wanglab/gogpt-training-data huggingface dataset:
Protein: ERO1-like protein 1 (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductin-1-like protein A) (O74401)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly pdi1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on pdi1 to transfer oxidizing equivalent. Does not oxidize all pdi related proteins, suggesting that it can discriminate between pdi1 and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15449306}; Peripheral membrane protein {ECO:0000269|PubMed:15449306}; Lumenal side {ECO:0000269|PubMed:15449306}.
Interaction partners:
- Thioredoxin domain-containing protein C959.05c
- Uncharacterized protein C1840.08c
- Protein disulfide-isomerase C17H9.14c
- Uncharacterized protein C3D6.13c
- Putative protein disulfide-isomerase C1F5.02
- 5-aminolevulinate synthase, mitochondrial
Sequence:
MIGITKLISIWNAIWNFLLLPEIIISQTDTSSTGIYQMQSKVRSLVPVLTERSDYFSYYRVNLYRSSCPLWENDNAMCSNQGCAVKSLNEIEIPKVWKKLSDFEPHSKKNDTKCNWKYNPDLDYCYLDNSTSPDEYVYVSLVQNPERFTGYAGDHSAAIWRSIYEQNCFVVDDDDNPSEQPKSNALFRPNQIPLNLFTENHDDTSLSPSVACLEKRMFNRIISGFHASISTHVCQNYYDVEEQRWTQNLDWWRAKVGSFPDRIENIFFNYALLHQALVQIATQMKNITSDSSFTFCPTDKDVDWRTHTAFEQLVYHAYQDRHVINREQFFADEEAKRFKDSFRKHFRDISRIMDCVGCDKCRLWGKVQITGYGTALKLLLEPETQLSDLRPEEVVALVNTFDRISHSVEATFWFSLKAKTNDTLDAIKALIYKTYRSPSKEILAFFIDQTWYLFYALFFICNVPRVI
Protein: Intraflagellar transport protein 70B (Tetratricopeptide repeat protein 30B) (TPR repeat protein 30B) (Q9CY00)
Organism: Mus musculus (Mouse)
Function: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 56
- Intraflagellar transport protein 172 homolog
- TRAF3-interacting protein 1
Sequence:
MAGLSSSQIPDGEFTAVVYRLIRDSRYSEAVQLLSAELQRSSRSRAGLSLLAYCYYRLQEFELAAECYEQLSQMHPELEQYRLYQAQALYKACLYPEATRVAFLLDNPAYQTRVLRLQAAIKYSEGDLPGARSLVEQLLSGEGVEDSGGESDYDGQINLGCLLYKEGHYEAACSKFLAALQASGYQPDLSYNLALAYYSSRQYAPALKHIADIIERGIRQHPELGVGMTTEGIDVRSVGNTIVLHQTALVEAFNLKAAIEYQLRNYEAAQEALTDMPPRAEEELDPVTLHNQALMNMDAKPTEGFEKLQFLLQQNPFPPETFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYDFLDAMITCQTAPEEAFIKLDGLAGMLTEQLRKLTIQVQDSRHSRDDESAKKAVNEYDETLEKYIPVLMAQAKIYWNFENYPMVEKIFRKSVEFCNDHDVWKLNVAHVLFMQENKYKEAIGFYEPIVKKNYDNILSVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQLSYGDPDKKIYHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYHKKLGTDTWYYAKRCFLSLLENMSKHTIMLRDSVIQECVQFLEHCELYGRNIPAVIEQPLEEERMHTGKNTVTYESRKLRALIYEIIGWNV
Protein: Vitamin K-dependent protein S (Q08761)
Organism: Mus musculus (Mouse)
Function: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
Subcellular location: Secreted.
Interaction partners:
- Tyrosine-protein kinase Mer
- Tyrosine-protein kinase receptor TYRO3
- Tyrosine-protein kinase receptor UFO
- Vitamin K-dependent gamma-carboxylase
- Coagulation factor V
- Coagulation factor VIII
- Growth arrest-specific protein 6
- Matrix Gla protein
- Furin
- Vitamin K-dependent protein C
Sequence:
MRVLSARFRVLLACLALVIPVSETNFLSKERASQVLVRKRRANTLFEETMKGNLERECIEELCNKEEAREVFENNPETDYFYPKYLGCLGAFRVGSFHAARQSANAYPDLRSCVKAISDQCDPIPCNEDGYLACQDGQAAFTCFCKPGWQGDRCQYDVNECKDPSNVNGGCSQICDNTPGSYHCSCKRGFAMLPNKKDCKDLDECALKPSVCGTAVCKNIPGDFECECPDGYRYDPSSKSCKDVDECSENMCAQLCVNFPGGYSCYCDGKKGFKLAQDQKSCEGIPVCLSLDLDKNYELLYLAEQFAGVVLYLKFRLPDITRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNINKLGSLFKPTDGFLDTKIYFAGLPRKVESALIKPINPRLDGCIRGWNLMKQGALGAKEIIEGKQNKHCFLNVEKGSYYPGSGIAQFSIDYNNVTNAEGWQMNVTLNIRPSTGTGVMLALVSGGTVPFALSLVDSRSGTSQDIVVFVENSVVARLEAVSLCSDQQSQLKCNVNRNGLELWTPLRKDVIYSKDLQRQLAVLDKAMKRTVATYLGGIPDISFSATPVNAFYSGCMEVNINGVQLDLDEAISKHKDIRAHSCPSVRKIQKNF
Protein: Fatty acid binding protein, isoform B (GEO09480p1) (RH06221p) (RH49003p) (Q9VGM2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFVGKKYKLDKSENFDEYMKELGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGDKPTTIVREFTDNELITTLTIGNVKCVRVYKAV
Protein: Tropinone reductase homolog At2g29330 (EC 1.1.1.-) (Q9ZW16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reductase active only on small flexible lipophilic carbonyls. No activity with cyclic monoterpenes, tropinone, nitrogen-containing tropinone analogs, tropine or pseudotropine as substrate.
Interaction partners:
- strictosidine synthase
- Protein STRICTOSIDINE SYNTHASE-LIKE 11
- Protein STRICTOSIDINE SYNTHASE-LIKE 2
- Protein STRICTOSIDINE SYNTHASE-LIKE 12
Sequence:
MDKRWSLQGLTALVTGGASGIGHAIVEELAGFGAKIHVCDISKTLLNQSLSEWEKKGFQVSGSVCDASNRLERETLMQTVTTIFDGKLNILVNNVGTIRTKPTIEYEAEDFSFLISTNLESAYHLSQLSHPLLKASGNGIITFISSAAGIVSFDAASIYGLTKGALNQLARNLACEWAKDGIRANAVAPNFITTALAKPFLEDAGFNEILSSRTPLGRAGEPREVASLVAFLCLPAASYITGQTICVDGGLTVNGFSYQP
Protein: Solute carrier family 7 member 11 (D4ADU2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- CD44 antigen
- Phospholipid hydroperoxide glutathione peroxidase
- Beclin-1
Sequence:
MVRKPVVATISKGGYLQGNVSGRLPSVGDQEPPGHEKVVLKKKITLLRGVSIIIGTVIGSGIFISPKGILQNTGSVGMSLVFWSACGVLSLFGALSYAELGTSIKKSGGHYTYILEVFGPLLAFVRVWVELLVIRPGATAVISLAFGRYILEPFFIQCEIPELAIKLVTAVGITVVMVLNSTSVSWSARIQIFLTFCKLTAILIIIVPGVIQLIKGQTHHFKDAFSGRDTNLMGLPLAFYYGMYAYAGWFYLNFITEEVDNPEKTIPLAICISMAIITVGYVLTNVAYFTTISAEELLQSSAVAVTFSERLLGKFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVHKHTPLPAVIVLHPLTMIMLFSGDLYSLLNFLSFARWLFMGLAVAGLIYLRYKRPDMHRPFKVPLFIPALFSFTCLFMVVLSLYSDPFSTGVGFLITLTGVPAYYLFIVWDKKPKWFRRLSAHHPPELGGKKG
Protein: Galactose oxidase/kelch repeat superfamily protein (F4KAN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEWDSGSDLSADDASSLADDEEGGLFPGGGPIPYPVGNLLHTAPCGFVVTDAVEPDQPIIYVNTVFEMVTGYRAEEVLGGNCRFLQCRGPFAKRRHPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQFFIETDIDLGPVLGSSTKEKSIDGIYSALAAGERNVSRGMCGLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVCQNAWGSETTRVLETVPGAKRLGWGRLARELTTLEAAAWRKLSVGGSVEPSRCNFSACAVGNRVVLFGGEGVNMQPMNDTFVLDLNSDYPEWQHVKVSSPPPGRWGHTLTCVNGSNLVVFGGCGQQGLLNDVFVLNLDAKPPTWREISGLAPPLPRSWHSSCTLDGTKLIVSGGCADSGVLLSDTFLLDLSIEKPVWREIPAAWTPPSRLGHTLSVYGGRKILMFGGLAKSGPLKFRSSDVFTMDLSEEEPCWRCVTGSGMPGAGNPGGVAPPPRLDHVAVNLPGGRILIFGGSVAGLHSASQLYLLDPTEDKPTWRILNIPGRPPRFAWGHGTCVVGGTRAIVLGGQTGEEWMLRYWSFRGERLSGGTLVLLIFFKSFFFFLPH
Protein: protein disulfide-isomerase (EC 5.3.4.1) (I3L514)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKMPHGVVTANSWLPFGINWERRTRTMRTSSSPRWTRLPTRWRPSKCTASPHSSSFLPVPTGRSLITTGNARWMVLRNSWRAVARMGQGMMTISRTWKKQRSQTWRKTMIRKL
Protein: Thyroid hormone receptor interactor 11 (H3BJU5)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
XEVLQNLLKEKDLLIKAKSDQLHSSNENLANKVNENELLRQAVTNLKERILILEMDISKLKGENEKIVDASKGKETEYQALQETNMKFSMMLREKEFECHSMREKALAFEQLLKEKEQLNQCRRRQLRFSRKETKLCWP
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 (Complex I-B14.7) (CI-B14.7) (NADH-ubiquinone oxidoreductase subunit B14.7) (Q86Y39)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Multi-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase flavoprotein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- Cytochrome b-c1 complex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
Sequence:
MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYTFTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARTHNYGIGAAACVYFGIAASLVKMGRLEGWEVFAKPKV
Protein: Integrin alpha-5 (CD49 antigen-like family member E) (Fibronectin receptor subunit alpha) (Integrin alpha-F) (VLA-5) (CD antigen CD49e) [Cleaved into: Integrin alpha-5 heavy chain; Integrin alpha-5 light chain] (P08648)
Organism: Homo sapiens (Human)
Function: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17158881}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}.
Interaction partners:
- Integrin beta-3
- Integrin beta-1
- Fibronectin
- Integrin beta-2
- Integrin beta-5
- Integrin beta-7
- Talin-1
- Vitronectin
- Scaffold protein ILK
- Focal adhesion kinase 1
Sequence:
MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA
Protein: Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (JV5-1) (SMAD family member 5) (SMAD 5) (Smad5) (hSmad5) (Q99717)
Organism: Homo sapiens (Human)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16516194, ECO:0000269|PubMed:28675158, ECO:0000269|PubMed:9442019}. Nucleus {ECO:0000269|PubMed:28675158, ECO:0000269|PubMed:9442019}. Mitochondrion {ECO:0000269|PubMed:12849988}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. {ECO:0000269|PubMed:9442019}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 9
- E3 ubiquitin-protein ligase SMURF1
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1B
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 7
Sequence:
MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHNEFNPQHSLLVQFRNLSHNEPHMPQNATFPDSFHQPNNTPFPLSPNSPYPPSPASSTYPNSPASSGPGSPFQLPADTPPPAYMPPDDQMGQDNSQPMDTSNNMIPQIMPSISSRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKSRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSSCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS
Protein: C3H1-type domain-containing protein (Q57VA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleobase/nucleoside transporter 8.1
Sequence:
MAKKNKHVEVKPSKYRTTLCEHYQRDGQCPYGDRCAFAHGEHQLHTEEQNMKLLRETGLRRLDGVALPVKTPTRGMPSDSPSLVLTPTMRRQPTFISLPSQLTAEKDATQGGEGSEGGSKQVYNSITESSDSDKEPPHPKCRSEFSASCSTENPMRYRHNPYGLYVF
Protein: Bile salt-activated lipase (BAL) (EC 3.1.1.13) (EC 3.1.1.3) (EC 3.1.1.6) (Bile salt-stimulated lipase) (BSSL) (Bucelipase) (Carboxyl ester lipase) (Cholesterol esterase) (Pancreatic lysophospholipase) (Sterol esterase) (P19835)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs). Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins.
Subcellular location: Secreted {ECO:0000269|PubMed:21784842}.
Interaction partners:
- Pancreatic triacylglycerol lipase
- Inactive pancreatic lipase-related protein 1
- Gastric triacylglycerol lipase
- Carboxypeptidase A1
- Lipoprotein lipase
- Pancreatic lipase-related protein 3
- Lysosomal acid lipase/cholesteryl ester hydrolase
- Hepatic triacylglycerol lipase
- Chymotrypsin-like protease CTRL-1
- Monoglyceride lipase
Sequence:
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF
Protein: SAC3 family protein A (F4IUY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the TREX-2 complex (transcription and export complex 2), a muliprotein complex that functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.
Subcellular location: Nucleus {ECO:0000269|PubMed:19843313}.
Interaction partners:
- Enhanced ethylene response protein 5
- Protein DSS1 HOMOLOG ON CHROMOSOME V
- Protein DELETION OF SUV3 SUPPRESSOR 1
- SAC3 family protein C
- Mediator of RNA polymerase II transcription subunit 20b
- Mediator of RNA polymerase II transcription subunit 20a
- Probable calcium-binding protein CML20
- Serine/threonine-protein kinase PRP4 homolog
- Mediator of RNA polymerase II transcription subunit 18
- At5g58020
Sequence:
MNHGGNTQAVAPMDPNSIENRYGVDGSQTQKYSYQYSTGSESAPWTGHSVENQAVENGNYSNSNYYHPQPTGPATGNVQEIPNTVSFTISSTSGTANVAQDYSGYTPYQTSSDPHNYSNTGYSNYYSGYQQQPSQSYPQPVGAYQNTGAPQPLSSFQNPGSYAGTPSYSGTYYNPADYQTAGGYQSTNYNNQTAGSYPSTNYSNQTPASNQGNYTDYTSNPYQNYTPDAANTHSSTIATTPPVHYQQNYQQWTEYYSQTEVPCAPGTEKLSTPTTSAYSQSFPVPGVTSEMPASNSQPAPSYVQPWRPETDSSHPPSQQPGAAVSTSNDTYWMHQAPSLQAHHPVPPQNNYQSPLETKPLYETPFQGHQRATYPQEMNSQSSFHQAPLGYRQPTQTAPLVDSQRVSKVQIPTNPRIASNLPSGFTKMDKDSTAASAAQAPAYVSVSMPKPKDHTTAMSDPGTFPKSLRGFVERAFARCKDDKEKESCEVALRKIVKKAKEDNTLYTRDWDTEPLSTVTTTNVTNSESSSAQLSSLQNKSPTRRPKSRWEPLVEGKPFVKPASTFSSAVKFGVWNHQNENNKKSSESFQKVDAATGFKPTYSGQNSAKKSFQRPVKRQRFSGGAATAIDDEASSDSDKDLTPYYSSAMALAGSAEEKKRRDSRSKRFEKIQGHSRGNDLTKPKNANVGNLHSRRATALRLSKVFDESGSRAVEDIDWDALTVKGTCQEIEKRYLRLTSAPDPATVRPEDVLEKALIMVQDSQKNYLFKCDQLKSIRQDLTVQRIHNHLTAKVYETHARLALEAGDLPEYNQCLSQLKTLYAEGVEGCSLEFAAYSLLYITLHSNNNRELLSSMSRLSEEDKKDEAVRHALSVRAAVTSGNYVMFFRLYKTAPNMNSCLMDLYVEKMRYKAVNFMSRSCRPTIPVSYIVQVLGFTGAASEGTDEKETDGMEDCLEWLKTHGANIITDSNGDMLLDTKATSTSLFMPEPEDAVAHGDRNLDVNDFFTRT
Protein: Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Q99KB8)
Organism: Mus musculus (Mouse)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: [Isoform 1]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16775}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q16775}.
Interaction partners:
- Lactoylglutathione lyase
- Probable D-lactate dehydrogenase, mitochondrial
Sequence:
MVLGRGSLCLRSLSALGATCARRGLGQALLGLSLCHSDFRKNLTVQQDIMKVELLPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGDDRIGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGRLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKDQFKVPRD
Protein: HDC02844 (RE53210p) (SQUASH) (Squash, isoform B) (Squash, isoform C) (Q7KT57)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Autophagy-related 1, isoform B
- RB1-inducible coiled-coil protein 1
- Autophagy-related protein 13 homolog
- Autophagy protein 5
- Autophagy-related 8a, isoform A
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related 8b, isoform A
- Autophagy protein 12-like
- Autophagy-related protein 9
- Autophagy-related 18a, isoform E
Sequence:
MAWVPNSQFEDDLVDMEPDFNFVHGQLAYDMKKQGEFWPRPKCTYEYLKSREKRNSELENIHGSRGGTGRDIRQSLQLMENIQKIAGTRPLGEHATMKDWEDESTNELEALAMMRHFGMMSMATDSLPVLPEVKPPEGPIKIIRNGRKQFPLITDPEFFKPRKIPRTKNSSSSSSYHTANSSISSFSLYESAASDLDSSKKQGEIKASKSEKYLEVPYKQLAESYDQEVESPVQFGNQFNE
Protein: ATR-interacting protein (ATM and Rad3-related-interacting protein) (Q8WXE1)
Organism: Homo sapiens (Human)
Function: Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein.
Subcellular location: Nucleus {ECO:0000269|PubMed:11721054, ECO:0000269|PubMed:18283122}. Note=Redistributes to discrete nuclear foci upon DNA damage.
Interaction partners:
- Serine/threonine-protein kinase ATR
- Replication protein A 70 kDa DNA-binding subunit
- DNA topoisomerase 2-binding protein 1
- Serine-protein kinase ATM
- Cell cycle checkpoint control protein RAD9A
- Serine/threonine-protein kinase Chk1
- Cell cycle checkpoint protein RAD17
- Replication protein A 32 kDa subunit
- DNA replication licensing factor MCM7
- Claspin
Sequence:
MAGTSAPGSKRRSEPPAPRPGPPPGTGHPPSKRARGFSAAAAPDPDDPFGAHGDFTADDLEELDTLASQALSQCPAAARDVSSDHKVHRLLDGMSKNPSGKNRETVPIKDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQSELQFKDAEMNELRTKLQTSERANKLAAPSVSHVSPRKNPSVVIKPEACSPQFGKTSFPTKESFSANMSLPHPCQTESGYKPLVGREDSKPHSLRGDSIKQEEAQKSFVDSWRQRSNTQGSILINLLLKQPLIPGSSLSLCHLLSSSSESPAGTPLQPPGFGSTLAGMSGLRTTGSYDGSFSLSALREAQNLAFTGLNLVARNECSRDGDPAEGGRRAFPLCQLPGAVHFLPLVQFFIGLHCQALQDLAAAKRSGAPGDSPTHSSCVSSGVETNPEDSVCILEGFSVTALSILQHLVCHSGAVVSLLLSGVGADSAAGEGNRSLVHRLSDGDMTSALRGVADDQGQHPLLKMLLHLLAFSSAATGHLQASVLTQCLKVLVKLAENTSCDFLPRFQCVFQVLPKCLSPETPLPSVLLAVELLSLLADHDQLAPQLCSHSEGCLLLLLYMYITSRPDRVALETQWLQLEQEVVWLLAKLGVQSPLPPVTGSNCQCNVEVVRALTVMLHRQWLTVRRAGGPPRTDQQRRTVRCLRDTVLLLHGLSQKDKLFMMHCVEVLHQFDQVMPGVSMLIRGLPDVTDCEEAALDDLCAAETDVEDPEVECG
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A8I6A8Z4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
TLMKRLAARCFAGLLILSPLTVISDSRSADSGKAIEDGNLEEMEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEEESNEEEEEEDEEESEAEAKSVKVKIKLNKKEEKGRDTGKGKKRPNRGKAKPVVSDFDSDEEQDENEQSEASGTDDE
Protein: E3 ubiquitin-protein ligase SspH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SspH2) (Salmonella secreted protein H2) (Secreted effector protein sspH2) (D0ZPH9)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Contributes to virulence in calves.
Subcellular location: Secreted. Host cytoplasm. Host apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. Localizes at the periphery of the host cell, specifically in areas of actin polymerization. Localizes to the apical membrane of polarized epithelial cells.
Interaction partners:
Sequence:
MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVINRFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEEGTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPALPSELCKLWAYNNQLTSLPMLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITSAPGYSGPIIRFDMAGASAPRETRALHLAAADWLVPAREGEPAPADRWHMFGQEDNADAFSLFLDRLSETENFIKDAGFKAQISSWLAQLAEDEALRANTFAMATEATSSCEDRVTFFLHQMKNVQLVHNAEKGQYDNDLAALVATGREMFRLGKLEQIAREKVRTLALVDEIEVWLAYQNKLKKSLGLTSVTSEMRFFDVSGVTVTDLQDAELQVKAAEKSEFREWILQWGPLHRVLERKAPERVNALREKQISDYEETYRMLSDTELRPSGLVGNTDAERTIGARAMESAKKTFLDGLRPLVEEMLGSYLNVQWRRN