVGALGARGMSLKPGTLPNLEGRISTGQNVIVPPARSRYLAELADTVRAYHRRVVAQSKLARERQQLRAAHDMLQGAGHESAALETLASERDVSLGAVERKLLAMWPQMQQAYSGDEYVVKIRDKEIRTGLISTTLSGTKIRKVVLPRFEDEGEILKWLMRENVPGSFPYTAGVFAFKREGEDPTRMFAGEGDAFRTNRRFKLVSEGMEAKRLSTAFDSVTLYGEDPHERPDIYGKVGNSGVSIATLEDMKVLYDGFDLTNPSTSVSMTINGPAPTILAMFMNTAIDQQIDRFRADNGRDPTADEEAKIRAWVLQNVRGTVQADILKEDQGQNTCIFSTEFSLKVMGDIQEYFVHHQVRNFYSVSISGYHIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSFFFSNGMDPEYSVLGRVARRIWAVTMRDKYGANDRSQKLKYHIQTSGRSLHAQEIDFNDIRTTLQALIAIYDNCNSLHTNAYDEAITTPTAESVRRALAIQLIINREWGVAKCENPNQGSFLIEELTDLVEEAVLQEFERIAERGGVLGAMETGYQRGKIQEESLYYEQLKHDGTLPIIGVNTFRNPNGDPTPQTLELARSSEDEKQSQLHRLTEFHGAHQADAEAMLARLRQAVIDNRNVFAVLMDAVRVCSLGQITHALFEVGGQYRRNM
Protein: Thiamine phosphate phosphatase-like protein (EC 3.1.3.100) (Q9SU92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: HAD-like hydrolase that has a thiamine monophosphate phosphatase activity in a heterologous system. Does not contribute to thiamine monophosphate phosphatase activity in planta.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PDX1.3
- Pyridoxal 5'-phosphate synthase-like subunit PDX1.2
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Pyridoxal kinase
- Inorganic pyrophosphatase 1
- Inorganic pyrophosphatase 2
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- Pyridoxal reductase, chloroplastic
Sequence:
MAKIVILFDFDRTLIDGDSDNWVVTEMGLTEIFHQLRFTLPWNRLMDRMMMELQSQGRSIDDIKSCLKKMPIDSHIIEAIKSAKSSGCDLKIVSDANQFFIEKILEHHDLVDCFSEIYTNPTSLDDNGNLRILPYHSDALPPHSCNLCPSNLCKGLVMDHLRASSSNDQIPRRFIYLGDGGGDFCPTLKLRECDFVMPRTNYPLWKKISDNPLLIKAEVKEWSSAEEQQRILLQLVSTITKEEDS
Protein: Histidine-containing phosphotransfer protein (Eurofung) (Q5BBS5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Cytoplasmic response regulator
- Two-component system protein B
- Transcription factor
- Response regulatory domain-containing protein
- histidine kinase
- Mitogen-activated protein kinase hog1
- Two-component system protein A
- MAP kinase kinase kinase
- mitogen-activated protein kinase kinase
- Uncharacterized protein
Sequence:
MASTTTTKTVKEEQPVQSKPRTLADMADSIDQATFEQILEMDDEDEHEFSQGIVYGFFDQAESTFDKMEKALEDKKLSELSSLGHFLKGSSATIGLTKVKDACEKIQHYGAGKDESGTNDEPDEKVSLEKIEKTLATAKKDYKEVENFFRREYYRDEETPSSPEESKKDAKA
Protein: Receptor mediated endocytosis 8, isoform B (A0A0B4LFW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPPKENVDLECFLVTKHSWKGRYKRILSIGTAGISTYNPDKLDLTNRWSYSDIVAAAPSKTTNIPHDFVITIKKDKKLDTIKLSSEYRNDILSSILKYYKEFADKPKNAQRFSAYKYHWSGISLPTVLEVTPCSLDQLDPTTNDVLASYMYKDIEGIIGISDYEGGIVMAYGGFSRLHLFKALNHHEIVQNIAQRSAQFLGIETKILKSQITLEQFERQRFGKFSGDQFQTSSTEFSVHKITPRHPDPVKRILCLTEVTLLERDPQTYSVCTLRPLTDVFALVRDKDNLQRFSIEYKNGIVRNYSTNDRDSLLATVLDAVRSSGNQDVHVRIGNTPRGKRYVPLNSSVDEETEANLMRLVINNFQNPSKRYEILERFNANVPHSGLNYSVTQDSLFAENKDKLILSALQALAQKELDSPTAQLSNLELEAIFHALTRLLASKVGYAAFTNLPGFREIIGTKVVAALRRKDLAVTYSAIDMINSLMHSVNSDHDLKQEQLNKSSILSSKSFLETLLNMWTTHVSHGSGALVLSAMLDFMTFALCVPYSETTDGKQFDTLLELVADRGRYLYKLFQHPSLAIVKGAGLVLRAIIEEGELQVAQQMQALALDEAALCRHLLVALYTPSNDPTQTTQRQLSRHLIGLWLTDSEEAMELFKRIFPAGLLTFLESEETVPESDVEEDKLNFRDNLKFAIQHSNKTRKNVIEKHLQGIKHWGMNLIEKQDGAAQALKNRPVVLRNRRQKKKTSDVVVNLPFFFYSFAKDHSLPNLIWNHKTREELRMCLENELRQFLNDRDLAGQMIVAWNYQEFEVAYQCLADEIKIGDYYIRLILEKDDWPQNLVKDPIELFNALYRRVLCRQRVNDDQMTVFSLQALAKVYRRYHAEIGKFNDMSYILQLSDRCLSPSMRDALINLISCLVLEKSNSRALIDHVQCLVDLITLAHLHKGRAQLNTKTNVIEAGPNMGTYEEKDWYYNIEKDGQKPERQGPITYSELKELWQKGLITPKTRCWAIGMDGWRSLQQIPQLKWCLIAKGTPLYDETELSSKILDILIKCTSFFPSRTQNGVAVLIPGPKLSRKLSEFICLPHVVQVCLTHDPGLLERVATLLYQIMEDNPEMPKVYLTGVFYFMLMYTGSNILPITRFLKMTHMKQGFRSEETSQSGIMHRSILGQLLPEAMVCFLENYSAEKFAEIFLGEFDTPEVIWSSEMRRLLIEKIAAHIADFTPRLRGHTMARYPYLAIPVISYPQLENELFCHIYYLRHLCDTQKFPNWPISDPVQLLKHTLDAWRKEVEKKPPQMTIQQAYQDLGIDLTKTPKPDESMIRKSYYKLAQMYHPDKNPNGREIFEKVNQAYEFLCSRNVWSSGGPDPNNIVLILRTQSILFERYPDVLRPYKYAGYPQLIKTIRLETRDDELFSKEAQLLTAASELCYHTVHCSALNAEELRREEGIEALLEAYTRCVSILGVDSKPDSLHYQVISNVTRCFEVACNFEKCKQKIIQLPQLLSDVCRVVYFKHTLSVSLVTSLAANNYDLQCQLSRNGVLWSLLLFIFEYDYTLDESGVDVSDKSNQQQLANNLAKMAVLGCIALAGYSMELRQKPVTGSETNSPAAKAPPVIKPKPSVSAASSSTYTQNAHNPLQSKQLAITSGKEKESDTSSGSSDTASSTPTESEQQQQLTKTRTSAIQQKYIVTGEAKNSLIKQVLDRLLTRYISNQLATVRDSDVLKLLTANTRNPYLIWDNGTRAQLKDFLEQQRTASAKETHEDIAQVSELVSSFEFDAHKDELQIGGIFIRIYNDMPTHPIAQPKLFIMDLLEYLKHAYQFLQYKKNPASTAAPVNATPKMGNDGILTPTLAPNHPQLQQASTGKSGTTFDEVLTAYNRSKSRKKLETDALTEQQLALQQSKYDFSSDGKIELHITMVLKALIAVIKANAEVEIQCIGNFDMIFGFLASNIFPDNSTVKAVALEVVSLVSRNKECVSEVAACEILGNYLVALKDPELRASQVKVLETLSGLMNVQEMIKEAQAKGATIYLLDMFCNSRNPQIREMCAGILAKMTADRLSGPKVRITVSKFLPALFIDAMVESPATSVQLFESIHEHPELIWNDTTRSNVCDAVADTCQRFYQLQKANSRHVWKDPEILKDIVSNEIVVAGVYLRLFVSNPAWTLRKPKQFLSDLLDFVVEQIGKSSSEQDVLDLSTTALVELLRSQPNLADDIPVLGHIPKLFNLLSVQPKNTLSVLHQLSLSEFCVSAISQTECVAPLKKCMEHNRDCIEKACEALSRLFKHQHDSLISQSLEVGLIPFLLGLLDSRLEFVDNPSAVKAQIVAALKGMTHNLNYGDRVTQILLKHPVWAEFKDQRHDLFIADTTIRGYLTGVNPTAGYLTAGPAQSVEVLTSPPPIDRDDPSARPPID
Protein: DNA cross-link repair protein SNM1 (AtSNM1) (Q38961)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be required for repair of DNA lesions formed after exposure to oxidative stress.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- ARM repeat superfamily protein
- Protein SIEL
- Embryo defective 2739
- ATP-dependent DNA helicase 2 subunit KU80
- ATP-dependent DNA helicase 2 subunit KU70
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- 30-kDa cleavage and polyadenylation specificity factor 30
- Protein GAMETOPHYTE DEFECTIVE 1
- DNA ligase 4
- Zinc finger CCCH domain-containing protein 65
Sequence:
MDFSDEDDDENCFGSRFNDGVNEEEEDEEGFVFNDDVEENEEEEGFASDFYKAGSDWSCLVEDEETVSSSVKKMKQSNLFQIWGLQENSPDTTKKMKQTDLFQSWGLQKPSPFTSPASNSAKKTTSALGKRRRDSSFSNDSPRPCPFYKKLPGTPFTVDAFRYGCVQGCSAYFLTHFHADHYIGLTKAWSHGPIYCSSLTSRLLRLSLSVNPSSIHPLELDVEYTINGIKVTLIEANHCPGAALIHFRLLDGTCYLHTGDFRASKQMQTHPLLFNQRVHVLYLDTTYCNPRYKFPSKEDVLSYVVRITKDFLRKQPKTLIVVGSYSIGKECVYLAIAKALGVKIFANASRRRILQSFGWDDISKNLSTDGKATCLHVLPMSSLKVERLDEHLKIYREQYGAVLAFRPTGWTYSEKIGEHLDLIKPTSRGKITIYGVPYSEHSSFTELREFVQFLRPDKIIPTVNNGNAGTREKMQSCFREWLRR
Protein: Serine protease inhibitor kazal-like protein, minor form (SPINKL, minor form) [Cleaved into: Serine protease inhibitor kazal-like protein, major form (SPINKL, major form)] (Q8CEK3)
Organism: Mus musculus (Mouse)
Function: Does not function as an inhibitor of trypsin, chymotrypsin, subtilisin or elastase. Binds sperm and enhances sperm motility. May act as a decapacitation factor, suppresses BSA-stimulated sperm capacitation and blocks sperm-oocyte interactions in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:18715980}.
Interaction partners:
- Semenogelin 1
- Seminal vesicle secretory protein 4
- Seminal vesicle secretory protein 3A
- Prostate and testis expressed protein 4
- Seminal vesicle secretory protein 6
- Seminal vesicle secretory protein 5
- Prolactin-induced protein
Sequence:
MSSTWIKFLFILTLVLLPYSVFSVNIFAGPENVIKEPNCTMYKSKSECSNIAENPVCADDRNTYYNECYFCIEKVVEKLKYRYHGICIYK
Protein: Zinc finger protein 125 (O89005)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PSHLQCHKRRQIGEKTHEHNQCGKAFPTPSHLQYHKRTHTGEKPYECHQCGQAFKNCSQLEHYKRTRTGEKSYECRQCGKAFSQHSHLQRHKRIHTGEKPYECNQCRKAFSQHSLLQRHKRTNWRETHEHNWLKPLHVILISNIIKLNRLERDPMNVINVVKPLQVTVISNIIKEHTLS
Protein: Carbon catabolite repressor protein 4 homolog 6 (CCR4 homolog 6) (EC 3.1.13.4) (Q8VYU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MRRSRFVAQVFSDVTFADASTISAPIFTMSTRAPYRGARGRGRGRGGRSFSDRPYNDDAGRDQFVTGDSHFQSVHDANFRFRHGEPYRQHQPPLDQRQQPPFNQNYEFRPPPPSRGQWQQFRQPNQFPSNQNYAACPPPPFYQNQMSRPPPQQSFRQRPRSKPSDYREWEYAKTPPSPGSEKFVVLSYNILADYLANDHWRSLYFHIPRNMLSWGWRKSKLVFELSLWSADIMCLQEVDKFQDLEEEMKHRGYSAIWKMRTGNAVDGCAIFWRSNRFKLVHEESIQFNQLGLRDNVAQICVLETLLTSHTKENETPPPESSAGSHRVVICNIHVLFNPKRGDFKLGQVRTLLDKAHAVSKLWDDAPIVLCGDFNCTPKSPLYNFISDRKLDLSGLARDKVSGQVSAEFRPPRPENYTTRYQSANKSPQGQVQPPNLITNAHMENNSNIDVGTAPSEKTSELPCGDTILAGHEATSSSDQVLPCENMASDCQFGIENRKPDDSGNLSTAEDLSSLTISDTEPQHASSAREDLNTDRSVSSGLSETEQTPEEICSSDQDISSSLSTKVDTFVAEMKLDGLKLDEPVVFAQDEESLGEDGETFLAKLHDNNENLSQKGELVSEVPLKWSSEALNSDKITYSPSSWTPMEIATATGDPERTTVEHALELKSTYSEVEGQANTRDENGEPVVTSYHRCFMGTVDYIWRSEGLQTVRVLAPIPKQAMQWTPGFPTPKWGSDHIALVSELAFCSSKTLPKS
Protein: Rho GTPase activating protein at 71E, isoform E (M9MRW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSWAERVHRRAADLGNVVTSCGHPATAPAYPYRLEKVKFGVPLEEVCKHNNNIPGPLLVLILKLNKESPNRRDVFRAPGHQGAMKKLIHFLQAGRLVNVDNYSVFTIASVLKKFLRKIPNGIFGRSGEMELFAINDLQNEAEQTERLHRLFGSLPKYTQHLLVLLFGTFRVIASNAAHASTGMTSEALGVSVAPSFFQSCVSDGKTARMEDVLKFKVSTKIMQNIIDKFATHDIFGRDNYEYYARVTGRILKVQDEWICSFQYPPPPRGKLAQQKYALQHSLEAEKTWLQCQCERWGLLAQEESRSTPALLTSSSSALENSVLSLGVSPEHSFIESCARLSVSLEGPGIYAMTSSPLPAKRNGNGNGNATDYDYDDYADDDEDNDELDGVHDFGAELEISSIAPPQGSRGIYRHKQRAQQQPHHYQQQQQQQQVPPQHQRDYDEDDDDDEDEMTFIKRRYRQNKKKPAPPSSSHHQRRLRTGTKSLDGGGERRTGSGAAGGSGGGASGSAVGNPTPPKLKQRTCSRCNRGIRHSSSCSSNSAGATGSNSGGGGNGGSGAGNGGGAEGGMTMEELRAVNRYAESTKSLSYLPQLATSV