wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipid-transporting ATPase C887.12 (EC 7.6.2.1) (O94296)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P39524}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit mug89
- Uncharacterized protein C1604.12
- Plasma membrane ATPase 2
- Adhesion defective protein 1
- Translation initiation factor eIF2B subunit gamma
- Uncharacterized protein C1805.14
Sequence:
MARDVDNKQNAKRISRDEDEDEFAGESMVGRTLDNPFLGEDEFEDIFGSESQYISSSGQNSTNPFLADTRIENSPLGSESKANQLNKQGTNVNHIEIPLRDFNDPTQPESFLPPPKNTFTSRIKKIKNLFKKEKKQVKPEDLGPRQIILNDYSANHFLHNAVSTCKYSAFTFLPKFLKEQFSKYANLFFLFTAVVQQIPGITPVNRYTTIGPMLIVLSVSGIKEIMEDIKRKKQDQELNESPCYVLQGTGFVEKQWKDVVVGDIVKIVSETFFPADLVLLSSSEPEGLCYIETANLDGETNLKIKQALPETAGLLKPVELGQLSGEVKSEQPNNNLYTFDATLKLLPSDRELPLSPDQLLLRGAQLRNTPWVYGIVVFTGHESKLMKNTTETPIKRTSVEKQVNSQILFLLCIFVFLCFASSLGALIHRSVYGSALSYVKYTSNRAGMFFKGLLTFWILYSNLVPISLFVTFELVRYIQAQLISSDLDMYNEETDTPAACRTSSLVEELGQVGYIFSDKTGTLTRNQMEFRQCTIAGVAYADVIPEDRQFTSEDLDSDMYIYDFDTLKENLKHSENASLIHQFLLVLSICHTVIPEYDESTNSIKYQASSPDEGALVKGAASIGYKFLARKPHLVTVSIFGKDESYELLHICEFNSTRKRMSIVFRCPDGKIRLYVKGADTVIMERLASDNPYLQTTIHHLEDYATVGLRTLCIAMREVPEDEYQRWSTVFETAASSLVDRAQKLMDAAEEIEKDLILLGATAIEDRLQDGVPDTISTLQTAGIKIWVLTGDRQETAINIGMSCKLIDEDMGLVIVNEETKEATAESVMAKLSSIYRNEATTGNVESMALVIDGVSLTYALDFSLERRFFELASLCRAVICCRVSPLQKALIVKMVKRNTGEVLLAIGDGANDVPMIQAAHVGVGISGMEGLQAVRSSDFSISQFCYLKKLLLVHGSWCYQRLSKLILYSFYKNIALYMTQFWYAFCNAFSGQVIFESWSISLYNVLFTVLPPVVIGIFDQFVSAGQLFQYPQLYQLGQRSEFFNLKRFWSWITNGFYHSLLLFLCSIAVFYYDGPNKDGLASGHWVWGTTLYAAILATVLGKAALISNHWTQYTVIATLGSFLLWIVFMPIYAVAAPAIGFSKEYYGIIPHLYGNLKFWASLLVLPTIALMRDFVWKYSSRMYYPEEYHYVQEIQKYNVTDYRPRIVGFHKAIRKIRQMQRMRKQRGYAFSQGEEDQSRILDAYDTTHTRGAYGEMR
Protein: Signal peptide peptidase-like 2C (SPP-like 2C) (SPPL2c) (EC 3.4.23.-) (Intramembrane protease 5) (IMP-5) (A2A6C4)
Organism: Mus musculus (Mouse)
Function: Sperm-specific intramembrane-cleaving aspartic protease (I-CLiP) that cleaves distinct tail-anchored proteins and SNARE proteins. In elongated spermatids, modulates intracellular Ca(2+) homeostasis by controlling PLN abundance through proteolytic cleavage. During spermatogenesis, processes SNARE proteins and impacts vesicular trafficking which supports compartmental reorganization in maturating spermatids and may play a role in formation of the acrosome.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30733280, ECO:0000269|PubMed:30733281, ECO:0000269|PubMed:35960805}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IUH8}; Lumenal side {ECO:0000269|PubMed:30733280}.
Interaction partners:
Sequence:
MACLGSLHPLGSLLLLFLLLLLSPEARGEYGLVRVVSKNWSKDYCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSFHQAQDSSPRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQGLLIVSRARNQQCSDTISKPQDPSKPWPALTIPVAVLRYTDMLDIVSHTYGDTDVRVAMFAPLEPVTDYNMAIIFILAVGTVAAGGYWAGLMEANKLQRRQAQRGGGLGGHNQQQTVAAERSQRAWEDDDFEDAPMDFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLPLWRYQWVLPGQRVSVTWPLLLLAGLCAMVTVLWVIHRNEDHWAWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLFTKTGESIMVEVASGPADSSSHERLPMVLKVPRLSFSALTLCNQPFSILGFGDIVVPGFLVAYCHRFDMQVQSRQVYYMACTVAYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQGRAKIPAEPVAQPCIASAVGSKMKLEDAKDSRTTNRFEQAVDGESGDLESSTGDDMAEMVTLSEDEATSPEGHSESSEGWSDTNLDPNELPSGSPMALEAMLIPLIQPIPHPSELGHIRTQSRVHDSSLPWMGLHKRKGLKVKKSMSAQAPL
Protein: Spink5 protein (Q5K5D4)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKTATVPMLLTLAFYLTQDAAGEKGNQDPCMKFQAQMKNGTLTCPKGNNSSQSLNDIIFQSECILCKRALEQGAPTKIMNVKVLSRANRATDPAKLNCESFKQRRKDGDFICPSDTSSVCGTDGKTYRGRCELCAENAKSQNHVDVKSEGECGSSHLETDMCSDFRANVQDGRLGCTRESDPILGPDGRTHGNRCAMCAELFLKEAKENATRNRESRIRRDAEKELCKEFENQVRNGRLFCTRESDPIRGPDGKMHGNKCALCAEIFMRQFTEEKGKAEKNQKDAEERAKAKMEIQKRCSEFQDRARNGTLFCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAGSRNRRGSEESETYAKLCDEYRKARKNGQLYCTRENAPIRGPDGKIHGNTCSMCQAFFIQEDKARAKVKREAAKEMCSEFRNQARNGMLMCTRENDPVVGPDGKRHSNKCAMCASVFLLEEEEKKKDDKTEKVDAGKAKKEAVQELCRKYHTQLRNGPLRCTRRNNPIEGLDGKMYKNACFMCWAFFQQEAKKSGAGFRPKVKREVKVDCSEYLALSKRGEIFCTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGENQRITSGESSSGGNPKAKDECAQYRESMKHGQLSCTRESDPVRGVDGEHYNNKCVMCKELLQKEMEETNKNSASRSNGTGSATGKDVCDQFRSQMKNGKLLCTRESDPTRGPDGAMHGNKCAMCKERLEKEAAEKKKKEDEEKRNTETNKSDKEDKCHEYRSMQLDGRLICTRENDPVRDADGKMHVNKCAMCQMMFEREANERKMREENSRSQPTNEAKDQCGEVHNSVEDAKPRPARSSLPSIRGISKDECSEFQNLMKNEKLTCPETDDPVRGADGTFYQNKCHMCRDVLKNEAMKRSGLQEKSSDIRSTKEGDPEFSSSSRDSDMCKNYRILPRMGYLCPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHNPGACEESSNLKTVSTGTPASEKMMQ
Protein: Hypoxanthine phosphoribosyltransferase (A0A1D8PGN7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase
- Adenine phosphoribosyltransferase
- Guanylate kinase
- AMP deaminase
- Purine nucleoside phosphorylase
- GMP synthase
- Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase
- Inosine triphosphate pyrophosphatase
- IMP-specific 5'-nucleotidase 1
Sequence:
MSESEKMYISYNNIHQLCQEIAPKIKEFKPDLIIAIGGGGFIPARMLRSFLKEPGQPNVRIMAIILSLYEEIESENGIEKPGTQVVRTQWIDYHQSKIDLVGKNVLIIDEVDDTRTTLHYAVSELKKDVEEQSKAKGADPKDTKFGIFVLHDKQKQKKAELPDDIMNTGNYFAARSVPDSWIAYPWESTDIVYHQMKAEEQGNDVFLPSSTLE
Protein: Pyridoxine-5'-phosphate oxidase (EC 1.4.3.5) (Pyridoxamine-phosphate oxidase) (Q9NVS9)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Interaction partners:
- Pyridoxal kinase
- Chronophin
- Aldehyde oxidase
- NAD
- Pyridoxal phosphate phosphatase PHOSPHO2
- YjeF N-terminal domain-containing protein 3
- Aromatic-L-amino-acid decarboxylase
- Pyridoxal phosphate homeostasis protein
Sequence:
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP
Protein: Major outer membrane protein (Q48827)
Organism: Legionella pneumophila
Interaction partners:
Sequence:
MFSLKKTTAAVFALGSSALFAGTMGPVCTPGNVTVPCERTAWDIGITALYLQPTYDADWGYNGFTDVGGWRNWHDVDLEWDWGFKLEGSYHFNTGNDINVNWYHLDANTDHWAFVDQLHAYDITWDAVNAELGQFVDFSANKKMRFHGGVQYAYIKTDVNRHLNGFFLDNFNSKFNGFGPRTGLDMNYVFGNGFGIYAKSAVAILVGTSKFVDNCTVCGFSYGSKNAIVPEVEMKLGADYTYAMAQGDVTLDVGYMWFNYFNALHNTAAVNVGLGTSLETDFSASGPYIGLKYVGNV
Protein: Uncharacterized protein (Q38FB1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PRP1 splicing factor N-terminal domain-containing protein
- PRP8 protein homologue
- Peptidyl-prolyl cis-trans isomerase
- Spliceosome-associated protein, putative
- U5 small nuclear ribonucleoprotein component, putative
- U6 snRNA-associated Sm-like protein LSm8p
- U6 snRNA-associated Sm-like protein LSm4
- Small nuclear ribonucleoprotein Sm D2
- H/ACA ribonucleoprotein complex subunit 2
- Sm protein G
Sequence:
MPAKRRPVNIDNDEVIDFSTVGSSNMMKTPVPTTLLKSVVDLSSSEPPSSEAVTTASAMDMRLNAYTHRHAPRRRIGFCCNIAPQPIAVSGASALPKSTTAPTAASPSSAVSHGSNTTSMSADSKEQLDAFWREEAARREEKSKQVSRQQYEQQLCDLFRGAAPLVTPDPKPSGNEDGSRDMVEHRAYSLLEQFFTDGVPDVEPWDHWALTMPRYSRSNIAVGISLDRIYHPTLPPTHYSQLYLHAPNSEETVFRLPKTRDELRAERQERMRKAKEERDRAKKAAKQNEQLTVVESTGGGPAKVSITVSAKDRLSNRNLRYNLFGDSVLNPLGTDNKVFSQYQERFLEHQRRNHKRHVEAIPHQIEKRKQDIKRHSEERPVFRAYHIYPIYSSAHLGKLRNFANDGLLRGFVLWICRCHAIIVLTGGEVAVRHLERWILEKMKWESSETKAVRLMTCPLPDPATFSFVRQKSRKRDRQQQGDDGSRGREENQLEGDRHGTDGERAHVYMNFVESVQEGESFMCNMPAEGPWRDLTHVWRAAVGAVVAVGGGNNTESQSTV
Protein: (thale cress) hypothetical protein (A0A384L7B9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEETKERKIVVAVDESEESMEALSWSLDNLFPYGSNNTLILLYVKPPLPVYSSLDAAGFIVTGDPVAALKKYEYELVESVMARSRTVYQDYESDINIERRVGRGDAKEVICNAVQKLRVDMLVMGTHDYGFFKRALLGSVSEYCAKRVKCPVVIVKKQAQDN
Protein: Protein AST2 (ATPAse stabilizing protein 1) (P39945)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid raft-associated protein involved in the targeting of PMA1 from Golgi to the plasma membrane (Probable). May induce clustering of PMA1, which facilitates partition of PMA1 into lipid rafts after leaving the ER its and transport to the cell surface (By similarity).
Interaction partners:
- Putative uncharacterized protein YGL214W
- Protein FYV8
Sequence:
MAEKILENKDPKLEAMTVDHEVSAPKPIPVDEPTLTRVARPLRHVRHIPVKSLVFHSKHGPITFSYENKIKLPISKNKLVVQVNYVGLNPVDMKIRNGYTKPIYGEAGIGREYSGVITHVGDNLTNRWNVGDDVYGIYYHPKLAIGALQSSLLIDPRVDPILMRPKNTLSPEKAAGSLFCLGTALNLLAQLKEKDQLNTESNVLINGGTSSVGMFAIQLLKRYYKVSKKLVVVTSGNGAAVLSEHFPDLKDEIIFINYLSCRGKSSKPLRRMLDTGKVVDYDDFNTLKETEDYTQGKFNVVLDFIGGYDILSHSSSLIHAKGAYITTVGDYVGNYKKDVFDSWDNPSANARKMFGSMLWSYDYSHFYFDPNIKIIPKKNDWIHECGKLLNEGVVDCVVDKVYSWKNFKEAFSYMATQRAQGKLIMKVEGF
Protein: Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAT-1) (EC 2.3.1.15) (Q9HCL2)
Organism: Homo sapiens (Human)
Function: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:36522428}; Peripheral membrane protein {ECO:0000269|PubMed:36522428}. Note=Associated with the mitochondrion outer membrane of hepatic cells via a patch of basic residues. {ECO:0000269|PubMed:36522428}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate acyltransferase 4
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Glycerol kinase
- Glycerol kinase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
Sequence:
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSALLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLGGPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAEHDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
Protein: Zinc finger protein ZIC 4 (XlZic4) (Zinc finger protein of the cerebellum 4) (A0JC51)
Organism: Xenopus laevis (African clawed frog)
Function: May bind to DNA (By similarity). Induces neural and neural crest differentiation. Does not induce anterior neural tissue.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O73689}.
Interaction partners:
Sequence:
MSVEALGNTGMEPPFTKRNPALRLVDLAGAHHPHHHHHPPHLPQSVTGYPGYVAHSHSMAHVHPGEFAADSRLGPSAAFRTEHIGHPGALKLSPAHNPHHRHHHHHHHHHHMAGHAEVASSQTGAFGPAQSPAGSYSSLPHPAQAICAAGRDWLIGRDVTVPVMPGLTEQHSPSHHGMFLSTTGSYHGHHTEAGSHPYFSGAPEQASHATPGGQPLNGHIRLGLPGDMYTRSDHFSQPVTRTDHFASPSLHNYCGMNLNMNITPHHHGPGAFFRYMRQAIKQELICKWIEEDQLPKKLCSKTFSTMHELVTHVTVEHVGGPEQSNHICFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHSHVHTSDKPYNCKVRGCDKSYTHPSSLRKHMKVHCKSPPPSSGYESSIPSLVSPSSDSGQDPGATSSQPEPPTSSQGANLSEWYVCQQGSAASGIPTPPGNTPSPEHRKPSYSNWQATNTF
Protein: Membrane-bound acid phosphatase, putative (Q383A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMRPLSLVWWAIFVLLAATGANCSYVLELVQVVHRGGITPPPVGTPDREKLCSPDSGSSCAAIANHGVQQLIDMGAYIEKLYKNDDETEGAKAWLGSTYDSAAVYTHSFADPALVQAATALLKGIYAEEQGNITPAVISAPPADDTLLNVNALPSFVLGNEAKAQHFNKTMEEAVDEQFPDSSVIGTMGREVGLSEACSSADNRVWCCHRLQQLATMYSAMKDGGSGAPTVMENVGRLDAVATVRSHTLYGYSTEDELAKARGSLGQPLAQELLLGMRRKMLQKDDVNYNTHKVMQYVHNTPIRTTVGYQPTDLVPVAETFLIDLLRDDTTEVYFVRLRHAVVKTEPAAMPSAADFPFRCVNAAGDSSGVKSKDGFICPFDDFVRFVDSSKGTGAGGAICHLDTSTADNLQCSVVGPPTSPQCERYRRLCPRLACPDGHIYDVVSGMCTSLYADEAILTGGVVASLCIALLFSGVMLGIIMVEMYPVMFKQKMAV
Protein: Probable D-lactate dehydrogenase, mitochondrial (DLD) (Lactate dehydrogenase D) (EC 1.1.2.4) (Q7TNG8)
Organism: Mus musculus (Mouse)
Function: Involved in D-lactate, but not L-lactate catabolic process.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12127981}.
Interaction partners:
- L-lactate dehydrogenase C chain
- L-lactate dehydrogenase
- L-lactate dehydrogenase B chain
- L-lactate dehydrogenase A chain
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- NADP-dependent malic enzyme
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Pyruvate kinase PKM
- NADP-dependent malic enzyme, mitochondrial
- Pyruvate carboxylase, mitochondrial
Sequence:
MAMLLRVATQRLSPWRSFCSRGSQGGLSQDFVEALKAVVGSPHVSTASAVREQHGHDESMHRCQPPDAVVWPQNVDQVSRVASLCYNQGVPIIPFGTGTGVEGGVCAVQGGVCINLTHMDQITELNTEDFSVVVEPGVTRKALNTHLRDSGLWFPVDPGADASLCGMAATGASGTNAVRYGTMRDNVINLEVVLPDGRLLHTAGRGRHYRKSAAGYNLTGLFVGSEGTLGIITSTTLRLHPAPEATVAATCAFPSVQAAVDSTVQILQAAVPVARIEFLDDVMMDACNRHSKLNCPVAPTLFLEFHGSQQTLAEQLQRTEAITQDNGGSHFSWAKEAEKRNELWAARHNAWYAALALSPGSKAYSTDVCVPISRLPEILVETKEEIKASKLTGAIVGHVGDGNFHCILLVDPDDAEEQRRVKAFAENLGRRALALGGTCTGEHGIGLGKRQLLQEEVGPVGVETMRQLKNTLDPRGLMNPGKVL
Protein: SRCR domain-containing protein (Q8BIC8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRTTLWPLSLGSLLTLGAALTGTSSEGDQGNLRLAHRQSTCDGVVLVRHQGEWGHLCNLEWTLAEASVVCRQLGCGPAVGAPKYVPLPGEMVRPWLHNVSCWGNESSLWECSLGAWSQRACPHEWVVVALCANGTFREIRLVKGHSPCAGLPEIMNVNGVDRLCGLHVEEATVFCRELQCGHALQAPRQDVGVSKYMTCKGTESTIRNCRLNNKLRGGCNLLLDAEVICSGHVEARLVGGEHSCAGRLEVLRGLTWGTICHADLDLPTAHVVCRELGCGIAVSTLGGAQFGQGSGPVWLEAFRCVGNESLLFHCPREPGHHCGHEQDAALTCSEFRLVNGSSDCEGRVELQVQGTWAPVCAANWDLADAMVLCHQLNCGNAVSVPPGGHFGDGDDLIWPDIFHCVGTEPHLLHCAASTLGAHGCVLGNTASTICSGLQDILRLRDGQSYCDGCVEISLDGSWGRVLDDAWDLHGASVVCRQLGCGEAQRAYDAPAPIFRRVPVGLSQVRCLGSETRLVHCNVSTSLLVPAGTLRDAGVVCSGSLRVRLAAGPGRCAGRVELFYQGSWGTVCDDAWDLQDAQVVCRQLDCGHALSAPRNAHFGAGTGHIWMDELHCLGNESSLWKCQSGSWGQHDCRHKEDAGVFCSESVALRLRGGTSGCVGWLDVLYNGSWGAVCSNALRDISLSIICRQLGCGDQGWLENRPSSGAGLGISWVDNIKCRNLHNATLWQCPSAPWNPHSCTQEEEVWINCEGTPQIALQDPAQTPNCSSPFGCLENSVLRVLGGEDGCSGRVELWHAGSWGTVCDDSWDLVDAEVVCRQLGRGQALAALGEASFGPGVGPVWLDEVECLGSEVTLEACQAEPWGHGDCTHKEDAGVRCAVKAQPSLCPTAPSLTPPSVAEVWKLSEIACLVLGCLLGIVFLVMIAQWCHIRDASMGAGMLGHLQSEGIYEDIEVDPVPKKEENTVSRLLMLEEGYNDAEEPEDQPTENDE
Protein: GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (Protein FX) (Red cell NADP(H)-binding protein) (Transplantation antigen P35B) (Tum-P35B antigen) (P23591)
Organism: Mus musculus (Mouse)
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Interaction partners:
- GDP-mannose 4,6 dehydratase
- Fucose-1-phosphate guanylyltransferase
- Ubiquitin-conjugating enzyme E2 L3
- Ubiquitin-like protein FUBI
- L-fucose kinase
Sequence:
MGEPHGSMRILVTGGSGLVGRAIQKVVADGAGLPGEEWVFVSSKDADLTDAAQTQALFQKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHINDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHSSNFGYSYAKRMIDVQNRAYFQQHGCTFTAVIPTNVFGPYDNFNIEDGHVLPGLIHKVHLAKSSDSALTVWGTGKPRRQFIYSLDLARLFIWVLREYSEVEPIILSVGEEDEVSIKEAAEAVVEAMDFNGEVTFDSTKSDGQYKKTASNGKLRSYLPDFRFTPFKQAVKETCTWFTDNYEQARK
Protein: Mannose-1-phosphate guanylyltransferase 1 (EC 2.7.7.13) (GDP-mannose pyrophosphorylase 1) (Protein CYTOKINESIS DEFECTIVE 1) (Protein EMBRYO DEFECTIVE 101) (Protein HYPERSENSITIVE TO AMMONIUM ION 1) (Protein SENSITIVE TO OZONE 1) (Protein VITAMIN C DEFECTIVE 1) (O22287)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein during embryogenesis. Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Plays an essential role in plant growth and development and cell-wall architecture. Provides GDP-mannose, used for cell wall carbohydrate biosynthesis, protein N-glycosylation, as well as for the biosynthesis of the antioxidant ascorbate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23424245}. Nucleus {ECO:0000269|PubMed:23424245}.
Interaction partners:
- ADP-glucose pyrophosphorylase family protein
- ADP-glucose pyrophosphorylase family protein
- Phosphomannomutase
- GDP-mannose 3,5-epimerase
- GDP-mannose 4,6 dehydratase 1
- GDP-mannose 4,6 dehydratase 2
- Dolichol-phosphate mannosyltransferase subunit 1
- GDP-L-galactose phosphorylase 1
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 5a
Sequence:
MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQETEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKKSPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM
Protein: Chitin synthase regulatory factor 2 (Chs four homolog 2) (O94486)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in chitin biosynthesis.
Subcellular location: Membrane {ECO:0000269|PubMed:14655046}; Lipid-anchor {ECO:0000269|PubMed:14655046}.
Interaction partners:
- Chitin synthase regulatory factor 1
Sequence:
MLVSNGGTGSAHEWDRTTIDYDIEPSSDTHAIEISSNDDYLHPLAQFKKSEEFDEVPTNTLIHEVPSFSDSASNIQSQRNLSPFKELEIVSKKKSEQTFSSAVDFSAINVKNLNLKSGLFDPEPPSYDPDYAFNQRSLQSDPGSDEMFRNFKKSISLEELKSSYKLASAEMCEPETRLSFLQLALQAEKSSSRRNREYVARKKEEAFDYLTSFVSQGNSFFGYSEALYLLAVCYGTGALRTEINEKEAYRLYKMAADLNHVQAAYRVAICLQMGFGVTQNTEEAIHYFFRAASGQHVGAMHRMALIYFRGLMSVKRDPVKAMYYLNLGALEADHEFPQALYDLAELYEHGSSYLDGLLELSPRKAFVLYHIAAKYGLKDAQLRVARCFELGQLECDINLVRSFVWYRRLARKRNPEAMWKLSQFYLNGVDDVIYPNPELANEWAKAAAYKNHHLASTFVQDVGKEDVFEKTSITISNEERKSRNSESLPKKKKRLSMLSFKRSKNRESCIIS
Protein: V-set and transmembrane domain-containing protein 5 (Q9D806)
Organism: Mus musculus (Mouse)
Function: Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27683913}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:27683913}. Cell projection, axon {ECO:0000269|PubMed:27683913}.
Interaction partners:
- Single-pass membrane and coiled-coil domain-containing protein 4
Sequence:
MRPLRCGERTQGIPLGLLAFWVTAARCLQSQGVSLYIPQSAINATVQQDILLSVDYICHGVPTIEWKYTPNWGVQRIVEWKPGTPANVSQSHRDRVCTFDNGSIQLFNVSVKDSGYYIVTVTEHPGSSQSGTILLRVSEIRYEDLHFVAVFFALLAAVAVVLISLMWVCNQCAYKFQRKRRYKLKESTTEEIEMKEVEC
Protein: Pregnancy-specific beta-1-glycoprotein 6 (PS-beta-G-6) (PSBG-6) (Pregnancy-specific glycoprotein 6) (Pregnancy-specific beta-1-glycoprotein 10) (PS-beta-G-10) (PSBG-10) (Pregnancy-specific glycoprotein 10) (Pregnancy-specific beta-1-glycoprotein 12) (PS-beta-G-12) (PSBG-12) (Pregnancy-specific glycoprotein 12) (Q00889)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pregnancy-specific beta-1-glycoprotein 1
- Pregnancy-specific beta-1-glycoprotein 3
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 2
- Pregnancy-specific beta-1-glycoprotein 9
- Pregnancy specific beta-1-glycoprotein 7
- Pregnancy-specific beta-1-glycoprotein 4
- Pregnancy-specific beta-1-glycoprotein 5
- Pregnancy-specific beta-1-glycoprotein 2
Sequence:
MGPLSAPPCTQHITWKGLLLTASLLNFWNLPTTAQVIIEAKPPKVSEGKDVLLLVHNLPQNLTGYIWYKGQMTDLYHYITSYVVHGQIIYGPAYSGRETVYSNASLLIQNVTQEDAGSYTLHIIKRGDGTGGVTGYFTVTLYSETPKPSISSSNLNPREVMEAVRLICDPETPDASYLWLLNGQNLPMTHRLQLSKTNRTLYLFGVTKYIAGPYECEIRNPVSASRSDPVTLNLLPKLPMPYITINNLNPREKKDVLAFTCEPKSRNYTYIWWLNGQSLPVSPRVKRPIENRILILPSVTRNETGPYQCEIRDRYGGIRSNPVTLNVLYGPDLPRIYPSFTYYRSGENLDLSCFADSNPPAEYSWTINGKFQLSGQKLFIPQITTNHSGLYACSVRNSATGKEISKSMIVKVSETASPQVTYAGPNTWFQEILLL
Protein: Dynein regulatory complex subunit 3 (Leucine-rich repeat-containing protein 48) (Q9H069)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:23354437}. Cell projection, cilium {ECO:0000269|PubMed:27120127}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8IVX2}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9D5E4}.
Interaction partners:
- Radial spoke head protein 4 homolog A
- Coiled-coil domain-containing protein 40
- Dynein regulatory complex subunit 4
- Dynein regulatory complex subunit 2
- Radial spoke head protein 6 homolog A
- Dynein regulatory complex subunit 5
- F-box and leucine-rich repeat protein 13
- Outer dynein arm-docking complex subunit 1
- Dynein regulatory complex subunit 7
- Dynein regulatory complex protein 1
Sequence:
MNQPCNSMEPRVMDDDMLKLAVGDQGPQEEAGQLAKQEGILFKDVLSLQLDFRNILRIDNLWQFENLRKLQLDNNIIEKIEGLENLAHLVWLDLSFNNIETIEGLDTLVNLEDLSLFNNRISKIDSLDALVKLQVLSLGNNRIDNMMNIIYLRRFKCLRTLSLSRNPISEAEDYKMFICAYLPDLMYLDYRRIDDHTKKLAEAKHQYSIDELKHQENLMQAQLEDEQAQREELEKHKTAFVEHLNGSFLFDSMYAEDSEGNNLSYLPGVGELLETYKDKFVIICVNIFEYGLKQQEKRKTELDTFSECVREAIQENQEQGKRKIAKFEEKHLSSLSAIREELELPNIEKMILECSADISELFDALMTLEMQLVEQLEETINMFERNIVDMVGLFIENVQSLMAQCRDLENHHHEKLLEISISTLEKIVEGDLDEDLPNDLRALFVDKDTIVNAVGASHDIHLLKIDNREDELVTRINSWCTRLIDRIHKDEIMRNRKRVKEINQYIDHMQSELDNLECGDILD
Protein: Protein BUD31 homolog (Protein EDG-2) (Protein G10 homolog) (P41223)
Organism: Homo sapiens (Human)
Function: Involved in the pre-mRNA splicing process. May play a role as regulator of AR transcriptional activity; may increase AR transcriptional activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:25091737, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. Note=Detected in chromatin at the promoter of AR target genes. {ECO:0000305|PubMed:25091737}.
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing-splicing factor 8
- Crooked neck-like protein 1
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein G
- Pleiotropic regulator 1
- Pre-mRNA-processing factor 19
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-processing factor 17
Sequence:
MPKVKRSRKAPPDGWELIEPTLDELDQKMREAETEPHEGKRKVESLWPIFRIHHQKTRYIFDLFYKRKAISRELYEYCIKEGYADKNLIAKWKKQGYENLCCLRCIQTRDTNFGTNCICRVPKSKLEVGRIIECTHCGCRGCSG
Protein: L-serine deaminase (L-threonine dehydratase) (Q9VHF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dorsal interacting protein 4
- IP10578p
- Phosphoserine phosphatase
- Serine hydroxymethyltransferase
- LD34157p
- Alanine--glyoxylate aminotransferase
- Cystathionine beta-synthase
- Branched-chain-amino-acid aminotransferase
- L-threonine 3-dehydrogenase, mitochondrial
- cystathionine gamma-lyase
Sequence:
MSQAVKTETPKEPNVVAAKANGGTAVNGKLEAQKRPRHVSGGVEEIIDPFCNPEKPQRISFHDVTSAAFLIRGGVERTPCPKSTSSDLYGMELYLKKDFLQYTGSFKERGARYALLSLTEEQKRTGVISASLGNHAQALCYHGWKLNIPVTVVMPKAAPIMKIQKCRNYKARVIVDGNDMGEAKSLAMRMSREEGLLYVNGYDHPHIMAGQGTIGLEILEQVPEPDAVVVPVGGGGLIAGIATAVKALSPKTKIIGVESEKCASFTRAMENDGPIHTPIKNTLADGLAVPKVGYNAYATAMPLIDRMVVVKEEWIAVAILRLVEEEKCVVEGAGGAGLAAILAGHLDELKGKKVVVLLCGGNIDTTVFGRCLERGLAAVGRLVKFNVEVSDRPGGINDLCALLVRVGVSIKDIMHERAWLRDVYTVEVKVVCETVDWTHSLQLKNELKKFYSKVQFSDVPLALSNDTDS