wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Maf (Proto-oncogene c-Maf) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog) (P54843)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters (By similarity). Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf-responsive element binding.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear factor erythroid 2-related factor 2
- Protein c-Fos
- Transcription factor Jun
- Transcription regulator protein BACH2
- Transcription factor NF-E2 45 kDa subunit
- Endonuclease 8-like 1 lyase Neil1)
- Paired box protein Pax-6
- Cyclic AMP-responsive element-binding protein 1
- Endoplasmic reticulum membrane sensor NFE2L1
- Runt-related transcription factor 2
Sequence:
MASELAMNNSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPGSGSEQKAHLEDYYWMTGYPQQLNPEALGFSPEDAVEALISNSHQLQGGFDGYARGAQQLAAAAGAGAGASLGGSGEEMGPAAAVVSAVIAAAAAQSGAAPHYHHHHHHAAGHHHHPTAGAPGAAGGASASASGAGGAGGGGPASAGGGGGGGGGGGTAGAGGALHPHHAAGGLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVSNGFRENGSSSDNPSSPEFFM
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (Optic atrophy protein 1 homolog) [Cleaved into: Dynamin-like GTPase OPA1, long form (L-OPA1); Dynamin-like GTPase OPA1, short form (S-OPA1)] (Q5U3A7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Binds lipid membranes enriched in negatively charged phospholipids, such as cardiolipin, and promotes membrane tubulation. The intrinsic GTPase activity is low, and is strongly increased by interaction with lipid membranes (By similarity). Plays a role in remodeling cristae and the release of cytochrome c during apoptosis (By similarity).
Subcellular location: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O60313}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000250|UniProtKB:O60313}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, short form]: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O60313}.
Interaction partners:
- Mitofusin 1b
- Mitofusin 1
- Mitofusin 2
- Metalloendopeptidase OMA1, mitochondrial
- PTEN-induced kinase 1.
- Mitochondrial fission 1 protein
- E3 ubiquitin-protein ligase parkin
Sequence:
MLRAGSVVTCIACKGLLPSRMGVKFRVPLQKLHPLSRAIHHRYSANNNPQRPPHCSAARHYTSLSRLPMRPPKSRSGGHGYQQHRTFWVARLAARLLKLRYILLGSAVGGGYTAKKTYDEWKEMLPDMSEYTWIVPDFVWELSENIDLDKLASALPELEEIAKLLPDMEKIGENFTFLKSLLSSETTGESALRAPDVPPASAAMADSGDKQFKKSSDKEKVDQLQEELLRTQLKYQRMLERLEKENKELRKVVLQKDDKGIHQRKVKKSLIDMYSEVLDILSDYDSNYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVAMFKDSSREFDLGKEEDLAALRHEIELRMRKSVKEGQTVSPETISLSVKGPGIQRMVLVDLPGVISTVTTGMAADTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPQGKRTIFVLTKVDLAEKNLASPSRIQQIVEGKLFPMKALGYFAVVTGKGSPNESIDSIKDYEEDFFQNSRLLKDGMLKAHQVTTKNLSLAVSDCFWKMVRESVEQQADAFKASRFNLETEWKNNYPRLRELDRNELYEKAKNEILDEVISLSQVTPKHWESILQKKLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPHKALEVAWETLQEEFARFMAEYKGKDQDDIFDKLKEAVKDESIKRHKWNERAMDSLRVIQHNALEDRSITDKPQWDAAIQFMEETLQSRLKDTESVIADMVGPDWKQRWMSWKNRTPEQHTRNETKNELERLLKLHEDHTAYLANDEVTTVRKNLEARGVEVDPVLIKDTWHQLFRRHFLQKALLHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLGITANTLRQQLTNTEVRRLEKNVKEVLEDFGEDNEKKVQLITGRRVQLAEDLKKVREIQEKLEAFIEALHKEK
Protein: Glutamate receptor interacting protein, isoform B (Glutamate receptor interacting protein, isoform C) (X2JIJ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKLWKSKKPIGGCVPGKSAALKQDQQQQQQQQQESHNNSFNGHHHPPTDTALAPMLSVDRAMSPAQSEDSGLAPERGTTYATITLPRNALHLAITFAERNDLSYPPVVGSLNPVGHAADFLAPGDRLHQIDGISTIGLSNQKVMNMLCAGGSDACPAIVEIEYSLPECISQNSLCVTSKLAQITVERESGCLGLTLRGGADYPLIVTHVRPHGPVYKTGRIKPGDRLLRVDNVSLIGKTLAEAQQIIKCGGHVSGYTNLTIEYDVSVVQSVEFSMGPLLIEIERPMNDKLGLVLCNYTAAVPASGSGSSTPSSGEKIEESAGVFIASILPASIADRCGALSVGDQVLSIDDTMIEHTAFSPDEVMTILDTSTGRGYTQMQIMPAHALARRGHTTLGSPKYSFSTLESRKSSTAGRQRQRFARKSSLPLENPACGTPGSTGGSMGTGGIHGSSSLGMGLGLCRAESFPVLLDCSHGAGIILSETVSGSGGSGAVAIAQIVPDSVADRSGCIQAGDRIVAINKMYSLDAAAMRQLLEGGSSRNGASNGTPANWLELEIEFDMPDAVVPASGVFSVKLLRAGKCGLGLSVSGSSHGGLVISDVKMGSPAHRSGSLRSGDILLAVDQHPVQHFNVDALLKEEGRSQNPSHSSSDFTTLTIKRIVLPDFLPMSSPIYSNCPASGINLGMGMGVSTSTDHDLYSSAYVTAGKYADCVSLKSRTPQPDYFRVPSMDDASLQSVQLRSGSGSNGGNQAANSWSTGVNSRSYVAPPNTQSLTTELPEEEDEQEQMYPGYELNRYASVDCTALPPPMENKVYGSAASSSSKSSGSSLHQIIFTVRLEPKGGLLGITLAGSEDITKSITISGLVEGGIAHKNGQIHVGDQLLAIDEHSVQGMPLSHATSLLQNLGDLVDLKILRSHDLANGSHLPQTQAIYAKVQRRPRSPSANTEASKESGSGNANGGGAVNGNSGSGKPRVFHVTLYKDKVYDDYGFSVSDGLYERGVFINRIRSGGPADMCGLLKPFDRIMQVNEMKTQDFDCCLTVPLIAAAGDKIEMIMQRSE
Protein: Kinesin-like protein (A0A8I6AP89)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
LPPGINKSEKPESCDNVKVVVRCRPLNEREKSMCYRQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAVPGLRGVIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGVDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEVSGSDISGSEEDDNEEGELGEDGEKRKKRRGKKKVSPDKMMEMQAKIDEERKALETKLDMEEEERNKARAELERREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRKELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPQDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKERDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRR
Protein: Reticulon-like protein (A0A1D8PM53)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}.
Interaction partners:
- Meiotic sister chromatid recombination protein 1
- GTP cyclohydrolase 1
- Vta1p
- Protein YOP1
Sequence:
MSTSIPTESPLTTNNTTTTTAADISTTSGTTATPAQASVPTSTSSIADTHHSSCSTTDFLTWKNPIKTGKVFGSLVFGLIVLKTVNLFNIFFHLAYIGLLISAAAEYSGKLITGKGFLANFKPTGKLYAKRFNDEVLPELANFNVHLEESFNKIVYSHDIETTLKAAGISYILYKLTSWFSLYTLIFIFVVLIFTVPVIYKTYKKEIDAAVADITKTIKTKSAEFTEKAHKAAGPHIDTLIKKTGPIGSFIQSKLPVRTAGSTVGDSKATSYGTDADKSIAGTTSATGTSSATANSTTVPVSVPAATSATSAEPISTGHSTGASQFPSAPTSGLHPSTVEDVIKQASEEADEFADTTQESFKPTLH
Protein: Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) (CROC-1) (Q9CZY3)
Organism: Mus musculus (Mouse)
Function: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation (By similarity). Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity). Together with RNF135 and UBE2N, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway.
Subcellular location: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. {ECO:0000250}.
Interaction partners:
Sequence:
MAATTGSGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIECGPKYPEAPPSVRFVTRVNMSGVSSSNGVVDPRATAVLAKWQNSHSIKVILQELRRLMMSKENMKLPQPPEGQCYSN
Protein: BHLH domain-containing protein (Q2U112)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- SSD domain-containing protein
- Importin-95
Sequence:
MAYTRTDPSFTLSDDERMYMSHHSPMHRPYDTFAAPKGPDPLSANWNYDSAIDLFSLNTMMPENFALDVPNEPMGVDPKDFPADFFAPPPDISGFTISNHSGEDAGSITSDLESDDQSWSPTYAAPAEMLPAPGRQSTRRKTTPAVKRETTWSSSPELAPQEYPAHTSPQTTPTSPPVNRKMTRTTSVDSNASTGQTTTATTTSGRNAAKRAAHNIIEKRYRTNMNAKFVALEKAMCGGVQKSNKSGSASLKKSEILTNAIAYMQELQEENKALQKELALFKQNMVPSGMWRHTKGAETFRA
Protein: Histone acetyltransferase subunit NuA4-domain protein (Q93VF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SWR1-complex protein 4
- Histone acetyltransferase of the MYST family 2
- Enhancer of polycomb-like protein
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Enhancer of polycomb-like protein
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Histone acetyltransferase of the MYST family 1
- Protein MRG1
- Protein MRG2
- PHD finger protein ING1
Sequence:
MSLGQKSSTDPGAMLTSLLNKREKLRQELRSIEKQVYELETSYLQESSHIGNALKGFEGFLSSSKSTASAKRSRKFQPEDRVFSLSSVTSPAAEELGVGREDGRAELGPGRSKGGLSTQGKPKKGRGQSIIAREAKRSRPSTEPDYEDEDDPDMNMYGHGSLI
Protein: Phosphatidylinositol 4-kinase PIK1a (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (Q9UW24)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Rab family GTPase
- Calcium-binding protein NCS-1
- Oxysterol-binding protein-like protein OBPa
- 1-phosphatidylinositol-4-phosphate 5-kinase
- Phosphatidylinositol-3-phosphatase
- Phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol-3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphoinositide phospholipase C
Sequence:
MPVAPHELRDTIKSRDLGLFQCIDLLKQHNDNIGVHHQLVQKLYSYSYDELEFFIPQFIQLLVNFETDSMALEDFLLHYCNQFPHFSLIVFWYLQAFLFELRNEPKSYSFQTVRKFINKLQNILFNVETSFHIRGPEFRENMQPALILCGSVASAFSSPLVNEYALPIVRSQGKQQKSFVFKLASFQKSLTRNLTMKNQRLSADAITPVISDDDSKVSNRIQESQRLKTKYSKKKISAALQLDDSENYTTDEEELGYVQTLSRPKIREMKYTEVEENLKINTIIRSKKNRSKTTVNSISFFSDTDQSASMEEYNRSAQSLPELVRTRSRLDLYSSESEAALGTSRNSAELIISKKKFMGSEVKTRPYKELLKILQVNYSKKETSFIMSLQNISLRLSSVPKVARLSALRAELSIINESILPSEIDIPQLLPVTSNKNKKFHKILKLNINEACVLNSAERVPYLLLIEYLSDEIDFNPFSDQNQKIINDCVRKPEVKPNDQISGDDDTSVVSSIQEEMFLDNNASENYNEDGDLGEISLLHSRSSSRDWAKSTPGSPVARSSQEDEKFYGNVSSTTGGTIESSVLADQMRIASLMLQQLESSGQSNTQQFVSIRNRIIESMISLQDQFDFIDYETLKELKTDEQDAGKRKLENDFKLAEDWNEKKHRIRKSSIYGHLENWDLCSVIVKNGDDLPQEAFACQLISLISNIWKKHKVDFWTKRMKILITSANAGLVETITNAMSIHSIKKSLTELSIENGENAKGRIFTLKDYFQKLYGSVDSSKYVKAQENFAISLASYSIICYVLQIKDRHNGNIMLDHEGHIIHIDFGFLLSNSPGSVGFEAAPFKLTSEYVEVLGGLESKAYLKFVDTCKNCFKALRKEWGQIVSIVELMQKGSSLPCFNNGDNTSVLLQQRLQLHLSDEEIDSFIEVYLIEKSVGSMYTRLYDQFQMITQGIYS
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A8I5ZT43)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RRITLRVSVQGLYSLFQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDSSKQIHRIHRDSGDNSQTEPHSFRHKSRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHHSHSHLSMPITINDVPPSIAQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCTETTLRAWLQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPLAAESEGSDCECNPTGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSNS
Protein: Calmodulin-3 (P0DP31)
Organism: Rattus norvegicus (Rat)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}.
Interaction partners:
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Glycine-rich protein 3 (AtGRP-3) (Q9SL15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the function of the receptor protein kinase WAK1, and namely the phosphorylation of OEE2.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Wall-associated receptor kinase 1
- Protein phosphatase 2C 70
- Glycine-rich protein 5
- Wall-associated receptor kinase-like 17
- Glycine-rich protein 23
- Putative oxygen-evolving enhancer protein 2-2
Sequence:
MASKALVLLGLFAVLLVVSEVAAASSATVNSESKETVKPDQRGYGDNGGNYNNGGGYQGGGGNYQGGGGNYQGGGGNYQGGGGRYQGGGGRYQGGGGRYQGGGGRQGGGGSGGSYCRHGCCYRGYNGCSRCCSYAGEAVQTQPGH
Protein: Myosin-11 (Myosin XI E) (AtXIE) (F4HWY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks, mitochondria and peroxisomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18503043}. Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or organelles.
Interaction partners:
- Ras-related protein RABA4d
- Glutamate receptor 2.2
- Protein NRT1/ PTR FAMILY 5.6
Sequence:
MRNSGTPVNIIVGSHVWIEDSDVAWIDGLVEKINGQDVEVQATNGKKITAKLSKIYPKDMEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPFGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPQEELEKYKLGHPKTFHYLNQSKCFELVGISDAHDYIATRRAMDIVGMSEKEQEAIFRVVAAILHLGNVEFTKGKEVDSSVPKDDKSKFHLNTVAELLMCDVKALEDALCKRVMVTPEEVIKRSLDPQSALISRDGLAKTIYSRLFDWLVEKINVSIGQDATSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVQYQSDLFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNSTEPHYIRCVKPNNLLKPAVFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLYPRALEGNYEEKAAAQKILDNIGLKGYQVGKTKVFLRAGQMAELDARRTMVLSAAAKKIQRRIRTHQAQRRFILLRKATISLQALCRGRLSSKIFDNLRRQAAAVKIQKNARRLHSRKSYKNLHVAALVVQTGLRAMAAHKQFRFRKQTKAATTIQAQFRCHRATLYFKKLKKGVILSQTRWRGKLARRELRQLKMASRETGALKEAKDMLEKKVEELTYRAQLEKRSRVDLEEEKNQEIKKLQSSLEEMRKKVDETNGLLVKEREAAKKAIEEAPPVVTETQVLVEDTQKIEALTEEVEGLKANLEQEKQRADDATRKFDEAQESSEDRKKKLEDTEKKAQQLQESVTRLEEKCNNLESENKVLRQQAVSIAPNKFLSGRSRSILQRGSESGHLSVDARPSLDLHSHSINRRDLSEVDDKPQKSLNEKQQENQELLIRCIVQHLGFQGKRPVTACIIYKCLLQWRSFEVERTSVFDRIIQTIGQAIETQDNNNILAYWLSNASTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMTQSFRGTPQGVNLAMINGGVDTLRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNNLKSNHVPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEHWCYNATDEYAGSSWDELKHIRQAIGFLVIHQKPKKTLDEISHELCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMERIEIGDVEPPPLIRENSGFSFLLPCSD
Protein: Arf-GAP domain-containing protein (Q19467)
Organism: Caenorhabditis elegans
Interaction partners:
- SH3 domain-containing protein
- Liprin-alpha
- Paxillin homolog 1
- Serine/threonine-protein kinase pak-1
- Serine/threonine-protein kinase max-2
- G protein-coupled receptor kinase 1
- ELKS/RAB6-interacting/CAST family member 2
- Ras-related protein rac-2
- G protein-coupled receptor kinase 2
- Cell division control protein 42 homolog
Sequence:
MYTAEALDLITSLEQKECDDCGKKEVEWASVKKGTVICSECFCFHSYLGPSVSYLRHLRKSAWDEEHIRLVHALNTSNTNMIWESALYEGSTKFQKPMAQDPSHIKEQFVKEKYEKLTFQPKRGKDEDLENSLNRQLIACARSDFAHVTLRLIALGADVNYPDPETGDTALHVAAREGNSNQVELLFLYGADIMAPNREGMLPYILARDAGHGQLSHRIYEFFFYVFDRFSFFMCNRKADHKNNQDFFIPEVTEKQFLTKTNDSRAAISVLPKGQFFDLCEDAFDETVRRENEVNWNMTKWAKTAKGPTNLFLPPTPQMSAARNQRRQKLAKFTPIQFTILLIDLIKDQKRRITGDNPAPVSEPPKNMRKSNDTPLRIMKKSEYADYDEVAGISCSPISGIVPNSQANTLDESSSRVWDELLEMKERLSSTETMVVTLTKQNEELTKLVHSLQAQNINLNSELITFRDDLYNLKRTNMTRRMPSPLAIVETPERVMPPVGIQQGFSRRDSEDRIDGGGARWRSNSSDRRNSNDHKLDKKVERRQDSMMESSSSLSRSSQNPSCLNREEVKTRVIQQSEKITRHIKTLLQHGHNGNLDMNARGGAHDIACAINSLITILLPYVRHEKIDTLTDAVVLLNAKCNSPVLMPMDIVDAAQTIAEKLRLIIMEFC
Protein: Vacuolar import and degradation protein 22 (Q05934)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A.
Subcellular location: Cell membrane; Single-pass membrane protein. Nucleus.
Interaction partners:
- Protein TBF1
- ATP-dependent helicase SGS1
Sequence:
MRAMDTQVQSAERGLVLPPMNSTVSSATAATTATNTDTDTDGDRDEERESLAEDGSEWVPAYMLTRDRSRYLGHFLGVDKMLEAVKCKYCGVIIRRQGNSISMAEASQTHLWSTHKIDPNANYYSGWTGVEAGSTFMVRPPLKNHQGGSATTNSIANLLEIDEDFLKRTREKEMALPLVQSLAIIIASENLPLSFVDNTAVRLLINQNANSLSFIDHDLILNAIRSIAYNLDRIIQRTALRNNSDLSLIIDKNYLLMDPTDRSNQLSNRLKNQLFEMQKINFFSLSHSVWNNTISILSIQYYDDFHSQVKTLPLIIQNLHEYNNDPKLSIPAQLLKISQELPGLQNTVISITLPRSQIVDLLNVMDSQPFFPNTYTNAKNYYHNCIISIINSAILPLFGTPKSADITHPRQSSFSKEPLTLLDSLIDLSNIDISNSIFSRINSFLDDLQSNSWQLDKFRSLCEKFGFEFVCSKFDLSRYSTATVSLQTFLNLRPIIEEYQSSIQIEKFNEIDFQIIDYLLITLNSINRILKFFTSSKSLNFTYVLFAIMSIEKHLLSTLGSLQFQRLIAPFETFLSKIQEFKTILFSDDMNLLAMFLCPAILFEREVLEYSFHTISLSEIVDKLSTSIFSLLKRFLNLHTIGNVNNSHNTSNHSNMNIHTDNQTNNINNRSGNNSDNNDNEHDNDNDNHSNSNTPASRIDIDPTGGENSVLPEQQPQNSNNNLSFGSLSDTHHLSDSTISKEIDSIFLQIIQEDLYDYLSTVNSIVPISYRSYCEQSNFIRDSGRFKKRIITEDSIIGELEQPMNFIEELLDIHVPVCNAFWSQYLDNDAGPIIRILFKIMQCQSSSSIRGEYSFLNDFIPRVHPDLTQEIIKIKLFNDQFVASKVDYDLDTLQTASQYLP
Protein: LD43460p (Q8MSU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRDGNTGVALYTRKVLIQSKTEHLLPKWLRFVKGVVDSEDIPLNLSRELLQNSSLIRKLSSVISTRVIRFLQERSKKQPEEYEAFYRDYGLFLKEGIVTSSDASEKEEIAKLLRFESSKSETASGRMSLEEYYNAVPAEQQNIYYLAAPNRVLAESSPYYESLKKRNELVLFCYEPYDELVLMQLGKFKSKKLVSVEKEMREESKETTATTDFGEGSLLRSELDTLIPWLEEELRGQVIKVKATTRLDTHPCVITVEEMAAARHFIRTQSHQVPEQNRFALLQPELEINPKHPIIKKLNKLRESDKDLAQLIAKQLFANAMVGAGLAEDPRMLLTNMNTLLSRALEKY
Protein: Adenylyl-sulfate kinase (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenosine-5'-phosphosulfate kinase) (APS kinase) (Q02196)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the synthesis of activated sulfate.
Interaction partners:
- Sulfite reductase subunit beta
- Sulfate adenylyltransferase
- Phosphoadenosine phosphosulfate reductase
- F-box protein SKP2
- 3'
- Sulfite reductase flavoprotein component
- Elongation factor Tu, mitochondrial
- Uncharacterized protein YMR178W
- Flavin adenine dinucleotide synthase
- Uroporphyrinogen-III C-methyltransferase
Sequence:
MATNITWHPNLTYDERKALRKQDGCTIWLTGLSASGKSTIACALEQLLLQKNLSAYRLDGDNIRFGLNKDLGFSEKDRNENIRRISEVSKLFADSCAISITSFISPYRVDRDRARELHKEAGLKFIEIFVDVPLEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPKAPELHLRTDQKTVEECATIIYEYLISEKIIRKHL
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q9DGL5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGKGYGHESSPEAAPTGGKRKKKDKDLDELKKEVSLDDHKLTLDELSTRYGVDLARGLTHKRAMEILARDGPNALTPPPTTPEWVKFCKQLFGGFSILLWIGAILCFLAYSIQAATEDEPVNDNLYLGVVLSAVVIITGCFSYYQEAKSSRIMDSFKNMVPQQALVIRDGEKLQINAEEVVQGDLVEIKGGDRVPADLRIISSSGCKVDNSSLTGESEPQTRSPEFTHENPLETRNISFFSTNCVEGTAHGIVIATGDHTVMGRIATLASGLEVGQTPINMEIEHFIHIITGVAIFLGMSFFILSIILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGCDFDKSSPTWFSLSRVGGLCNRAVFKAGQEEIPIRTRDTAGDASESALLKCVEILSGNVETLRGNNRKVAEIPFNSTNKYQLSIHELEDSPTGHLLVMKGAPERILDRCSTIMINGVEFPIDDDWMDAFQGAYMELGGLGERVLGFCHLFLSPSQFPRGFEFDCDDVNFPVNQLCFLGLISMVDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAERLNIPLSQVNPREAKACVVHGSDLKDMSSEYLDDILRNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGITGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIASVPLPLGTVTILCIDLGTDMVPAISLAYESAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVIMAENGFLPQTLLGIRLDWDDRTVNDLEDGYGQQWTYEQRKIIEFTCHTSFFVSIVVVQWADLIICKTRRNSVFQQGMKNRILIFGLFAETALAAFLSYCPGMDVALRMYPLKIMWWFCAFPYSLLIFVYDEIRKFILRRNPGGWVEIETYY
Protein: GM06145p (Signal peptide peptidase-like, isoform D (EC 3.4.23.-)) (Signal peptide peptidase-like, isoform E) (Q86P97)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Protein FAM98B
Sequence:
MSHGGAGGGLGAQTVGAGQLGGGAAAAGGGEYRELHWTVSSVMDSSRVSTCLISMLLIVYGSFRSLNIEQEAREREQKKRNESMTNLLTGEPVEKEPNLYFTADKFATLDTMHALCLPLGASISLLIMFFFFDSMQLLFAVCTAIIATVALAFLLLPMCQYIIRPCTDGKRFSFGFCGRFTAAELFSFTLSVSIVCIWVLTGHWLLMDAMGMGLCVAFIAFVRLPSLKVSTLLLTGLLIYDVFWVFLSSYIFSTNVMVKVATRPADNPVGIVARKLHLGGIVRDTPKLNLPGKLVFPSLHNTGHFSMLGLGDVVMPGLLLCFVLRYDAYKKAQGVTSDPTLSPPRGVGSRLTYFHCSLLGYFLGLLTATVSSEVFKAAQPALLYLVPFTLLPLLLMAYLKGDLRRMWSEPFIAQQPSKQLEV
Protein: Stationary phase protein 3 (Q04398)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for survival during stationary phase.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MICYFLVVTINFLKEKTTICHYFVNIFSLFLFLFVFVFVFIFVYFFYVILFYRFCSLFTYFPANSIWYYLSIINIFFPLCFFLYENFTGRNRRKCSLFCLTLIKITYTSPNHGFMVTGKEKFEKLRD