wanglab/gogpt-training-data huggingface dataset:
Protein: Exo-1,4-beta-xylosidase xlnD (EC 3.2.1.37) (1,4-beta-D-xylan xylohydrolase xlnD) (Beta-xylosidase A) (Beta-xylosidase xlnD) (Xylobiase xlnD) (Q5BAS1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Endo-1,4-beta-xylanase B
- Xylanolytic transcriptional activator xlnR
- Exo-1,4-beta-xylosidase bxlB
- Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein
- Endo-1,4-beta-xylanase C
- Endo-1,4-beta-xylanase A
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Alpha-glucuronidase A
- DNA-binding protein creA
- Probable alpha-galactosidase B
Sequence:
MRSLISVAVLSALPTAFSQANTSYTDYNVEANPDLFPLCLQHLNASFPDCASGPLSLTPVCDRSLSPKDRATALVSLFTFDELVNNTGNTGLGVSRLGLPNYQVWGEALHGVGRANFVESGNFSWATSFPMPITMMAALNKTLIHQIGTIVSTQLRAFSNAGLGGVDVYSPNINTFRHPVWGRGQETPGEDAFLTSVYGYEYITALQGGVDPETLKIIATAKHYAGYDIESWNNHSRLGNDMQITQQELSEYYTPPFIVASRDAKVRSVMCSYNAVNGVPSCANKFFLQTLLRDTFEFSEDGYVSGDCGAVYNVWNPHGYASNEAAASADSILAGTDIDCGTSYQWHSEDAFEDSLVSRSDIERGVIRLYSNLVQAGYFDGEDAPYRDITWDDVLSTDAWNIAYEAAVEGIVLLKNDETLPLSKDIKSVAVIGPWANVTEELQGNYFGPAPYLISPLTGFRDSGLDVHYALGTNLTSHSTSGFEEALTAAKQADAIIFAGGIDNTIEAEAMDRENITWPGNQLDLISKLSELGKPLVVLQMGGGQVDSSSLKDNDNVNALIWGGYPGQSGGHALADIITGKRAPAGRLVTTQYPAEYAEVFPAIDMNLRPNETSGNPGQTYMWYTGTPVYEFGHGLFYTTFEESTETTDAGSFNIQTVLTTPHSGYEHAQQKTLLNFTATVKNTGERESDYTALVYVNTTAGPAPYPKKWVVGFDRLGGLEPGDSQTLTVPVTVESVARTDEQGNRVLYPGSYELALNNERSVVVKFELKGEEAVILSWPEDTTSDFVSSIDGGLDRKQDVIA
Protein: Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (CII-4) (Malate dehydrogenase [quinone] cytochrome b small subunit) (QPs3) (Succinate dehydrogenase complex subunit D) (Succinate-ubiquinone oxidoreductase cytochrome b small subunit) (Succinate-ubiquinone reductase membrane anchor subunit) (O14521)
Organism: Homo sapiens (Human)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:37098072, ECO:0000269|PubMed:9533030}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase assembly factor 2
- Succinate--CoA ligase subunit alpha, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL
Protein: DNA-dependent ATPase (Q5AKX3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair protein RAD51 homolog
- DNA repair and recombination protein RAD52
- DNA repair and recombination protein RDH54
- DNA repair and recombination protein RAD52
- DNA-dependent ATPase
- Crossover junction endonuclease MUS81
- Vacuolar protein 14 C-terminal Fig4-binding domain-containing protein
- DNA 3'-5' helicase
- DNA 3'-5' helicase
- DNA repair protein RAD50
Sequence:
MAVRKPLTQFTTPLGSGAGVPKDKRPPRVTDSATRLSKPFKVPFSSSTQNSVSSETITISRRPVRSTRKRTNYAVDGITSEKDDEEEYNNDQNVNGDGQIIKRKKFGALLPRSIINSDNIAKNEDKFKRSFTVPFDKNNSKQTEIQRGPPPPLGTKVRAILPPRALHDPTSEFAIVLYDPTVDKIPKISEVESSTSSSTSPEPEPETKETEERPIKRKRTHKSLAEILGIVTNPEEKLSKYPDVPVVIDPKLAKILRPHQIAGVKFLYRCTAGLIDARAKGCIMADEMGLGKTLQCLTLMWTLLRQSPRGKRTIEKCIIVCPSSLVRNWANEIVKWLGEGALTPLAVDGKSTKNSELGTALQQWSTAQGRNIVRPVLIISYETLRRNVDKLAGTEVGLMLADEGHRLKNGDSLTFTALNSLRCERRVILSGTPIQNDLSEYFSLLNFANPGYLGTRIEFKKNYENAILKGRDSTASDEEREKGDKKLNELSQMVSKFIIRRTNDILSKYLPIKYEYVLFTGLSPMQKDIYNHFITSPEIKKLMKGTGSQPLKAIGMLKKLCNHPDLLDLPEDVEGSEEFIPDDYQSSIAGGSASRNREIQTWFSGKFLILERFLQKINKETDDKIVLISNYTQTLDLIEKMCRYKKYGVLRLDGTMNINKRQKLVDKFNDPNGPEFIFLLSSKAGGCGINLIGANRLVLMDPDWNPASDQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVDEKEDVERLFSVANLRQLFKFQPDTQCDTHDTFNCNRCKGDKGQFIKAPAMLYGDATTWNHLNHQALANNEDILITNEAQHNDVTFAFQYISH
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A0A8I5ZW41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGSLGALALCLLRLLLLGLQRPPLPGAGAQSAAGGCSFDEHYSNCGYSVALGTNGFTWEQINTWEKPMLDPAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDTHCIDFHYYFSSRDRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFYQVIFESVSLKGHPGYIAVDEVRVLAHPCRKAPHFLRLQNVEVNVGQNATFQCIAGGKWSQHDKLWLQQWNGRDTALMVTRVVNHRRFSATVSVADTSQRSVSKYRCVIRSDGGSGVSNYAELIVKEPPTPIAPPELLAVGATYLWIKPNANSIIGDGPIILKEVEYRTTTGTWAETHIVDSPNYKLWHLDPDVEYEIRVLLTRPGEGGTGPPGPPLTTRTKCADPVHGPQNVEIVDIRARQLTLQWEPFGYAVTRCHSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEGRMESEELVVQTEEDVPGAVPLESIQGGPFEEKIYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTRIATKISAPSMPEYDADSPLNETDTTITVMLKPAQSRGAPVSVYQLVVKEERLQKSRRAADIIECFSVPVSYRNASNLDSLHYFAAELKPSNLPVTQPFTVGDNKTYNGYWNPPLSPLKSYSIYFQALSKANGETKINCVRLATKGASTQNSNTVEPEKQVDNTVKMAGVIAGLLMFIIILLGVMLTIKRRRNAYSYSYYLKLAKKQKETQSGAQREMGPVASTDKPTTKLSTNRNDEGFSSSSQDVNGFTDGSRGELSQPTLTIQTHPYRTCDPVEMSYPRDQFQPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHPAEHTVGTATLGRAASPGMVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGNTAIPVCEFRSLYYNISRLDPQTNSSQIKDEFQTLNIVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQLCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKAVRRLEKWQEEYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF
Protein: MIP08013p1 (Mitochondrial phosphate carrier protein 2, isoform A) (Mitochondrial phosphate carrier protein 2, isoform B) (Mitochondrial phosphate carrier protein 2, isoform C) (Q0E8E8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- ATP synthase subunit alpha, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- AT02348p
- Cytochrome c oxidase subunit 5A, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit beta
- ADP,ATP carrier protein
- ATP synthase subunit b, mitochondrial
Sequence:
MFSSFFETARNSPFRTPMSMARCDAAAPVVEPQPVEGRQIAAAATPVANQQDSCEFGSTKYFALCGIGGILSCGTTHTFVVPLDLVKCRLQVDQAKYKNLVHGFKVTVAEEGARGLAKGWFPTLLGYSAQGLCKFGLYELFKVKYAEIIGEENAYLYRTSLYLAASASAEFFADIALAPFEAAKVKIQTIPGYANNFREAVPKMLKEEGVNAFYKGLVPLWMRQIPYTMMKFACFERTVELLYKYVVPKPRADCTKGEQLIVTFAAGYIAGVFCAVVSHPADVVVSKLNQAKGASAISVAKSLGFSGMWNGLTPRIIMIGTLTALQWFIYDGVKVALGIPRPPPPEMPASLKAKQH
Protein: Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) (Q9I514)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylamine--glycine ligase
- Phosphoribosylformylglycinamidine synthase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Amidophosphoribosyltransferase
- N5-carboxyaminoimidazole ribonucleotide mutase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Bifunctional protein FolD
- N5-carboxyaminoimidazole ribonucleotide synthase
Sequence:
MPKLCNVVVLISGSGSNLQALIDSLRDGATPARIRAVISNRADAYGLERARQAGIQTEVLDHKAYADRESFDEALAQRIDAHEPHLVILAGFMRILSADFVRHYQGRLLNIHPSLLPRHKGLHTHQRALEAGDREHGCSVHFVTEELDGGPLVVQAVIPVESQDTPERLARRVHEEEHRIYPLAMRWFAEGRLRLGEQGALLDGQALPATGHQIRTKEIRNA
Protein: DENN domain-containing protein 5B (Rab6IP1-like protein) (A2RSQ0)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- DENN domain-containing protein 3
- DENN domain-containing protein 4C
Sequence:
MSGSSAAPGPGSGSSPAACRFAHYFVLCGIDADSGLEPDELAGENFDQSPLRRTFKSKVLAHYPQNIEWNPFDQDAVNMLCMPKGLSFRTQADNKEPQFHSFIITREDGSRTYGFVLTFYEEVTSKQICTAMQTLYQMHNAEQYSSVYASSSCSMDSLASSIDEGDATSLLKLQRYNSYDINRDTLYVSKSICLITPLPFMQACKKFLFQLHKAVTSQQPPPLPLESYIHNILYEVPLPPPGRSLKFYGVYEPVICQRPGPNELPLSDYPLREACELLGLENLVQVFTCVLLEMQTLLYSQDYQRLMTVAEGITTLLFPFQWQHVYVPILPASLLHFLDAPVPYLMGLQSKEGTDRSKLELPQEANLCFVDIDNHFIELPEEFPQFPNKVDFIQELSEVLLQFGIPPEGSLHSSESATKLKNMVLKDLANDKKNGNVPNNSVSVYELLKGSETIARLQALAKRTGVTMEKIDLPASLSEKEKDLKLQCEEADLRDSQLNVQLREVFANRFTQMFADYEAFVIQTAQDMESWLTNREQMQNFDKASFLSDQPEPYLPFLSRFIETQMFATFIDNKIMSQWEEKDPLLRVFDSRIEKIRLYNVRAPTLRTSIYQKCSSLKEAAQSIEQRLMKMDHTAIHPHLLDMKIGQGKYEQGFFPKLQSDVLATGPANNNRWVSRSATAQRRKERLRQSSEHIGLDSDLREKYMQEARSLGKNLRQPKLSDLSPAVIAQTNWKFVEGLLKECRMKTKRMLVEKMGHEAVELGHGEANITGLEENTLIASLCDLLERIWSHGLLVKQGKSALWSHLLQFQDREEKQEHLTDSPVALGPERRKSDSGVMLPTLRVSLIQDMRHIQNMTEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQPLTKKLYKRYAFLRCEEEREQFLYHLLSLNAVDYFCFTSVFTTIMIPYRSVIIPIKKLSNAIITSNPWICVSGELGDTGVMQIPKNLLEMTFECQNLGKLTTVQIGHDNSGLLAKWLVDCVMVRNEITGHTYRFPCGRWLGKGVDDGSLERILIGELMTSASDEDLGKQCRTPPQQKSPTTTRRLSITSLTGKPAKPNAGQIQEGIGEAVNNIVKHFHKPEKERGSLTVLLCGENGLVAALEQVFHHGFKSARIFHKNVFIWDFVEKAVAYFETTDQILDNEGDVLIQKPSSKTFCHYVNAINTAPRNIGKDGKFQILVCLGTRDHLLPQWIPLLAECPAITRMYEENALLRDHMTVNSLIRILQTIQDFTIVLEGSLIKGVDV
Protein: Spatacsin isoform 1 (Spatacsin variant 1) (D4HMK8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLEALSRSDAGAQAVLEVDLLADGELCVGLKDWRRVKLSAGPSLLCCVNAQGETSLRNISDSRRAEHTLQHTCVDFLWEDVSVSSGARVKPKLLLLDSEFSLHMYDVDQDDQPTLVCETSSNTLLQIIKHTHADMCAVASVRLLCFSEGRCMLLVNTCVLLQLRLTEDTLEPISCCRLGVECVEECVDCRLCRGALFILLNSGLSYVFDSTDGQLLAKVDFPSYCCNAGVSPSTSSFCLLQISADLSTAVSVTRQNQAYAVHLDHYFSVYTDHLYCRAAPIRPFLRPVESWDQDSLSSSTHSLSALNKPLQADRSWESRLSALYNQTKAPVRPVHISPWYKDFPHIECRRAAATAKLCHSSVKTGGAVMSFNVPDGATPAGLNVSEFSALITFVSPANANTVLAYWGLENESVTYHRADANAIPVQRSAEENLCLLLKTSGLSVVLFCVSQDELLNRLMVFGSAGTVDSLCHLNAWGRCSIPIHALQAGLKNHQLDTVDFFLKSKENILSSSSGFSPGDPPPSSSNTHTHLRSIEALCPALDLLRSAIRDTHTEAQSQQFCEQLLSITMSFLNTQTRVLLSGAHDLDDNLQQCVCVLDGFISDLRVFLKRFPWGVGGDARTHTDAHTHTAASGREEEHQWISLSDEEVVHRAVLSRRISHAQAFLRRRGSAEHTLQDIRRTGLKHTHTCLTLRDLQQATTLLTHMGFNVKEQLHNICVYTADRDLRAFMVEELQKQHHLSADELKQVNFIHTIESLCSKPANRSSRRLDANRVLQVSRCDPQSRRLLEKLLQDSDSSSTSLLDPLRLHWVKHWDRDAQTHILLSRTHTHTQCSGDAAVLWAYLTSLHDSVRCSAWLSSSSVCDRESSAAPCWPQLTAHVLDTCTRCGEHLHNIILDQLARQGQFVPAEMQDFQQLLWRLAQAGGVMHDGKEPSLPQAGGVMHDGKELCCSQEQEFHQRFILHCLENNLQFLLYTYLEHYGLSPENCPLLSDSSVCESFPCFQMMLKLQKITTHLTEPECVFEASLAAAQVLLLPGSQASISSVLLEGHSLLTLATAMFTAGGIQQAVSTVDPQLLRMALRQYPQLKTALFPQSGPRGDVSLYHLLQSLHPLDSSRLFGWQSANSVSASSEASSEPPHFSSSHLVSNFAIVENLDFLYFLRHGRPAFAYAVYLTQHLRDCSNTKLQLSMAVDQSYSLALLNFSSASVSSACVCFCELMGVCSLKLRTDLRTLNLIHKHWSQSREDGDADSLRHTLVEKASQLISAEHRAAQDLLLHLEAAIRDALEKKTISRWSFEAAQEWALPVQFCRLHALPLSSAYPLDCAHDGQWLHFLLFVQTHQYPPQQVRFLSESFSPALQSHISLAFQDLRSPIEDQGVSVTPPSPDESSDWPTELFQVLLQSQEKPHPWRILLSEAVRRRCAPLAVLAASHQGSELLQCLCVWILTSVDDDDVTQEAAAHINESPAHHVWNLHDLSILWKTLLSRSKIRPLIRGFQLFQRESPLIAMLQMYEFCFDYKDYQRAKDKLLDFQKSLLNLRSSSVLSSSDVLPVQWVESQASVLLLTLLKQSRTQYELRRLLQLLLDVEKLLKSNGPDFRLLSELSQLLCETPVCVSSRLLDCYSPSVLQEECVRIMEELQDAGLYMQARRVAELAELPAHTLIINQLLRDLSAQKLKRQWERQEIRLAFWRRSHDQLQTEHVQPETACHFFLSQAEVALQSDSELVNLQERCVLLGLAGLWLSRCDPPPSTPILADLEKRQWECRIQQRLLLADLERQSLFAPSALSEDSPENLLRDFSFSRMPALNDDANLSLDGLPADSNSCILPDDQQRALASLIAQLLNDGSVNEASRVCRYFRFFHRDVWLVLRCRGLACGELQPELHSPDGESRRSLPSSPSMSSLSSFVVVSSPDDQLQLQLQLLVDQCSHGKSYCKQVLSLYQLSKELQCSFSELWSSEPECVLQKVLLSRQSERCKKAEAFISAQSLQPHTVANLISTAVLEGLTAHTRDADTSERLIFSASDSRESFLQLAKLCGDANLVGNKLLDSIGSVPLSDLSCIVELLILAHDCFSVTCNLEGIVRVLQACRHLSHTHLAHGDAHGLLVRLLTGIGRYNDMTYVFDLLHQNHRFEMLLRKKVESNVRLKTALLDYIKRCLPGDSEKHNMVALCFSMCREIGENHEAAARTQLKLIESQPWVITAELKKALVKVQTLLKDAAESYSKDSCVRQAVRCVKLAKLVTLQLHFLNQGLELRIINLQHTDLQNTSNTLPHCYQVFVLAEAYDFSPDWAEVLYQKVIMRGDFSYLEEFKRHRPLAASLFQDISNKVCHQKPPASCSQHLKKLLSHCEDVYTHYKLAYEHQFLDVANMLLQDSKTNSFLKDRLRT
Protein: Reticulon-like protein (Q9VMV9)
Organism: Drosophila melanogaster (Fruit fly)
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:
Sequence:
MDRNFDELKKEAAATNEDIFKQAQRAYEDSALGGDTGNVSGGAQDDNAHTEHYFANEQKKLDFGDAQEFVQRLAADAKDAKLDLDTKFAQKTDDFEDFLRDAGKEVKQGISGLTTDFMNAERGFSAPLAPFSETVAQAPVIPAQAPAVPDHAPAVPAPVAPAPAVPAPLPVEEDLLGSFTDQPSAPLQAFQPTAPSTANFYDDEEDDFLGKPTTAAPAAPVAPLTKANQDSDTESPSVSYTPSPAKKPIVDALKDQDNEKFISSEDLASDFKEEPRSAPTPAPAPAPILDAAPAVAPAPVAVPVSVPVAKPQPVPVAVPVTTALITDLDDEEVVFKPTVQEAPKAPTIAAPVVEPKPEPPKPKVEPAKPKVVPVAPVESTQPQPKIASVEEIFCKYGLVESLIYWRDVKKSGIVFGAGLITLAAISSFSVISVFAYLSLLTLFGTVAFRIYKSVTQAVQKTNEGHPFKDYLELDLTLSHEKVQNIAGVAVAHINGFISELRRLFLVEDIIDSIKFGVILWVFTYVGAWFNGMTLVILAFVSLFTLPKVYENNKQSIDTHLDLVRSKLTEITDKIRVAIPIGNKKPEAAAESEKDK
Protein: Coatomer subunit delta (Q9U8A9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}.
Interaction partners:
Sequence:
AAFPKLMTAGKQHTYVETDSVRYVYQPMEKLYMLLITTKASNILEDLETLRLFSKVIPEYSHSLDEKEIVENAFNLIFAFDEIVALGYRESVNLAQIKTFVEMDSHEEKVYQAVRQTQERDARQKMREKAKELQRQRMEASKRGGPSLGGIGSRSGGFSADGIGSSGVSSSSGASSANTGITSIDVDTKSKAAAKPASRNALKLGGKSKDVDSFVDQLKNEGEKIANLAPAAPAGGSSAAASASAAAKAAIASDIHKESVHLKIEDKLVVRLGRDGGVQQFENSGLLTLRITDEAYGRILLKLSPNHTQGLQLQTHPNVDKELFKSRTTIGLKNLGKPFPLNTDVGVLKWRFVSQDESAVPLTINCWPSDNGEGGCDVNIEYELEAQQLELQDVAIVIPLPMNVQPSVAEYDGTYNYDSRKHVLQWHIPIIDAANKSGSMEFSCSASIPGDFFPLQVSFVSKTPYAGVVAQDVVQVDSEAAVKYSSESILFVEKYEIV
Protein: Protein shisa-like-1 (Q3SXP7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTSCGQQSLNVLAVLFSLLFSAVLSAHFRVCEPYTDHKGRYHFGFHCPRLSDNKTFILCCHHNNTVFKYCCNETEFQAVMQANLTASSEGYMHNNYTALLGVWIYGFFVLMLLVLDLLYYSAMNYDICKVYLARWGIQGRWMKQDPRRWGNPARAPRPGQRAPQPQPPPGPLPQAPQAVHTLRGDAHSPPLMTFQSSSA
Protein: Lipoarabinomannan carrier protein LprG (27 kDa lipoprotein) (Antigen P27) (Lipoprotein LprG) (Triacylglyceride transfer protein LprG) (A0A0H3M3S8)
Organism: Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Function: Probably helps membrane protein BCG_1471c (P55) transport triacylglycerides (TAG) across the inner cell membrane into the periplasm and probably ultimately to the outer membrane. TAG probably regulates lipid metabolism and growth regulation. Binds di- and triacylated phosphatidyl-myo-inositol mannosides (PIMs), and glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM), facilitating their recognition by TLR2. Required for activity of drug efflux transporter BCG_1471c. Required, probably with BCG_1471c, for normal surface localization of LAM.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000305}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WK45}. Secreted {ECO:0000250|UniProtKB:P9WK45}. Note=Present in extracytoplasmic vesicles (PubMed:21364279). {ECO:0000269|PubMed:21364279}.
Interaction partners:
Sequence:
MRTPRRHCRRIAVLAAVSIAATVVAGCSSGSKPSGGPLPDAKPLVEEATAQTKALKSAHMVLTVNGKIPGLSLKTLSGDLTTNPTAATGNVKLTLGGSDIDADFVVFDGILYATLTPNQWSDFGPAADIYDPAQVLNPDTGLANVLANFADAKAEGRDTINGQNTIRISGKVSAQAVNQIAPPFNATQPVPATVWIQETGDHQLAQAQLDRGSGNSVQMTLSKWGEKVQVTKPPVS
Protein: Protein transport protein sec24 (Q9UUI5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- COPII coat assembly protein sec16
- Protein transport protein sec13
- Protein transport protein sec31
- Protein transport protein sec23-1
- Protein transport protein sec23-2
- Uncharacterized protein C4.03c
- Protein transport protein sec22
- Small COPII coat GTPase sar1
- Sad1-interacting factor 1
- Uncharacterized protein C227.19c
Sequence:
MSQEDAFYGKGSYGASSGNSNIPPQGFQPVYPVAGQLDNTAPYVGAVAEGTAEGIVSNGEYAVGAMGAAPTNIIGSVDQQPPVSHTSHKSRRQYPAEVFELTNTLAASPAPPSLSEPSYVMARTPSSSPYPHDRAEVGTKSLSAQFGGMSLGADGAAAMPTNELVSVDLYNQTPEISDLTSPPPPINLPLSYSATGAATSNCPPKYVRSTINCVPTTNSLLKKSKIPFALVIRPYTSLVEEDDPVPVVTDTIISRCRRCRMYINPFSIFIDNGHRYRCNSCGIVNEVPQSYDWDSFRNVQRDRWQRPELNYAVVDFIAPQEYMVRAPQPLVYVFLIDISFVSISSGMVGTASRAILESLDRIPNKEGRAKVAFIGVDSALHFFSVSPGAEEATQLVVSDLEEPFLPRNQDLLLNLRECRQGIENLLERFQSMFATTRDSSNALGPGLKAAHRLIENIGGKICCLISSLPNVGVGKLELREDPKLLGTNRESSLLHPNDSFYKSFAVECSTSQVSVDMFLFSSQYQDVATLSCLPRYTSGKTQFYHRWNASRSEDALKFASELTNYLSMEIELEAVMRVRGSNGLRMSSFYGNFFNRSSDLCAFPSFPRDQSYVVEVVIEDTITKPFVSFQTAMLHTTCNGERRIRVLTISLPTTNSMTDLYASADQVAIAQYLTVRASEKALSSTLNEARDSIISKLVEILEVYKKNLAGQNTGAAIPLQISTNLRLLPLLCLALTKHTGFRRSSHISSDLRSIALCYLSTLPTPLLMRYIYPTLYSLHDMPIEAGTVTEQGVVLPSALNLTSALLQSFGLYLVDTHIHQFLYIGKDAVPQLLIDAFGVNSLADLKAGRFTMPVIDNPLNVRINAILGKLRSLDKGSTIMPSLYLVRGDGDPQLRSWFFSHFVEDRSENSPSYLQFLQTLKEKVRD
Protein: Ion transport domain-containing protein (Q688B4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSERKKSLITTINNQRKYSQVAKAAVLSSAMLARKNSSSRGAPGSAAGFGARESIAAISDMLSSQHKKPVRSSYVESDRVEWALKIACTISMITVCIHTPRTIELFQPLNYIILAADFISVSIFMLDSVLRIHYEGIFRCDSSYLSNRWSQFSVFISIIHLLSFLLHCYQLIDNFFPFLHLNYRAWYGAIRSIRPFIIIRLIPLVVKFKLPKNRIEQLLKRSSQQVKNVTLFFVFFMTLYAIFGIQLFGRMDYHCVQPKTDPNNVTIMDLAIPDTMCAPEGIGGYECPAPMVCMQLNLNAKGEGFYGMFNDFGASVFTVYLAASEEGWVYVLYDCMDSLPSYLAFLYFCTLIFFLAWLVKNVFIAVITETFAEIRVQFSEMWQKKEVTLDEGFRKKLEKTDDGWRLIRLDGEVEPEGPKQKLQWMLRSMYFQCFVIIFVVINAIGNAMFVYRHDETDKPRKYNFYLFEVGFTILFNVECIIKILCYGFRNFIRRGIFKFELILCLGSSLNCVKFFYERNYFTYFQTFRLLRLIKASPILEDFVWKIFSPGKKLGGLVIFTIAFICCYSAISLQLFYSVPNLHHFRTFPQAFMSMFQIITQEGWTDFVVEVLRATDDNLVPLVALYFVAYHLFVTLIVLSLFVAVILDNLEMDEELKKVKQLRAREATTSMRSTLPWRLRVFEKFPTRPQMAAMRKADSDFPMPKVRGSFTHQFAVDHSLETTDVIESDFEFPKRIMKSAGKRKISKSGLTFRQIGSTSLRCSLNNLLEKSRSMTGKFLQTAVRNKQFNMYSENGDLSRPSDSAPKKNAKQGEIDIRALQQKRQLAEITRNRIEEDMRENHPFFDRPLFLVGRASQLREFCKKMVHSKYDSQDDGTNGGAKTKKRFKEIRALIGIMPYIDWAMATVTIVSCISMLFESPWPTTGENLVMNNGYLQISDYFFVLSMTFELCVKIIANGLFFTPKAVVRDVGGVMNLFIYFTSVIFLAWMPKHVEINSLAQFLMICRAMRPLRIYTLVPHIRRVVLEFFRGFKEILLVTILMIVVMFIFASFGVQIVGGKLAACNDPTVSSRENCTGVFWQKLFVTRLEVYGKDTEAMHPKIMVPRVWTNPRNFNFDHVGNAMLALFETLSFKGWNVIRDILWSRHGPWAVVFIHIYVFIGCMIGLTLFVGVVIANYTQNRGTALLTVDQRRWHDLKARLKMAQPLHVPPKPSESARLRTKLYDLTMSRWFNQAFALLVVLNSFTLVIPWNVEEEEQRATYVFTVTALAAFMNMLFVIEIILKVIAYTFSGFWQSRRNRVDLLITVFGVIWIFLHFFVALPSSKIDVDVQVELKKFTYTFGYLVVILRFFTIASRNSTLKMLMLTVIMSMFRSFFIITALFLLVLFYAYTGVILFPMVKYGMAVSKHVNFRTASEALVVLFRCLTGEDWNDIMHDCMRSAPFCYWNEGMNYWETDCGNFYGAIIYFCSFYLIITYIVRNLLVAVIMENFSLFYSSEEDALLSYADIRNFQYVWNMVDQEQKRTIPVERVKFLLRLLKGRLEVDPEKDRILFKHMCYEMERLHNGEEVSFHDVLYMLSYRSVDIRKSLQLEELLQREELEFIIEEEVAKQTIRTWLEGCLRKMRNPSQKDAEGVLPFGGGHPVIHSSGHSSISHEETVAQRLRFENIRGDSVDTEETESSEEETPPPIRKKAAVKNRRGSIPDVLSRTGLFQEAARKFMVGSSSEKKQVKSRSPETVQLLPKRANSEIRKGSGQPKNFHLQLNVYDLPDVEERGEDSPFSPKNLSDDFNGEHSPLVITPSLPVPPTHGSPRPLMPCETTKDIEKWWNSLVD
Protein: Lipid transferase CIDEA (Cell death activator CIDE-A) (Cell death-inducing DFFA-like effector A) (O70302)
Organism: Mus musculus (Mouse)
Function: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:20810722, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26609809}. Nucleus {ECO:0000269|PubMed:22245780}. Note=Enriched at lipid droplet contact sites (PubMed:18509062, PubMed:22144693). Using a GFP-tagged construct, has been shown to localize to mitochondria, where it could interact with UCP1 and hence inhibit UCP1 uncoupling activity (PubMed:12910269). These data could not be confirmed (PubMed:18509062, PubMed:22245780). {ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780}.
Interaction partners:
- Mitochondrial brown fat uncoupling protein 1
- Lipid transferase CIDEC
- Cytochrome c oxidase subunit 8B, mitochondrial
- Histone-lysine N-methyltransferase PRDM16
- Very long chain fatty acid elongase 3
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Hormone-sensitive lipase
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Type II iodothyronine deiodinase
- Transmembrane protein 26
Sequence:
METARDYAGALIRPLTFMGLQTKKVLLTPLIHPARPFRVSNHDRSSRRGVMASSLQELISKTLDVLVITTGLVTLVLEEDGTVVDTEEFFQTLRDNTHFMILEKGQKWTPGSKYVPVCKQPKKSGIARVTFDLYRLNPKDFLGCLNVKATMYEMYSVSYDIRCTSFKAVLRNLLRFMSYAAQMTGQFLVYAGTYMLRVLGDTEEQPSPKPSTKGWFM
Protein: Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) (P49088)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Argininosuccinate synthase
- Isoaspartyl peptidase/L-asparaginase
- Adenylosuccinate synthetase isozyme 2
- Multifunctional protein CAD
- Adenylosuccinate synthetase isozyme 1
- N-acetylaspartate synthetase
- Amine oxidase
- Aspartoacylase
Sequence:
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPYLWLCYNGEIYNHKALQQRFEFEYQTNVDGEIILHLYDKGGIEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKALTEDGFLAVCSEAKGLVSLKHSTTPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCTDEPLHAIYDSVEKLFPGFEIETVKNNLRILFNNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEAQVPYALQTFAIGMEDSPDLLAARKVANYIGSEHHEVLFNSEEGIQSLDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKDGIEKHLLRETFEDSNLLPKEILWRPKEAFSDGITSVKNSWFKILQDFVEHQVDDAMMSEASQKFPFNTPQTKEGYYYRQIFEHHYPGRADWLTHYWMPKWINATDPSARTLTHYKSTAKA