wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium-binding protein C (Calcium-binding protein 3) (Q54QT7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a role during cell aggregation and slug migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15843041}.
Interaction partners:
- Cyclin-C
Sequence:
MLTNNEIYQEVQKFAKGYDLNQDGVLTSQEIYYSLLKKMNGNSYEASKATGVLCSTIDINKDGKFSYHEIAKYCADNAKKLIEQNADIAALADVEAFLLRFDKDKDRKLNKTEFVEYFKGGTDTPYSDRDYVLKIIDLDKDGCVSANELQEWFKKKRIDYASRPHC
Protein: Acetyl-CoA decarbonylase/synthase complex subunit gamma 2 (ACDS complex subunit gamma 2) (EC 2.1.1.245) (5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 2) (ACDS complex methyltransferase 2) (Corrinoid/iron-sulfur component large subunit 2) (Q9C4Z0)
Organism: Methanosarcina thermophila
Function: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.
Interaction partners:
Sequence:
MKINSPLEAYKYLPQTNCGECGEATCMAFASKLIDRSGKPTQCPPLVKEKKFAKKLAELERLLAPEIREITIGVGDRAVKIGGDDVLYRHKLTFFNKTKMFYDVTDTMDEAALLERTKKVADFRKFYVGRNLLLDGVAIRSVSNDPEKFAAAVKKVSEVGIPMILCSFNPAVLKAGLEVAKDKNPLIYAANKDNWKEVGELALEYNVPVVVSAFNDLDGLKTLAKTFAEAGIKDIVLDPGTYPSGQGLKDSFTNFLKIRRAGIMGDTEIAYPIMALPITAWMAGISDPVSAAYWETAMAAIFTIRYGDIMILHSLEPYATLPEVHLAETIYTDPRTPVAVDSKMYKVGEPDENSPVLFTTNFALTYYTVESDLSSNGITCWLLAVDTDGIGVEAAAAGGQLTADKVKDAFEKSGFDLKKDVTHNTVIIPGLAARLQGDLEDKLGARVLVGPMDSGRLPGWFEKNWPPK
Protein: Polycystin-2 (D4A5F1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004272}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
- Polycystin-1
- Short transient receptor potential channel 1
- Transient receptor potential cation channel subfamily V member 4
- Uncharacterized protein.
- Adenylate cyclase type 5
- Exocyst complex component 5
- Intraflagellar transport 88
- Glucosidase 2 subunit beta
- Polycystin-1-like protein 3
- Fibrocystin
Sequence:
MVNSSRVQPQPPGDPGRSPAPRASGPGRLLAGGAGLAVPGGLREQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRPASSSAVSSAGARGRGLGSYRGAAYPSGRRRRLEDQGAPCPSPAGGGDPLHRHLPLDGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLRSVLRELVTYLFFLILLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQSSNHTQADNRSFIFYENLLLGVPRLRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQLAGLRRNFWLDRGTRAAFIDFSVYNANINLFCVVRLLVEFPATGGVVPSWQFQPVKLIRYVTAFDFFLAACEIIFCFFILYYVVEEILEIRIHRLNYFRSFWNCLDVVIVVLSVVAMMINIYRMSNAEGLLQFLEDQNSFPNFEHVAYWQIQFNNIAAVMVFLVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFTIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPLYFTTFVFFMFFILLNMFLAIINDSYSEVKSDLAQQKAEMELSDLIRKGCQKALVKLKLKRNTVDAISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEREHQQMRDDLEREREDLDLEHSSLPRPMSSRSFPRSLDDSEEEDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKVKRREVLGRLLDGVAEDARLGRDSEIHREQMERLVREELERWESDDAASQSGHGLGTQVGLGGQSHPRSSRPPSSQSAEGLEGGGGNGSTNAHA
Protein: Translin (Component 3 of promoter of RISC) (A0A8J8YNL9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ARSSWSCRAFWLPSRTSEEIRKVVQSLEQTAREILTLLQGVHQGTGFQDIPKRCLKAREHFGTVKTHLTSLKTKFPAEQYYRFHEHWRFVLQRLVFLAAFVVYLETETLVTREAVTEILGIEPDREKGFHLDVEDYLSGVLILASELSRLSVNSVTAGDYSRPLHISTFINELDSGFRLLNLKNDSLRKRYDGLKYDVKKVEEVVYDLSIRGFNKETAAACGEK
Protein: Spore wall protein 5 (G0Z414)
Organism: Nosema bombycis (Microsporidian parasite) (Pebrine of silkworm)
Interaction partners:
Sequence:
MNFILTSVTCILYYILFAQAAAKENKNVPGSAIVNSGSQNEVTATVNAEAQKDTDSFEIKPLKTPVDKDKPVQTLDDLKEEASEEKLVPISILAVFADPKEVMNTPSPVLIAAEQYIQESGAAGKPQNVRLDKEDDESEKNDDKNKKDEDDKNKNGDDDKSKKNGESAPEEKKEPPSTSETAPSDK
Protein: Apelin receptor B (Angiotensin receptor-like 1b) (Angiotensin receptor-related protein B) (G-protein coupled receptor APJ-B) (APJb) (Q2TAD5)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively (By similarity). Promotes angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone. Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility, and heart failure. Acts upstream of the i/o type of G-alpha proteins in the differentiation of endothelium, erythroid cells, myeloid cells and cardiomyocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17412318}; Multi-pass membrane protein {ECO:0000269|PubMed:17412318}. Note=Internalized to the cytoplasm after exposure to apelin (apln) (PubMed:17412318). After exposure to apelin receptor early endogenous ligand (apela), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P35414, ECO:0000269|PubMed:17412318}.
Interaction partners:
Sequence:
MESEGFSATTEQYEYYDYANETGLQPCDETDWDFSYSLLPVFYMIVFVLGLSGNGVVIFTVWKAKPKRRSADTYIGNLALADLAFVVTLPLWATYTALGFHWPFGSALCKLSSYLVLLNMFASVFCLTCLSFDRYLAIVHSLSSAKLRSRSSILVSLAVIWLFSGLLALPSLILRDTRVEGNNTICDLDFSGVSSKENENFWIGGLSILTTVPGFLLPLLLMTIFYCFIGGKVTMHFQNLKKEEQKKKRLLKIIITLVVVFAICWLPFHILKTIHFLDLMGFLELSCSAQNIIVSLHPYATCLAYVNSCLNPFLYAFFDLRFRSQCFFFFGFKKVLQGHLSNTSSSLSAQTQKSEIHSLATKV
Protein: Glutathione S-transferase (EC 2.5.1.18) (GST class-pi) (P91505)
Organism: Caenorhabditis elegans
Interaction partners:
- Thioredoxin domain-containing protein
- Glutathione S-transferase P
- Glutathione peroxidase
- Glutathione peroxidase 3
- Epoxide hydrolase
- Glutathione peroxidase
- Glutathione peroxidase 2
- Glutathione peroxidase 1
- Probable glutathione S-transferase 6
- Glutathione S-transferase omega
Sequence:
MTLKLTYFDIRGLAEPIRLLLNDQEIPFEDNRISREEWAEMKSTMIFAQLPCLHIGTETIVQSAAILRHLGRIYGLNGSTESETSFIDMFSEGLRDLRTKYFTMIKTDYEDGKEAYITETLPGELLRIEKLFCTFNNGENFVSGDKLSYADYALFELLDIHLILTPTALNGTPALKRFHGRFAERPNMRLYLNKRAELNPFVSGNGKQ
Protein: Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (Q383G8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Phosphoacetylglucosamine mutase
- glutamine--fructose-6-phosphate transaminase
- Glucosamine-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- GDP-L-fucose synthase
- GDP-mannose 4,6-dehydratase
Sequence:
MTDIVDLELRVLEESDLSSHLELLGHLTEAPPLSGVELANIADMRRRAGIVTKVFCHQPTGGIVGSASLMIQPKFTRGGRAVGHIEDVVVDPSYRGAGLGKALIMDLCEISRSKGCYKVILDSSEKSLPFYEKLGFRAHERQMRLDL
Protein: Trophozoite exported protein 1 (Q6LFN2)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Host cell membrane {ECO:0000269|PubMed:17653272, ECO:0000269|PubMed:23056243}; Peripheral membrane protein {ECO:0000269|PubMed:23056243}; Cytoplasmic side {ECO:0000269|PubMed:23056243}. Note=In late rings, localizes to punctuated structures in the parasite cytoplasm (PubMed:23056243). In trophozoites, exported to the host erythrocyte cytoplasm where it localizes to Maurer's clefts (PubMed:23056243). In schizonts, localizes near to the host erythrocyte cell membrane (PubMed:23056243). {ECO:0000269|PubMed:23056243}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- Histone H2A
- CDC73 domain-containing protein, putative
- Probable ATP-dependent helicase PF08_0048
Sequence:
MSNKKRSKNENDESTSLPLENSELLIEYIHNLKSCLNVYRREIQEKNKYISIIKNDLSFHECILTNVNVVWSVFNNDLLNLLCNNEQKEEGEEIIKQRNIGDEINEYNNLTKLQNDENIKNNNMIKEDLEDDANQNILMKSPYYNIENFLQVFLKYINKKKKKVKVKVKDEGKKEKIEDKKYEQDDEEENEEEEEEEEEEEGEEENKEDEEFFKTFVSFNLYHNNNEKNISYDKNLVKQENDNKDEARGNDNMCGNYDIHNERGEMLDKGKSYSGDEKINTSDNAKSCSGDEKVITSDNGKSYDYVKNESEEQEEKENMLNNKKRSLECNPNEAKKICFSLEEKIGTVQSVKLKEYNELSKENIEKNKHDDNNICNYLSHNEGENVIEREDKLFNKLNNKNYRNEEEKKKNQINFDYLKKKIKNNQDVFEETIQKCFLINLKKTLNLINKIMYLKNVEFRKYNLDYIRKINYEKCFYYKNYIDIKKKISELQKDNESLKIQVDRLEKKKATLIYKLNNDNIRKHILDNNIKDYQNGIDNSKVSYFDEGENPYNRNNKNYRTDNKNSDDNNNNNNYYYNNYNSDDNYNSEDNEYNNGNYRFRNNYKKDSLNEDDVKKNPLKVCHKINSDSNIFVNFENIITKQNIIHSEPFRNLLKESNELYITLKEKEKENIILKNEILKMENKKDEEYEHLLNNTIEDKKELTRSIKELEINMMTCNMEKDKISNKVNTLEYEINVLKNIDKNQTMQLQQKENDILKMKLYIEKLKLSEKNLKDKIILLENEKDKMLSGIHIKDNSFNEESKSEEGKIQLRDIQNDNDEKYDDEKKRFKELFIENQKLKEELNKKRNVEEELHSLRKNYNIINEEIEEITKEFEKKQEQVDEMILQIKNKELELLDKFNNKMNKAYVEEKLKELKNTYEEKMKHINNIYKKHDDFVNIYLNLFFQARKNAILSDSQREEQMNLFIKLKDKYDIIFQKKIELTDILKNVYDCNKKLIGHCQDLEKENSTLQNKLSNEIKNSKMLSKNLSKNSDDHLLIEENNELRRRLICSVCMENFRNYIIIKCGHIYCNNCIFNNLKTRNRKCPQCKVPFDKKDLQKIFLD
Protein: B3 domain-containing protein REM9 (Auxin response factor 23) (Protein REPRODUCTIVE MERISTEM 9) (O81778)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- AUGMIN subunit 8
Sequence:
MANASPLSPTNQHFFQPLLPGFQSNLKIPVNYFSEHIEGKHEGKTVTLRTDASERTWEVKMEGHRLTEGWKEFVEAHDLRIGDFVVFRHEGDMVFHVTALGPSCCEIQYPQSSRHEEGEESGENEISEKEGEENVQKESDKSSSDLNCFSQSVTHSNISRDAVSVPRDFVKRSGFSKGRHEIVLMNEEGKSWESEVKSYMSGAVYLVGGWTTFCTENKLDVGDSCTFKLLQKAKTPVFQLCSRTKHLPLSFTKVNGLINPGKIILVDKDRAEWSMMLKVDSRGAVYIIGGNDWKSFCAANEVGAGESLALELIQGGVLLNQITTCFQMEQPSFKAEDGRHKRARVQNRSQETDKGAETSRASTMGPKLEITEKGEPSRASTMRPKVEIREKIAETGEPSRASNKSSGIEGNLQHTKPCSVKTDQLAKVKESVVDTLTSIGRFQAELETMKRKLEDSLQELN
Protein: mRNA stability protein IGO1 (Initiation of G zero protein 1) (P53897)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
Interaction partners:
- Serine/threonine-protein kinase RIM15
- Protein phosphatase PP2A regulatory subunit B
- mRNA stability protein IGO2
- ATP-dependent RNA helicase DHH1
- Transcriptional activator/repressor GIS1
- Cyclin-dependent kinase 1
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Protein ZDS1
Sequence:
MSNENLSPNSSNPDLTKLNNGESGTIDTSKFSPNEMKLYKMYGKLPSKKDIFKHTMQKRKYFDSGDYALQKAGIQNNDPINYGKNNLPLTNPSKLREDIIKRRISTCPSTASTAGVVDNATLIQKEGSISSGPPSSNNGTIGGGSTSSTPVGNHSSSSSSLYTESPIR
Protein: NAD-dependent dihydropyrimidine dehydrogenase subunit PreT (DPD) (EC 1.3.1.1) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (P76440)
Organism: Escherichia coli (strain K12)
Function: Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT).
Interaction partners:
- Glutamate synthase large chain
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- D-phenylhydantoinase
- NADH-quinone oxidoreductase subunit F
- Purine nucleoside phosphorylase DeoD-type
- Uridine phosphorylase
- Pseudouridine-5'-phosphate glycosidase
- 7-cyano-7-deazaguanine synthase
- Cytosine deaminase
- Thymidine phosphorylase
Sequence:
MPQQNYLDELTPAFTSLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSGCTRAGVDAPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVGLSSGSGLPLFEHSDVEIAVDFLQRARQAQGDISIPQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFTSARELGVSIIDGFTPVAVEGNKVTFKHVRLSGELTMAADKIILAVGQHARLDAFAELEPQRNTIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEGACSC
Protein: Histone-lysine N-methyltransferase EZH1 (EC 2.1.1.356) (ENX-2) (Enhancer of zeste homolog 1) (P70351)
Organism: Mus musculus (Mouse)
Function: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation.
Subcellular location: Nucleus {ECO:0000250}. Note=Colocalizes with trimethylated 'Lys-27' of histone H3. {ECO:0000250}.
Interaction partners:
- Zinc finger protein AEBP2
- Polycomb protein Suz12
- Histone-binding protein RBBP4
- Polycomb protein EED
- Protein Jumonji
- Histone-binding protein RBBP7
- E3 ubiquitin-protein ligase RING1
- Histone-lysine N-methyltransferase EZH2
- PHD finger protein 1
- E3 ubiquitin-protein ligase RING2
Sequence:
MDIASPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQPMKPVSGHPFLKKCTIESIFPGFDSQDMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEDGHNDPSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGRRRRRHPVVSASCSNASASAMAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPAQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPAQKKKRKHRLWAAHCRKIQLKKDNNSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCSPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVF
Protein: Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.17) (EC 2.1.1.71) (Overproducer of inositol protein 3) (Phospholipid methyltransferase) (PLMT) (P05375)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). Can also catalyze the first methylation reaction of PE to PMME in the absence of PE methyltransferase CHO2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
Interaction partners:
- Phosphatidylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 2
- Cholinephosphotransferase 1
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Choline/ethanolaminephosphotransferase 1
- Lysophospholipid acyltransferase
- Phospholipase D1
- Triacylglycerol lipase 4
- Triacylglycerol lipase 5
Sequence:
MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKGCYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFMYKIALRWEEPFTAMIYANRDKAKKNM
Protein: PMA1 stabilization in the Golgi protein 1 [Cleaved into: PSG1-N'; PSG1-C'] (P36081)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With EXP1, the specific cargo receptor protein for the plasma membrane ATPase PMA1, is involved in the transport and/or maturation of PMA1. EXP1 and PSG1 probably act sequentially to promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting PMA1 export from the ER to the Golgi while PSG1 has a role in PMA1 maturation or quality control in the Golgi. PSG1 might also couple PMA1 sorting and maturation in the early secretory pathway with the glycosylation machinery (Probable).
Subcellular location: [PSG1-N']: Golgi apparatus lumen {ECO:0000269|PubMed:28727280}.; SUBCELLULAR LOCATION: [PSG1-C']: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:28727280}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein YIL067C
- Protein UIP5
- ER-retained PMA1-suppressing protein 1
- Vacuolar membrane protein YOR292C
Sequence:
MRFHDSILIFFSLASLYQHVHGARQVVRPKEKMTTSEEVKPWLRTVYGSQKELVTPTVIAGVTFSEKPEETPNPLKPWVSLEHDGRPKTIKPEINKGRTKKGRPDYSTYFKTVSSHTYSYEELKAHNMGPNEVFVEEEYIDEDDTYVSLNPIVRCTPNLYFNKGLAKDIRSEPFCTPYENSRWKVDKTYFVTWYTRFFTDENSGKVADKVRVHLSYVKENPVEKGNYKRDIPATFFSSEWIDNDNGLMPVEVRDEWLQDQFDRRIVVSVQPIYISDEDFDPLQYGILLYITKGSKVFKPTKEQLALDDAGITNDQWYYVALSIPTVVVVFFVFMYFFLYVNGKNRDFTDVTRKALNKKRRVLGKFSEMKKFKNMKNHKYTELPSYKKTSKQN
Protein: FLX4 (A0A178USJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSRERIGSNHHSRVSQGMSTSGSSSSRHHDTISSTSDPRHLRDHQISLSDILENKIAVQAAEIDRLSNDNRKLASSYVALKEDLTVADREVQGLRAHIRKTETDHEIQIRSTLEKIAKMEGMVKNRENIRREVQSAHIEAHRLAREREELASKVKLGMKDLKKVCLEAESLEASSQELERLKEEHQRLRKEFEEEKSGNVEKLAQLKGMERKIIGAVKAIEKLRSEISTARNKAVEN
Protein: Photosystem II reaction center Psb28 protein (Photosystem II 13 kDa protein) (Photosystem II reaction center W protein) (Q55356)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Subcellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:12069591}; Peripheral membrane protein {ECO:0000305|PubMed:12069591}; Cytoplasmic side {ECO:0000305|PubMed:12069591}.
Interaction partners:
- Photosystem II lipoprotein Psb27
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein H
- Photosystem II extrinsic protein O
- Photosystem II reaction center protein I
- Photosystem II D2 protein
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein M
- Photosystem II reaction center protein L
- Photosystem II CP43 reaction center protein
Sequence:
MAEIQFSKGVAETVVPEVRLSKSKNGQSGMAKFYFLEPTILAKESTDDITGMYLIDDEGEIITREVKGKFINGRPTAIEATVILNSQPEWDRFMRFMERYGAENGLGFSKSE
Protein: Probable global transcription activator SNF2L1 (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily a, member 1) (A5WUY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Bromodomain PHD finger transcription factor
- Chromatin accessibility complex subunit 1.
- CECR2 histone acetyl-lysine reader
- DNA polymerase epsilon subunit 3
- Histone-binding protein RBBP4
- Bromodomain adjacent to zinc finger domain, 1A.
- Bromodomain adjacent to zinc finger domain, 1A.
- Histone-binding protein RBBP7
- Tyrosine-protein kinase BAZ1B
Sequence:
MSDEELPSTSREAHAEAEEEDPPFLLGPPPKAVVKESLADPEYEEKRKTDRANRFEFLLKQTELFAHFIQPASQKSPTSPLKVKMGRPRIKQDEKQNLLSVGDNRHRRTEQEEDEELLSESRKADNVLVRFEESPSYIKNGTLRDYQIRGLNWMISLYENGINGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPTLKAVCLIGNKDERAAFIRDVMMPGEWDVCVTSYEMVIREKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIAREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSASDFDSWFDTNCLGDQKLVERLHAVLRPFLLRRIKAEVEKSLPPKKEVKIYLGLSKMQREWYTRILMKDIDILNSAGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDTHLVINSGKMVALDKLLPKVQEQGSRVLIFSQMTRVLDILEDYCMWRGFEYCRLDGNTPHEAREQAIDAFNAPNSSKFIFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQRKPVKVFRLITDNTVEERIVERAEMKLRLDSIVIQQGRLIDQQNKLGKDEMLQMIRHGATHVFASKDSELTDEDIDTILERGAKKTAEMNERMQNLGESSLRNFTVDTGATETSLYNFEGEDYREKQKVGVFIFGHLIFVHIAVLKSINLSLIEWIEPPKRERKANYAVDAYFREALRVSEPRAPKAPRPPKQPNIQDFQFFPPRLFELLEMEILYYRKTIGYKVPRSPDIPNSAQVQKEEQRKIDEAEPLSPEETEEKEKLLTQGFTNWNKRDFNQFIKANEKYGRDDIDNIAREVEGKTPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDVKIARYKAPFHQLRIQYGTNKGKNYTEEEDRFLICMLHKMGFDKEYVYEELRQCVRNAPQFRFDWFIKSRTAMELQRRCNTLISLIEKENMEIEEKERAEKKRRTPKGQSAQKRKAEVSSEKKEKKART
Protein: M-spondin (O02029)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGATPKTDFPAHWLLCILLALGSLSSKANAVSAYGASFISNPSIYVYSVENQPDERESRDNNIKFAAEHGNLNSNSNLNRNYYYTDDPSPVPNMNPTASLATPPATQTAPQTGCTLDRLAVYKVVLHTYWTRELFPKHYPDWRPTAQWTKTLGRTHNANYALYHIGQPATAAVKQFAESGRTDLLDSNAGEQQQVQMQLQSQMQAGKSPSGGISSGTTSFNATAASTATPTGGSGGSGGSGVTGTTTAERSVFDEFSMPAIPMGAGRSEAQVFVDSNHSLVSLMTRIVPSPDWFIGVDSFELCVGGSWIDTVTVELDPLDAGTDNGFTFTAPNWPTAPQGVIYRITSRYPGHPAGSFYYPKSKRLPPIATFQFIKLKEYELSEVFNIAEDDRKYETVQTQTHLDAEHNHVEMNNELSASIERERQTEQQQLQQNDDERQRIRSQLLAKMNPIYGSNNSLQAAPGQVVSVVPKNDKHAILQSIASSYRRAADASDANASKPTPSAIGGGKAGGAVGGGAATRRRSSAQRRRDCRVSHWSEWTACSKSCGVGEMHRYRKVIKHGKRGGRQCPALQQSKWCGTERNCHGSQTYFNWSDSDT
Protein: FERM domain-containing protein (Talin) (G5EGK1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Vinculin
- Paxillin homolog 1
- Alpha-actinin, sarcomeric
- Integrin beta pat-3
- Actin
- Integrin-linked protein kinase homolog pat-4
- Calponin-homology
- Paralyzed arrest at two-fold protein 6
- Zyxin
- Calponin-homology
Sequence:
MGVLSLTVSSAEKGIKKTMQFEPSTLIYDAAKLIREKFAMHDVNANEYGIFRLDENPSKSLWMDNGRTFEHYLVRNKDEIEYKRKIRLLKVRMLDGAVKTISVDESQPVSQLMMTVCNKIGISNYEEYSLVRDDILMQNGGGGGGGGGQNGGSTWNLKEKESRSKSSDRGGGGIYGTMRKKNEQKLEELRKKLHTDEELPWLDHTKTLREQGITEEETLILRRKYFFSDSNVDSRDPVQLNLLYVQCRDGILRGLHPVEKETAFQLAALQSHIQYGDFPYDKPKFHLDGRDVLPKEYAKNKENEKKVVAMYKELSGTSELDAKSKYVHLCRGLKTYGVTFFVVKEKLPGKNKLVPRLLGVNKESVMRVDENSKQILKEWPLEQVRRWVPSAKCFSLDFGDYQDGYYSVQTTDGEKIAQLIQGYVDIILKKKRTQDHQGIEGDEGSTMLEDMVAPAKATLVAHGQIGSGQHATDGLVAVRGVLRTPQGGQGYGINGAQYGAVSGEITSQELARAQRLRYQDMYQHPQRALIGTIEATIRAVEDAEIELEAEPQIDIPRFNDDYSQNRWMEEQQAVNKENVNERLAAMGAATAQVVQWTAVEEYDDRVGTAIATIGSNLPDVSRNVRDLGAFMEHRERGDLLDATKKLCGAFGKFLNTVNPETEARRNEVFRTAGHVGETSQHLINVMEAPNEGQQKFDERLVQSAKNVATSTAQLVLCAKTISAECDEPQVQERVIQSATKCAFATSQLVACARVVAPTIDNNACQQQLSTAATEVTQSVNNLLHDAEHAVYQQSSLTDIHEAARQVTSALDSLLEHAKCSPKTQTTRREEEEMYNEVLRRTNRMVVHQGPSEDLTREARKVVRHSQLLTEQFQHEAHQRPEHRERLLDAAAKVAHATSEMILATEQAESQPRQVETEYALRTAAERLGQVTNETTQEQQEQHIMQRLEQAAKQTAYDATQTISAANSAKDVIESRSYKENLVYESTQTAGHLPNLITSIRESQKVDNTPGEKFKAQSRLIRDSYKVLETSVRLFETARTAVPMVSDSHLASSLDQSANRLGTSLADLRTSVNDAQQLNFSQQLLYSEELIKELDDQLVNTQKRAIARELPPIQNATSFSVSSKLMATTSNVGSGVAQLITAAATSNDDKYVGTSAVELAQGLRDFTDAITEIVTVRTDIQLDKLIVSARSVVHESGRVFDRVREKSAPTVLTDAAMNVSTSLKQVISCLPDTKHIEKAIHEIQTAHTSANIRPMEVRQAANKFIEATSQLVVTIGSPDSREAVDIFVRAYCDLHGSVVAQLQRQSNMNNVKTAIIDRLEEAQRGSIGVLETLRQAGNPSDHTLSQQFTSKTRELATTVNQLVELSGMDGGESRWQRECDAALRRIQAVYHVTQHANVPLNDNGYFASLQSVSDGSRRLGEAMTGMARHAKGNDTEGFCTSVRDSADALCSLAESASHSAYLVGISHPASSPGRAALIDSSEVARSVESINASCQRVESRQLNREELMSDISSITKQSSSLAQLCRIASEKTQNPNVKKHLVGCAMGVASKTSSLVTAFKDLDRMPDAESRCTSSASELRQVALQLLHFADKPDFAAIQGSISTEGHSAQQPILQSSREMLDSSAQMIQTAKSWASAPQDEATWQRMAVNSRQVSDSIMRLVNAIHEAAPGQMELEAAIGRLSALSGQIERSAMDCYASGNVQKHGANAERQLLQQVQHIASQLEDKVDDLHNAAVEHGERLPKVVQLHCQMVEDLADAACCAAGMTVDSNQQTELFDKCKTVVEAELAMMVASRESGGNPNAVHAHANVKDAAGQLKHAIGDMRQTIAKVSSEQGAVQGMVDTISSSIAHTDVAVSSAHPGSSFADAQTRMTAYLEDIRRTAIEMPTLNTTDLGAASLNLSEKYRLVAGDVRQAAGMLPEADIGQRLKLAVQKLGTSCIETVTVAGGKRAHPEDERIQRQLSSQAGTVVERVEQVLAALHSASRGTQACINAANTVSGIIGDLDTTIMFATSGSLNSSDDRKFPSHKEAIVKTAKALVEDTKALVAGAASNQEQLAVAAQNAVRTIVNLSDAVKTGAVSLSSENSETQVLVIHAVRDVAAALTSLIQATKNASGLSLQHPAMGHLKDAAKVMVSNVARLLKTVATVEEKNQQGTRAVEAAVDAIGFEMKQFEHDLNEGAAIPTDFRPEHLQQTAEHVSEITKRVMQGADAPQSEEEIIGVANLSRSAVRSLLAVVRTISNDADTAPQRYAVLDSGRDVANNVKSLLVSLHTQMVRNPGQEESRRLLLEASKGVSSALSHLVGLCNEMTGLPHNHEMESAAAQAENELLGAASSIEAASAKLAELRPRQIVQENTQEIVETEFDDNIIISAKGILHAVHTLMRSASNAQRELAMQGRAAAGGTGTYQWSEGLISAARVVVASVHKLCDAANTLMKGQTTEERLISAAKQVSSSTAQLLVACNVRADPDSQANRRLQAAGQAVRNAAERLVQSAQQEMIARDDRNIAISDRLVNGIAQVMDAQEEVLRKERELGEARHKLAHLNKARYERDGEEA