wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic AMP-dependent transcription factor ATF-6 beta (cAMP-dependent transcription factor ATF-6 beta) (Activating transcription factor 6 beta) (ATF6-beta) (cAMP response element-binding protein-related protein) (Creb-rp) (cAMP-responsive element-binding protein-like 1) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 beta] (O35451)
Organism: Mus musculus (Mouse)
Function: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 beta), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99941}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 beta]: Nucleus {ECO:0000250|UniProtKB:Q99941}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250|UniProtKB:Q99941}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- DNA damage-inducible transcript 3 protein
- Wolframin
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Cyclic AMP-responsive element-binding protein 3
- Cyclic AMP-responsive element-binding protein 3-like protein 4
Sequence:
MAELMLLSEIADPTRFFTDNLLSPEDWDSTLYSGLDEVAEEQAQLFRCVEQDVPFDSSSLDVGMDVSPPEPPWDPLPIFPDLQVKSEPSSPCSSSSLSSESSHLSTEPPSQVPGVGEVLHVKMESLAPPLCLLGDDPASPFETVQITVGSASDDLSDIQTKLEPASPSSSVHSEASLLSADSPSQPFIGEEVLEVKTESPSPPGCLLWDVPASSLGAVQISMGPSPDSSSGKAPATRKPPLQPKPVVLTTVPVPPRAGPTSAAVLLQPLVQQPAVSPVVLIQGAIRVQPEGPAPAAPRPERKSIVPAPMPGNSCPPEVDAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSGLKLGSGNRKVVCIMVFLLFIAFNFGPVSISEPPPAPMSPRMSREEPRPQRHLLGFSEPGPAHGMEPLREAAQSPGEQQPSSAGRPSFRNLTAFPGGAKELLLRDLDQLFLSSDCRHFNRTESLRLADELSGWVQRHQRGRRKIPHRAQERQKSQLRKKSPPVKPVPTQPPGPPERDPVGQLQLYRHPGRSQPEFLDAIDRREDTFYVVSFRRDHLLLPAISHNKTSRPKMSLVMPAMAPNETVSGRGPPGDYEEMMQIECEVMDTRVIHIKTSTVPPSLRKQPSPSPGNTTGGPLPGSAASPAHQASQPLYLNHP
Protein: Transcriptional adapter 2 (Q02336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B.
Subcellular location: Nucleus.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex subunit SPT3
- Ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex subunit SGF11
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SPT7
- SAGA complex subunit NGG1
- Histone acetyltransferase GCN5
Sequence:
MSNKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPILCPDWGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDITQNIHVPQDEFLEQRRHRIESFRERPLEPPRKPMASVPSCHEVQGFMPGRLEFETEFENEAEGPVKDMVFEPDDQPLDIELKFAILDIYNSRLTTRAEKKRLLFENHLMDYRKLQAIDKKRSKEAKELYNRIKPFARVMTAQDFEEFSKDILEELHCRARIQQLQEWRSNGLTTLEAGLKYERDKQARISSFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQNYSENGGRKKNMTISDIQHAPDYALLSNDEQQLCIQLKILPKPYLVLKEVMFRELLKTGGNLSKSACRELLNIDPIKANRIYDFFQSQNWM
Protein: Calsequestrin-2 (Calsequestrin, cardiac muscle isoform) (P12637)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000250|UniProtKB:O09161}.
Interaction partners:
- Ryanodine receptor 2.
- Ryanodine receptor 1.
- Triadin
- Ryanodine receptor 3.
- Calsequestrin
- Calmodulin like 5.
- Calmodulin like 4.
- Uncharacterized protein
- Calmodulin 2
Sequence:
MKRTHLFIAGLYLLASCRAEEGLNFPTYDGKDRVVSLTEKNFKQVLKKYDVLCLYYHESVSSDKVAQKQFQLKEIVLELVAQVLEHKDIGFVMVDAKKEAKLAKKLGFDEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIINSKLEVQAFERIEDQIKLIGFFKSEESEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPDKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAERSDPDGYEFLEILKQVARDNTDNPDLSIVWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEEGDDGDDDEDDDDDDGNNSDEESNDDSDDDDE
Protein: Probable UDP-arabinopyranose mutase 4 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 4) (AtRGP4) (UDP-L-arabinose mutase 4) (Q9LUE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}. Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Soluble and membrane-associated.
Interaction partners:
- UDP-sugar pyrophosphorylase
- Two-component response regulator ARR22-like protein
- Actin-related protein 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Methylesterase 4
- F-actin-capping protein subunit beta
- Actin-related protein 9
- DEAD-box ATP-dependent RNA helicase 9, mitochondrial
- Chromatin structure-remodeling complex protein SYD
Sequence:
MAGYNLEAIEAAPLKDDLDIVIPTIRSLDFLEQWRPFLHHYHLIIVQDGDPSIKIRVPEGYDYELYNRNDINRILGPRANCISYKDGGCRCFGFMVSKKKYIYTIDDDCFVAKDPSGKDINVIAQHIKNLETPSTPHYFNTLYDPFRDGTDFVRGYPFSLREGVQTAISHGLWLNIPDYDAPTQLVKPRERNTRYVDAVMTIPKRVLYPMCGMNLAFNRELVGPAMYFGLMGEGQPISRYDDMWAGWAAKVVCDHLGFGVKTGLPYLWHSKASNPFVNLKKEHKGLHWQEDMVPFFQNLRLSKESDTAAKCYMEISNMTKEKLTKVDPYFEKLADAMVVWIEAWEELNPPVKKKQSDGKDVKAK
Protein: Dehydration-responsive element-binding protein 1D (Protein DREB1D) (C-repeat/dehydration-responsive element-binding factor 4) (C-repeat-binding factor 4) (CRT/DRE-binding factor 4) (Q9FJ93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates abscisic acid- and dehydration-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Low-temperature-induced 78 kDa protein
- Floral homeotic protein APETALA 2
- Protein COLD-REGULATED 15A, chloroplastic
- H/ACA ribonucleoprotein complex subunit 4
- NAC domain-containing protein 72
- Transcription factor ICE1
- Low-temperature-induced 65 kDa protein
- Stress-induced protein KIN2
- Basic leucine zipper 8
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
Sequence:
MNPFYSTFPDSFLSISDHRSPVSDSSECSPKLASSCPKKRAGRKKFRETRHPIYRGVRQRNSGKWVCEVREPNKKSRIWLGTFPTVEMAARAHDVAALALRGRSACLNFADSAWRLRIPETTCPKEIQKAASEAAMAFQNETTTEGSKTAAEAEEAAGEGVREGERRAEEQNGGVFYMDDEALLGMPNFFENMAEGMLLPPPEVGWNHNDFDGVGDVSLWSFDE
Protein: Uncharacterized protein YKL063C (P35725)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MQGDIRRKKDLLPRYKTGSKYNSRRRGGYLTTPMKKIIVYIILLCGVYFVIKVAYSDLNKETEIKLESHSSDVSASASDHTNIAAGGAADATNNKQPQQAKVPKEKFNNEVAKQQEVKNLENDLKPQIDSEKQKQINKDKKEQKQQLQKEKQDLAKENLANNEILDN
Protein: Cell adhesion molecule CEACAM6 (Carcinoembryonic antigen-related cell adhesion molecule 6) (CEA cell adhesion molecule 6) (Non-specific crossreacting antigen) (Normal cross-reacting antigen) (CD antigen CD66c) (P40199)
Organism: Homo sapiens (Human)
Function: Cell surface glycoprotein that plays a role in cell adhesion and tumor progression. Intercellular adhesion occurs in a calcium- and fibronectin-independent manner. Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM5 and CEACAM8. Heterophilic interaction with CEACAM8 occurs in activated neutrophils. Plays a role in neutrophil adhesion to cytokine-activated endothelial cells. Plays a role as an oncogene by promoting tumor progression; positively regulates cell migration, cell adhesion to endothelial cells and cell invasion. Also involved in the metastatic cascade process by inducing gain resistance to anoikis of pancreatic adenocarcinoma and colorectal carcinoma cells.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2317824}. Apical cell membrane {ECO:0000269|PubMed:10436421}. Cell surface {ECO:0000269|PubMed:1378450, ECO:0000269|PubMed:16204051, ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:8776764, ECO:0000305|PubMed:2803308}. Note=Localized to the apical glycocalyx surface. {ECO:0000269|PubMed:10436421}.
Interaction partners:
- Cell adhesion molecule CEACAM8
- Cell adhesion molecule CEACAM1
- Defensin alpha 4
- Cell adhesion molecule CEACAM5
- Fibronectin
Sequence:
MGPPSAPPCRLHVPWKEVLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLAHNLPQNRIGYSWYKGERVDGNSLIVGYVIGTQQATPGPAYSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPEVQNTTYLWWVNGQSLPVSPRLQLSNGNMTLTLLSVKRNDAGSYECEIQNPASANRSDPVTLNVLYGPDVPTISPSKANYRPGENLNLSCHAASNPPAQYSWFINGTFQQSTQELFIPNITVNNSGSYMCQAHNSATGLNRTTVTMITVSGSAPVLSAVATVGITIGVLARVALI
Protein: Micronemal protein 1 (TgMIC1) (O00834)
Organism: Toxoplasma gondii
Function: Adhesin. Required for attachment of the parasite to the host cell prior to invasion. Ensures correct folding of MIC6 and transport of the MIC6-MIC1-MIC4 complex into the micronemes.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:11157983, ECO:0000269|PubMed:15684324, ECO:0000269|PubMed:18818666}. Host early endosome {ECO:0000269|PubMed:33912181}. Note=Localizes to host early endosomes after interacting with host TLR4. {ECO:0000269|PubMed:33912181}.
Interaction partners:
Sequence:
MGQALFLTVLLPVLFGVGPEAYGEASHSHSPASGRYIQQMLDQRCQEIAAELCQSGLRKMCVPSSRIVARNAVGITHQNTLQWRCFDTASLLESNQENNGVNCVDDCGHTIPCPGGVHRQNSNHATRHEILSKLVEEGVQRFCSPYQASANKYCNDKFPGTIARRSKGFGNNVEVAWRCYEKASLLYSVYAECASNCGTTWYCPGGRRGTSTELDKRHYTEEEGIRQAIGSVDSPCSEVEVCLPKDENPPLCLDESGQISRTGGGPPSQPPEMQQPADRSDERGGGKEQSPGGEAQPDHPTKGGNIDLPEKSTSPEKTPKTEIHGDSTKATLEEGQQLTLTFISTKLDVAVGSCHSLVANFLDGFLKFQTGSNSAFDVVEVEEPAGPAVLTIGLGHKGRLAVVLDYTRLNAALGSAAYVVEDSGCSSSEEVSFQGVGSGATLVVTTLGESPTAVSA
Protein: Melanoma-associated antigen B18 (MAGE-B18 antigen) (Q96M61)
Organism: Homo sapiens (Human)
Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BQR7}.
Interaction partners:
- E3 ubiquitin-protein ligase LNX
Sequence:
MPRGQKSKLRAREKRHQARCENQDLGATQATVAEGESPSPAYLLFGDRPQNLPAAETPSIPEALQGAPSTTNAIAPVSCSSNEGASSQDEKSLGSSREAEGWKEDPLNKKVVSLVHFLLQKYETKEPITKGDMIKFVIRKDKCHFNEILKRASEHMELALGVDLKEVDPIRHYYAFFSKLDLTYDETTSDEEKIPKTGLLMIALGVIFLNGNRAPEEAVWEIMNMMGVYADRKHFLYGDPRKVMTKDLVQLKYLEYQQVPNSDPPRYEFLWGPRAHAETSKMKVLEFVAKIHDTVPSAFPSCYEEALRDEEQRTQARAAARAHTAAMANARSRTTSSSFSHAK
Protein: Serine/threonine protein kinase (EC 2.7.11.1) (Q8IL41)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein kinase, putative
- Protein phosphatase PPM5, putative
Sequence:
MSKTEYDILSLVNAVEEFSKYCSEYKKRHLTNYIQSCSVKNQINNNEEVIFKTTLQDFMNKVNMLGNNILQIEKINKCQIPENILYEKNGNKMIYDPKHYNEDKLNNENILEDKNKRNICEHIKSKINDKNFVQNNDYGKNIKIINNINEQNLLMKDKNDYTNISENLYMRKISTEYTSSDRSSEDNVLLHNINNVLVKYVSGLDYTLNIRRISRKDLIEEIKQFYIIHNNNIQLNDYSTYLSDEVINILKQKKDNIKCLDKNNLFIIEKNVDFYKNNFLPFFYIPCNYLFIKNYCNDNERCLETTYDTNDEKNSTTENSYILSSPNHMYNTNTNSYNSHSNSIIARNTSSNKCNSPIFGINERNSSPNFGIFNESIKNHKDQYNMDPNYLIMRYNLNEEVHIKDDRVINSPNNIKSMNDNRYNSPNFNIEHIHINNNDTQINNYDIYDINNMDGKKNNLNSNTSDFYQSISDFYKNNEKNLICQEQNNNNTYIQKCAFFLNSNETNVLTNNKNHHKSGKNLISLCFDDELSSAITINNDSSLNKAIYNEFNNSEKDIVEDICNTTNYKDINMEHMNTYQNDERKWMDEYCNGDYNLFRSKQLKKKKELLLSCISYNEKENKYNDQDNMINVEINNDTKVKNILYDTGNISFDENIGINNHYNTINLKVIYEANKSEYGNNERLNFIKGQIILNKYKVVKVLSKTQFSTTLKCLNLLYKKVKTDTQVFLPYCHKYMKDDSEITHDKKKNNYDKFVNLNTIKKKKNENYNRQHDIKNNLHDNKHQIINNKKKVEPKYVCLKVMKNGKQFLDQGLLELMVLNILCNANTNNNLSNKNIIQLYDSFYYKEHLIIVTEYMQSDLYNYFIRKGKLGTLGQLQILTKNLLEGLAYIHSKNLIHCDLKPENIMINMKKNKKNHEKGKYNKVNQNGVNIYNDTIEPHILNSSNINNSNLEKKNIIAYPSFDQTFIENKDAQYDNNEKTSNVLYDSDKSYNNNVKNMIDNNLYCNNIKNIDNNSDNNNNNNNNNFPHNNINIYNTKQFDKIKIIDFNSCIYESDKLEMYIQTRSYRSPEVLLQQNYDRKIDIWSLGCILFEFLTKKILFDYQNIYRFIYSIVSYIGPFPFYMINNCRIPHIFTKHGLIILKKFTTDNMYENYIKEEQLNQEDDEEIVFNSNDFFRLNKKDNILTKDLLKNKNPNTSTPRKRNNNNNEIYYDVCYPSDNLLKNNFQISDTLFVDFLSSLLQIDPSKRCNAMEALKHPWLQPNLYKDGL
Protein: Cathelicidin antimicrobial peptide (18 kDa cationic antimicrobial protein) (CAP-18) (hCAP-18) [Cleaved into: Antibacterial peptide FALL-39 (FALL-39 peptide antibiotic); Antibacterial peptide LL-37; Antibacterial peptide KR-20; Antibacterial peptide LL-23; Antibacterial peptide LL-29; Antibacterial peptide KS-30; Antibacterial peptide RK-31; Antibacterial peptide FF-33] (P49913)
Organism: Homo sapiens (Human)
Function: Antimicrobial protein that is an integral component of the innate immune system. Binds to bacterial lipopolysaccharides (LPS). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin. The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro).
Subcellular location: Secreted {ECO:0000269|PubMed:14978112}. Vesicle {ECO:0000269|PubMed:7529412, ECO:0000269|PubMed:9736536}. Note=Stored as pro-peptide in granules and phagolysosomes of neutrophils (PubMed:7529412, PubMed:9736536). Secreted in sweat onto skin (PubMed:14978112). {ECO:0000269|PubMed:14978112, ECO:0000269|PubMed:7529412, ECO:0000269|PubMed:9736536}.
Interaction partners:
- N-formyl peptide receptor 2
- Neutrophil elastase
- Myeloblastin
- Myeloperoxidase
- Mas-related G-protein coupled receptor member X2
- Cathepsin G
- Toll-like receptor 9
- Lactotransferrin
- Glyceraldehyde-3-phosphate dehydrogenase
- C-X-C chemokine receptor type 2
Sequence:
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
Protein: Ligand-dependent nuclear receptor corepressor-like protein (LCoR-like protein) (Q8N3X6)
Organism: Homo sapiens (Human)
Function: May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. May play a role in spermatogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320}.
Interaction partners:
- Condensin complex subunit 3
- C-terminal-binding protein 1
- Protein FAM184B
- DDB1- and CUL4-associated factor 16
- Zinc finger protein PLAG1
Sequence:
MDKGRERMAAAAAAAAAAAAAAQCRSPRCAAERRGFRRELDSWRHRLMHCVGFESILEGLYGPRLRRDLSLFEDCEPEELTDWSMDEKCSFCNLQREAVSDCIPSLDSSQSTPTEELSSQGQSNTDKIECQAENYLNALFRKKDLPQNCDPNIPLVAQELMKKMIRQFAIEYISKSGKTQENRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNREDYVERSAEFADGLLSKALKDIQSGALDINKAGILYGIPQKTLLLHLEALPAGKPASFKNKTRDFHDSYSYKDSKETCAVLQKVALWARAQAERTEKSKLNLLETSEIKFPTASTYLHQLTLQKMVTQFKEKNESLQYETSNPTVQLKIPQLRVSSVSKSQPDGSGLLDVMYQVSKTSSVLEGSALQKLKNILPKQNKIECSGPVTHSSVDSYFLHGDLSPLCLNSKNGTVDGTSENTEDGLDRKDSKQPRKKRGRYRQYDHEIMEEAIAMVMSGKMSVSKAQGIYGVPHSTLEYKVKERSGTLKTPPKKKLRLPDTGLYNMTDSGTGSCKNSSKPV
Protein: ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein) (Q8N6T3)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor 1
- Mannosyl-oligosaccharide glucosidase
- ADP-ribosylation factor GTPase-activating protein 2
- ADP-ribosylation factor 6
- ADP-ribosylation factor GTPase-activating protein 3
- ER lumen protein-retaining receptor 1
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor 5
- AP-2 complex subunit beta
- Enhancer of mRNA-decapping protein 4
Sequence:
MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLESQEDYDPCWSLQEKYNSRAAALFRDKVVALAEGREWSLESSPAQNWTPPQPRTLPSMVHRVSGQPQSVTASSDKAFEDWLNDDLGSYQGAQGNRYVGFGNTPPPQKKEDDFLNNAMSSLYSGWSSFTTGASRFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGKIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHFQNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRSSDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGWDNQNW
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (Q59TD1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MTEEEKKRLQVLERDAETAYPFLASDEKSSTFKTAEDLESGINPLVSIATTNESQQKLDNVSSISTTTNEKPKPKPKPWVHFVAGGIGGTVGAVVTCPLDVVKTRLQSDVYHSMYNKIPKSGNPIIQAWQHLSETGSVLRGMYINEGASSLFKGLGPNLVGVIPARSINFFTYGATKEFLLGNFSPTNSIQGPRQEETWIHLVSGINAGFVTSTATNPIWLIKTRLQLDKSKGKNYKNSWDCFKHIIKHEGFTSLYRGLSASYLGGIESTIQWVLYEQMRMFINKRSLQIHGNDPSNKTTKDHILEWSARSGAAGLAKFMASLITYPHEVVRTRLRQAPLESTGKPKYTGLIQCFKLVIKEEGFGSMYGGLTPHLLRTVPNSIIMFGTWELVVRLLSEW
Protein: SPS-sensor component SSY1 (Amino-acid permease homolog SSY1) (Q03770)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Amino acid sensor component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Amino-acid permease homolog that seems to interact directly with the extracellular signaling molecules, but has no amino acid transporter activity. May recruit casein kinases YCK1 and YCK2 to hyperphosphorylate and activate downstream component PTR3 in response to amino acid stimulus.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269}; Multi-pass membrane protein {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269}.
Interaction partners:
- SPS-sensor component PTR3
- SPS-sensor serine protease component SSY5
- Transcription factor STP2
- Transcription factor STP1
- General amino-acid permease GAP1
- Peptide transporter PTR2
- ERAD-associated E3 ubiquitin-protein ligase ASI1
- Protein ASI2
- Probable ERAD-associated E3 ubiquitin-protein ligase ASI1
- Vacuolar amino acid transporter 5
Sequence:
MSSVNQIYDLFPNKHNIQFTDSHSQEHDTSSSLAKNDTDGTISIPGSIDTGILKSIIEEQGWNDAELYRSSIQNQRFFLTDKYTKKKHLTMEDMLSPEEEQIYQEPIQDFQTYNKRVQREYELRERMEEFFRQNTKNDLHILNEDSLNQQYSPLGPADYVLPLDRYSRMKHIASNFFRKKLGIPRKLKRRSHYNPNAEGHTKGNSSILSSTTDVIDNASYRNIAIDENVDITHKEHAIDEINEQGASGSESVVEGGSLLHDIEKVFNRSRATRKYHIQRKLKVRHIQMLSIGACFSVGLFLTSGKAFSIAGPFGTLLGFGLTGSIILATMLSFTELSTLIPVSSGFSGLASRFVEDAFGFALGWTYWISCMLALPAQVSSSTFYLSYYNNVNISKGVTAGFITLFSAFSIVVNLLDVSIMGEIVYVAGISKVIIAILMVFTMIILNAGHGNDIHEGVGFRYWDSSKSVRNLTYGLYRPTFDLADAGEGSKKGISGPKGRFLATASVMLISTFAFSGVEMTFLASGEAINPRKTIPSATKRTFSIVLISYVFLIFSVGINIYSGDPRLLSYFPGISEKRYEAIIKGTGMDWRLRTNCRGGIDYRQISVGTGYSSPWVVALQNFGLCTFASAFNAILIFFTATAGISSLFSCSRTLYAMSVQRKAPPVFEICSKRGVPYVSVIFSSLFSVIAYIAVDQTAIENFDVLANVSSASTSIIWMGLNLSFLRFYYALKQRKDIISRNDSSYPYKSPFQPYLAIYGLVGCSLFVIFMGYPNFIHHFWSTKAFFSAYGGLMFFFISYTAYKVLGTSKIQRLDQLDMDSGRREMDRTDWTEHSQYLGTYRERAKKLVTWLI
Protein: Intracellular coagulation inhibitor 2 (Limulus intracellular coagulation inhibitor 2) (LICI-2) (Q27086)
Organism: Tachypleus tridentatus (Japanese horseshoe crab)
Function: Serine protease inhibitor that inhibits proclotting enzyme and to a lesser extent clotting factor C and clotting factor G.
Subcellular location: Secreted {ECO:0000269|PubMed:7822280}. Note=Localizes in the large granules of hemocytes (PubMed:7822280). Secreted in hemolymph in response to external stimuli (PubMed:7822280). {ECO:0000269|PubMed:7822280}.
Interaction partners:
Sequence:
MLSRRTLDCCLVMLIVSTTFCQELHFYKEKADRSHENLKTAVNQFGIHLCRRLLNEGKNIIFSPFSLSTALSMAFVGARGNTAIEMRSGLGFREAGLAQEDVPDSFYQAFQLLKSDQSGDKFYVANTALVQNNYNILNSYKRILHRKFYSDIQPVDFVRNGLWVKEMVNKWVSNITHNKITSLIDKPLSPLTRLFLLNAVYFKGSWKTQFDRKRTTLSLFYNNNKVARRVEMMSLTNKFPYTYDSELKCQVLELPYDGDKTSMIFILPEWDVRLKHVENALSAQSVKQLINNLQDTEIVVTIPKFKLENSPQIKEYLQVMGMNEAFSFSADFSGMNGRRNLFVKDVLHKAMIDVNEEGSEAAAVSGVVVMLKSASHNLPTFVANHPFMFLIINKESGMILFLGSVREL
Protein: Nicotinic acetylcholine receptor Dalpha6 subunit variant type II (Q8T7S2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MDSPLPASLSLFVLLIFLAIIKESCQGPHEKRLLNHLLSTYNTLERPVANESEPLEVKFGLTLQQIIDVDEKNQLLITNLWLSLEWNDYNLRWNETEYGGVKDLRITPNKLWKPDVLMYNSADEGFDGTYHTNIVVKHGGSCLYVPPGIFKSTCKMDITWFPFDDQHCEMKFGSWTYDGNQLDLVLNSEDGGDLSDFITNGEWYLLAMPGKKNTIVYACCPEPYVDITFTIQIRRRTLYYFFNLIVPCVLISSMALLGFTLPPDSGEKLTLGVTILLSLTVFLNLVAESMPTTSDAVPLIGTYFNCIMFMVASSVVLTVVVLNYHHRTADIHEMPPWIKSVFLQWLPWILRMGRPGRKITRKTILLSNRMKELELKERSSKSLLANVLDIDDDFRHTISGSQTAIGSSASFGRPTTVEEHHTAIGCNHKDLHLILKELQFITARMRKADDEAELIGDWKFAAMVVDRFCLIVFTLFTIIATVTVLLSAPHIIVQ
Protein: Rifin (Q8IBE4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKDHYINILLFALPLNILVYNQRNYYITPRHTETNRSLCECELYSPTNYDSDPEMKRVMQQFVDRTTQRFHEYDERMKTTRQKCKDKCHKEIEKIILKDKMEKQMAQQLTTLETKIGTDDIPTCVCEKSMADKMEKDCLRCTYGLGTLAPTVGLIGSVAVGAWKPTALKAAIVAAQKAGDAAGVAAGEAAGKKAVILALQHFKLDNLFPEIYNAIVKIRHYADVKNFSVAIVEEHSLKCQSLDLKVTTNPTCETFEFNIGMRIPDSSFVEPVDQVVPEVLDSLVGNIKEVAEAKAAEVAAAKTAEFKIANVGAVESTYGSCQTAIIASIVAIVVIVLIMVIIYLILRYRRKKKMKKKLQYIKLLKE