wanglab/gogpt-training-data huggingface dataset:
Protein: Probable polyamine transporter At1g31820 (Q9C6S4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cell membrane polyamine/proton symporter involved in the polyamine uptake in cells.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- WAT1-related protein At3g28100
- Cationic amino acid transporter 7
- WAT1-related protein At3g28070
- WAT1-related protein At4g15540
- WAT1-related protein At3g28130
- Cationic amino acid transporter 4
- WAT1-related protein At3g28050
- WAT1-related protein At3g28080
- Cationic amino acid transporter 9
- Cationic amino acid transporter 2
Sequence:
MGDYNMNEFAYGNLYDDDDGDVGGSSKEGNNSIQKVSMLPLVFLIFYEVSGGPFGAEGSVNAAGPLLALLGFVIFPFIWCIPEALITAEMSTMFPINGGFVVWVSSALGTFWGFQVGWMKWLCGVIDNALYPVLFLDYLKSAVPALATGLPRVASILILTLLLTYLNYRGLTIVGWTAVFMGVFSMLPFAVMSLVSIPQLEPSRWLVMDLGNVNWNLYLNTLLWNLNYWDSVSTLAGEVANPKKTLPKALCYGVIFVALSNFLPLLSGTGAIPLDRELWTDGYLAEVAKAIGGGWLQLWVQAAAATSNMGMFLAEMSSDSFQLLGMAELGILPEIFAQRSRYGTPLLGILFSASGVLLLSGLSFQEIIAAENLLYCGGMILEFIAFVRLRKKHPAASRPYKIPVGTVGSILICVPPIVLICLVIVLSTIKVALVSFVMVVIGFLMKPCLNHMDGKKWVKFSVCSDLAEFQKENLDCEESLLR
Protein: Chitin-binding type-2 domain-containing protein (Q9XUB6)
Organism: Caenorhabditis elegans
Interaction partners:
- Activated in Blocked Unfolded protein response
- Prion-like-
- Activated in Blocked Unfolded protein response
- Nematode cuticle collagen N-terminal domain-containing protein
- MATH domain-containing protein
- Chitin-binding type-2 domain-containing protein
- Prion-like-
- Zinc metalloproteinase nas-30
- Activated in Blocked Unfolded protein response
- Activated in Blocked Unfolded protein response
Sequence:
MARFLLIIGCATLAALASCESKSGEETPQYWRAILGDICQLPSFPRATGDPTRYVECVRQSSFAADRKDLGIWLLRECLPGYEFVASARRCKTVRSVNKQQELCESANATEYNFCPTASAMQFLVEETREAPRQCACPNGEQNCVCPSPEILEPISAVKKVRRSAQQQPLRFSQYPSCPCPQNQPACTCSTNNQQNEQILVSISCCQQQETTTQAPVQMQPCQCTPTQIQQNCQTTTTQQQYCPQQSAPVVQPQPCPLVQGSGVQNAQYQGICSWMIDPLATDPQSRTHYLQCQPAPNNLFCGRWQRMPCAPGTVFDVQSQVCVWDTNSQPGTLPTPAPYVSTQAPQNAQCGCTGGVQIGSCNQNYQCPGQSVCQVGQNAGQQCMVCCYFRKKARRF
Protein: Syncrip, isoform J (A0A0B4KHT5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein gurken
Sequence:
MLSQMEASKVQKDEGGGEALSRTILKTPSSFRTPSPIPSCSKMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLNDFEIRTGKKIGVTISFNNHRLFVGNIPKNRDRDELIEEFSKHAPGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGFETLSPYRNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPVVGKRKFDGGHQNPADVKRRYPSGLIGNGGSWGSLPLPQQPLGTNGEQWYMDTFSAWS
Protein: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.9) (MVLCAD) (VLCAD) (P50544)
Organism: Mus musculus (Mouse)
Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P49748}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49748}.
Interaction partners:
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal bifunctional enzyme
- 3-ketoacyl-CoA thiolase A, peroxisomal
- 3-ketoacyl-CoA thiolase B, peroxisomal
Sequence:
MQSARMTPSVGRQLLRLGARSSRSTTVLQGQPRPISAQRLYAREATQAVLDKPETLSSDASTREKPARAESKSFAVGMFKGQLTIDQVFPYPSVLSEEQAQFLKELVGPVARFFEEVNDPAKNDALEKVEDDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQREKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAIPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPSENVLGEVGDGFKVAVNILNNGRFGMAATLAGTMKSLIAKAVDHATNRTQFGDKIHNFGVIQEKLARMAILQYVTESMAYMLSANMDQGFKDFQIEAAISKIFCSEAAWKVADECIQIMGGMGFMKEPGVERVLRDIRIFRIFEGANDILRLFVALQGCMDKGKELTGLGNALKNPFGNVGLLMGEAGKQLRRRTGIGSGLSLSGIVHPELSRSGELAVQALDQFATVVEAKLVKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGYPTAQHEKMLCDSWCIEAATRIRENMASLQSSPQHQELFRNFRSISKAMVENGGLVTGNPLGI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5M813)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPQAAYCYLRVVGRGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGDLYRKLKEQKGQLLPESQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHSDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPKVYSAELAELIRTMLSRRPEERPSVRSILRQPYIKHHISLFLEATKALHGAEEMAQQLRALTSLPEVLSSTPSNHMVAHNHL
Protein: AT10048p (Uncharacterized protein, isoform B) (Q8INM2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO12034p1
- AT25643p
- IP03738p
- Uncharacterized protein
- Uncharacterized protein, isoform A
- Uncharacterized protein
- Uncharacterized protein
- CG32712
- GEO10781p1
- Uncharacterized protein, isoform E
Sequence:
MVVTRSAATKKQNQVLTLSDQNILAESSRTKGPPVPKKNVKKLPTARQCVKVAANLLDAQEPNENENTGTQRKDGKQLDSKLSSTVQNTEAARSKETPAPKKNVKKLQAALPCADAAANLLEEQASNEMNEEGPPVPKKNVKKLPAARQCVKVAANLLDAQESIENEKTGTKRKDGKQLQAQNSNENEKTSTLKKDKKLLASKTPEAATNDNANPNMKPSLKKSTREHKSKKCNDIQKAGKDHIEHQAE
Protein: Probable ferredoxin/ferredoxin--NADP reductase (FNR) (EC 1.18.1.2) (P9WJI1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Glutamate synthase large chain
- Possible oxygenase
- Uncharacterized protein Rv0885
- NADPH-ferredoxin reductase FprA
- 2-oxoglutarate oxidoreductase subunit KorA
- Possible electron transfer protein FdxB
- NADPH oxidoreductase
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- Probable oxidoreductase
- Malate dehydrogenase
Sequence:
MPHVITQSCCNDASCVFACPVNCIHPTPDEPGFATSEMLYIDPVACVDCGACVTACPVSAIAPNTRLDFEQLPFVEINASYYPKRPAGVKLAPTSKLAPVTPAAEVRVRRQPLTVAVVGSGPAAMYAADELLVQQGVQVNVFEKLPTPYGLVRSGVAPDHQNTKRVTRLFDRIAGHRRFRFYLNVEIGKHLGHAELLAHHHAVLYAVGAPDDRRLTIDGMGLPGTGTATELVAWLNGHPDFNDLPVDLSHERVVIIGNGNVALDVARVLAADPHELAATDIADHALSALRNSAVREVVVAARRGPAHSAFTLPELIGLTAGADVVLDPGDHQRVLDDLAIVADPLTRNKLEILSTLGDGSAPARRVGRPRIRLAYRLTPRRVLGQRRAGGVQFSVTGTDELRQLDAGLVLTSIGYRGKPIPDLPFDEQAALVPNDGGRVIDPGTGEPVPGAYVAGWIKRGPTGFIGTNKSCSMQTVQALVADFNDGRLTDPVATPTALDQLVQARQPQAIGCAGWRAIDAAEIARGSADGRVRNKFTDVAEMLAAATSAPKEPLRRRVLARLRDLGQPIVLTVPL
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Q4Q127)
Organism: Leishmania major
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03008}.
Interaction partners:
- Putative eukaryotic translation initiation factor 3 subunit 8
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Translation initiation factor-like protein
- Eukaryotic translation initiation factor 3 subunit E
- RRM domain-containing protein
- Uncharacterized protein
- CSN8/PSMD8/EIF3K domain-containing protein
- Putative eukaryotic translation initiation factor 5
- Putative translation initiation factor
- Putative elongation initiation factor 2 alpha subunit
Sequence:
MMGPRSRLQPGPSAAVSPLLNTPSPFFFWCLLLSHLASLLAAFLTETKKSKTQLIFVSRTSATMTAAVDLEGVALHGHMKGVTMLKFNRDGDLLFSSAKDTNCSACCWQVKTGKLFGSYTTVGQVEGRTYDAAMVALDVNRESTLLATASAGEEVLLWSVESGALLGSVSRSLSSGASVGFSHDDTLMMVATKGRSSTNSAIQVYNVPFTVPKAGEDIAPVKTPFTTFSTFETPDTITWAAWGPTNETIYYSEGGYMNILDVEANKVIRSRQIHEDENEVINRFSWDPNYLALATASTDKTSHLIDFRDLATIQVYRSDVPVNDVSISPNADHVILGGGMDAASVTTQGGQSIFEVKFFHKVHGHQLGQLRCHFGTINAMSFHPDGRGFASASYDGLIKMYRFGDSYDSTPGAQPLWTL
Protein: Bifunctional aspartokinase/homoserine dehydrogenase 2 (Aspartokinase II/homoserine dehydrogenase II) (AKII-HDII) [Includes: Aspartokinase (EC 2.7.2.4); Homoserine dehydrogenase (EC 1.1.1.3)] (P00562)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Cystathionine gamma-synthase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Homoserine kinase
- Aspartate-semialdehyde dehydrogenase
- Threonine synthase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Homoserine O-succinyltransferase
- 5,10-methylenetetrahydrofolate reductase
- Lysine-sensitive aspartokinase 3
- Met repressor
Sequence:
MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMAEYSQPDDMMVVSAAGSTTNQLINWLKLSQTDRLSAHQVQQTLRRYQCDLISGLLPAEEADSLISAFVSDLERLAALLDSGINDAVYAEVVGHGEVWSARLMSAVLNQQGLPAAWLDAREFLRAERAAQPQVDEGLSYPLLQQLLVQHPGKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSEIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLIEFQVPASQDFKLAHKEIDQILKRAQVRPLAVGVHNDRQLLQFCYTSEVADSALKILDEAGLPGELRLRQGLALVAMVGAGVTRNPLHCHRFWQQLKGQPVEFTWQSDDGISLVAVLRTGPTESLIQGLHQSVFRAEKRIGLVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLAGVVDSRRSLLSYDGLDASRALAFFNDEAVEQDEESLFLWMRAHPYDDLVVLDVTASQQLADQYLDFASHGFHVISANKLAGASDSNKYRQIHDAFEKTGRHWLYNATVGAGLPINHTVRDLIDSGDTILSISGIFSGTLSWLFLQFDGSVPFTELVDQAWQQGLTEPDPRDDLSGKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEGGSIDHFFENGDELNEQMVQRLEAAREMGLVLRYVARFDANGKARVGVEAVREDHPLASLLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDINRLAQLL
Protein: RNA binding protein with serine rich domain 1 (H3BTR6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPS
Protein: Slc39a1 protein (Solute carrier family 39 member 1) (B5DEF5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable proton-coupled zinc antiporter SLC30A4
- Proton-coupled zinc antiporter SLC30A1
Sequence:
MGPWGEPELLVWRPEAIASEPSVPVGLEVKLGALVLLLLLTLICSLVPVCVLRRSGANHEASASGQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALEALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQSSPPHPEETRALLGTVNGGPQHWHDGPGIPQASGTPAAPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRAQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELATSEQRILKVILLLAGFALLTGLLFVQV
Protein: Cytochrome P450 709B2 (EC 1.14.-.-) (F4IK45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in stress response (By similarity). Does not function as cytokinin hydroxylase in yeast heterologous system (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- 11-beta-hydroxysteroid dehydrogenase-like 2
- Protein BRI1-5 ENHANCED 1
- Nucleotide binding protein
- UDP-glycosyltransferase 73D1
- rRNA biogenesis protein RRP36
- At1g19540
Sequence:
MLFCSVRILFIISSKQLVLISETEVTTTLTLHTTHKIESPTANPPQSKKNLFVIRMELLSTINLLAIALVLLVVPKIYGACRILVWRPWMLSRRFKKQGISGPKYRILYGNLREIRKMKNEAKLMVLDPNSNDIVPRVLPHLQQWKSQYGETFLYWQGTDPRLCISDHELAKQILSNKFVFFSKSKTKPEILKLSGNGLIFVNGLDWVRHRRILNPAFSMDKLKLMTQLMVDCTFRMFLEWKKQRNGVETEQFVLISREFKRLTADIIATAAFGSSYAEGIEVFKSQLELQKCCAAALTDLYFPGIQYLPTPSNLQIWKLDMKVNSSIKRIIDARLTSESKDYGNDLLGIMLTAASSNESEKKMSIDEIIEECKTFFFAGHETTANLLTWSTMLLSLHQDWQEKLREEVFNECGKDKIPDAETCSKLKLMNTVFMESLRLYGPVLNLLRLASEDMKLGNLEIPKGTTIILPIAKMHRDKAVWGSDADKFNPMRFANGLSRAANHPNALLAFSMGPRACIGQNFAIMEAKTVLAMILQRFRLNLSADYKHAPADHLTLQPQYDLPVILEPIDG
Protein: Pre-mRNA-splicing factor CWC25 homolog (Sex determining protein MOG-3) (G5EBT5)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-1
- Splicing factor YJU2
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor CWC22 homolog
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Protein BUD31 homolog
- Pre-mRNA-splicing factor syf-2
- Pre-mRNA-processing factor 19
- Probable U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 17
Sequence:
MSKDVSIGWMYEGAKGNVHREDYLLGKKVDKNFEKYSDVVNAQKAEAIDSIVGTRAVFNSGQSTGLKTSSLQKDIIKSEDPFVAVKVREETKRREIMDNPLTKMRLQAALKSMMTSKAEKSKEKKSKKDKKKKKKKRSSSSSDESSDERVERKRRRSPSPKRRRRPSEKPRKRSRSPRRERPRSPKRSREESRKLSRKPSSSRSKSPRRSREDPRKVARKPSRSRSRSAERLRRKSRSPRRSREEPRKMSRSRSRSADKASSSRQFDSHIPRHLQQQRSRHDSSSGSESEHETRSSHRRRNSDDDERQDPRKKSYGLVEMRKRTAEEREEESRAPTKEYKLVKIPTGRGTGNTPREPRRALSEAEKAARLAEMQQDNVKWRDEIRERNVTKGRKEDDEEKEEADKNGYAPSFIRSQMREACDDMTVEKRLQSNKRGVQRAHGYMDRSFAKK
Protein: Alpha-glucan phosphorylase 2, cytosolic (AtPHS2) (EC 2.4.1.1) (Alpha-glucan phosphorylase, H isozyme) (Starch phosphorylase H) (Q9SD76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Isoamylase 3, chloroplastic
- Phosphoglucomutase, chloroplastic
- Isoamylase 2, chloroplastic
- Probable phosphoglucomutase, cytoplasmic 2
- Probable phosphoglucomutase, cytoplasmic 1
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
- Isoamylase 1, chloroplastic
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
Sequence:
MANANGKAATSLPEKISAKANPEADDATEIAGNIVYHAKYSPHFSPLKFGPEQALYATAESLRDRLIQLWNETYVHFNKVDPKQTYYLSMEYLQGRALTNAIGNLNLQGPYADALRTLGYELEEIAEQEKDAALGNGGLGRLASCFLDSMATLNLPAWGYGLRYRHGLFKQIITKKGQEEIPEDWLEKFSPWEIVRHDVVFPVRFFGKVQVNPDGSRKWVDGDVVQALAYDVPIPGYGTKNTISLRLWEAKARAEDLDLFQFNEGEYELAAQLHSRAQQICTVLYPGDATENGKLLRLKQQFFLCSASLQDIISRFHERSTTEGSRKWSEFPSKVAVQMNDTHPTLAIPELMRLLMDDNGLGWDEAWDVTSKTVAYTNHTVLPEALEKWSQSLMWKLLPRHMEIIEEIDKRFVQTIRDTRVDLEDKISSLSILDNNPQKPVVRMANLCVVSSHTVNGVAQLHSDILKAELFADYVSIWPNKFQNKTNGITPRRWLRFCSPELSDIITKWLKTDKWITDLDLLTGLRQFADNEELQSEWASAKTANKKRLAQYIERVTGVSIDPTSLFDIQVKRIHEYKRQLMNILGVVYRFKKLKEMKPEERKKTVPRTVMIGGKAFATYTNAKRIVKLVNDVGDVVNSDPEVNEYLKVVFVPNYNVTVAEMLIPGSELSQHISTAGMEASGTSNMKFALNGCLIIGTLDGANVEIREEVGEENFFLFGATADQVPRLRKEREDGLFKPDPRFEEAKQFVKSGVFGSYDYGPLLDSLEGNTGFGRGDYFLVGYDFPSYMDAQAKVDEAYKDRKGWLKMSILSTAGSGKFSSDRTIAQYAKEIWNIEACPVP
Protein: Protocadherin gamma (Q8K497)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
VLLALKLRRWHSLRLLQAASGLAGVPPSHFVGVDGMRAFLQTYSHEVSLTADSRKSHLIFPQPNYADTLISQESCGKSEPLLITEDSTTVLGKCEPTDIQPRQPNPDWRYSASLRAGMHSSVHLEEAGI
Protein: Uncharacterized protein YDR524C-B (Q3E6R4)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Uncharacterized endoplasmic reticulum membrane protein YMR122W-A
- Protein HOR7
- Uncharacterized protein YCL048W-A
Sequence:
MQFKTIVAAFATVAAVQAANVSTNGSNRTNGSNTTSTKISTGAAASNALGAGVFGAAVAAGVAFLF
Protein: Periplasmic chaperone PpiD (Periplasmic folding chaperone) (P0ADY1)
Organism: Escherichia coli (strain K12)
Function: Chaperone that functions as a gatekeeper on the periplasmic side of the SecYEG translocon. Facilitates the translocation of precursor proteins across SecYEG by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the periplasmic exit site of the Sec translocon. May be involved in the early periplasmic folding of many newly translocated proteins. Acts as a transient subunit of the Sec translocon that binds to the lateral gate of SecY and is detached by nascent membrane proteins but not by SecA.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}; Single-pass type II membrane protein {ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}; Periplasmic side {ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}. Note=Located at the lateral gate of SecY. {ECO:0000269|PubMed:24951590}.
Interaction partners:
- Ancillary SecYEG translocon subunit
- Outer membrane protein assembly factor BamA
- Chaperone protein Skp
- FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
- Membrane protein insertase YidC
- Protein translocase subunit SecY
- Trigger factor
- Outer membrane protein assembly factor BamB
- Periplasmic serine endoprotease DegP
- Protein translocase subunit SecA
Sequence:
MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLIGGGNNYAAKVNDQEISRGQFENAFNSERNRMQQQLGDQYSELAANEGYMKTLRQQVLNRLIDEALLDQYARELKLGISDEQVKQAIFATPAFQVDGKFDNSRYNGILNQMGMTADQYAQALRNQLTTQQLINGVAGTDFMLKGETDELAALVAQQRVVREATIDVNALAAKQPVTEQEIASYYEQNKNNFMTPEQFRVSYIKLDAATMQQPVSDADIQSYYDQHQDQFTQPQRTRYSIIQTKTEDEAKAVLDELNKGGDFAALAKEKSADIISARNGGDMGWLEDATIPDELKNAGLKEKGQLSGVIKSSVGFLIVRLDDIQPAKVKSLDEVRDDIAAKVKHEKALDAYYALQQKVSDAASNDTESLAGAEQAAGVKATQTGWFSKDNLPEELNFKPVADAIFNGGLVGENGAPGINSDIITVDGDRAFVLRISEHKPEAVKPLADVQEQVKALVQHNKAEQQAKVDAEKLLVDLKAGKGAEAMQAAGLKFGEPKTLSRSGRDPISQAAFALPLPAKDKPSYGMATDMQGNVVLLALDEVKQGSMPEDQKKAMVQGITQNNAQIVFEALMSNLRKEAKIKIGDALEQQ
Protein: Stathmin, isoform D (M9NEA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tubulin beta chain
Sequence:
MGCNFSALPTKCKGCGQIRADFDRRYGCSECGSEVMYCGQCFDEGRNQHTETHKDDRRIKIIYHRSFLDKFFSGEKLLNGDASKSYNCVFCKKRFSAEELQLHLSEMHSNPADASALTVMLERMRQEDLENRIATEIRCQEKSRGGLSYEVILAEPAPNVAVPKRPVTPGKNVSVEEIEQKLKAAEERRISLEAKKMADISTKLAKVEEATRKKDEITNEFITQTKEQLESKMELHVEKREAIISDMKEKLKIHAQDIEKTRETLEQQKANEQKAIEEKLKIAQSLRDENIKKMLDRLKEHNTIKIAEIKSQNDQLECQKIEEKARIYENKLFAAEQKREKELQKKIEKVQKLERRAELVRQNKAQAQDLDGQQSAIASSG
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 6 (H0Y922)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00034476}; Lipid-anchor {ECO:0000256|ARBA:ARBA00034476}.
Interaction partners:
Sequence:
XTLPRSGSSGGQQPSGMKEGVKRYEQEHAAIQDKLFQVAKREREAATKHSKASLPTGEGSISHEEQKSVRLARELESREAELRRRDTFYKEQLERIERKNAEMYKLSSEQFHEAASKMESTIKVEPVCSGLQAQILHCYRDRPHEVLLCSDLVKAYQRCVSAAHKG
Protein: Microsomal triglyceride transfer protein large subunit (A0A0R4IVV0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the transport of triglyceride between phospholipid surfaces. Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. Required for yolk lipid utilization and absorption of dietary lipids in larvae.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:17924655}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum. {ECO:0000269|PubMed:17924655}.
Interaction partners:
- Apolipoprotein Ba.
- Protein disulfide-isomerase
- Apolipoprotein Bb, tandem duplicate 2.
- Apolipoprotein Bb, tandem duplicate 1
- Apolipoprotein Eb
- Vitellogenin 6.
- Si:dkeyp-106c3.3.
- Si:dkeyp-106c3.1.
- Lysophosphatidylglycerol acyltransferase 1.
Sequence:
MMPVAGLLLCVTAVLCTSALGAGPRLDNGKLYRYSYSTEVGLNRPTGSPGGNVGFRISSDVDINLAWRNPEIQDEQLLQVKISNIQVESAGKHSRKNNIFHGSSAESILGKVRLEALQRPFLVLWKMGKIRSLYAQKAEPATVKNLKRGVASMLMMQLKSGKMSEADASGKCLVEYKVNKHQVIRTKHLETCKSQETGFTTHSPVLGISGKCAAETVITLENGIIKSADAKETHVLSINARHKAATKVLSRQSLTLKAIEAGPAEVAGKDVAGVVKALDDKFLSVGVIVEKTKPKCKGCPNLMETWKAVRSQLEPNSLSKAEAPRSFLTLVHSLRKSSKSEILTVLQNCSKTALPQLVDAVTSAQTPSSLSAILEFLDFSKKDGLILQERFLYACGFASHPTESMLQSLLEVSQGKIGSTEIKESVVIIMGALLRKLCLKGACDLPAVLKVKELLLAGPDSTQEESEVQMYLLALKNALLPEGIPVLAKYAESEVGAYSTIAITALQRYDPALITAEVKKALNRIYHQNQRIYEKNVRAAAADVIMSSNPSYMEVKNLLLSIGHLPHEMNKYMLSKIQDVLRFQMPAYKLVRQVMKDMISHNYDRFSKTGSSSAYSGFMAETVDVTCTYNLDILYSGSGVLRRSNMNIYGQSNNALLHGLQVTIEAQGLESLIAATPDEGEEELESFAGMSALLFDVQLRPVTFFKGYSDLMSKMFSMSGDPINVVKGLILLTDHSQVIPLQSGLRASAEFQAGLSIDISGGMEFSLWYRESKTSVNNRGALVIIGNMTVDTDFVSAGVEVGFETEATLDFITTVQFSEYPFLVCMQMDKTTFPFRETVSKQEKLPTGQMFSRKRSRDQVVPGSEFPLHQENSNMCKKVFEPAW
Protein: BBSome complex member BBS1 (Bardet-Biedl syndrome 1 protein homolog) (Q9NEZ7)
Organism: Caenorhabditis elegans
Function: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization. Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:15231740}.
Interaction partners:
- BBSome complex member bbs-7
- BBSome complex member bbs-4
- Protein pthb1 homolog
- BBSome complex member bbs-5
- BBSome complex member bbs-2
- Tetratricopeptide repeat protein 8
- BBSome-interacting protein 1
- WD repeat-containing protein dyf-2
- Intraflagellar transport protein 88 homolog
- Rab8
Sequence:
MAKPVNVNQSKWTVPVLLKECEIYCPSTCVAFGPILSDNDSKLIIAHGGHRGVNMKLKVFQQLEQLSESSLADMPTALVHFINDLSSIPSIAVAAGPSLLIYKNLKPFYKFTVPSSAINPTESEAWKAVVNKKINGDTLLTVLKRLEDDVAFSKLTPISQTYLRADKETQVVLVEHYGTKIANSATITCIAKLTKSTAEPLDILVIGTEHCEIFLIDSQAFTILETIKIGSVPVNICAYGTYDVDYRLFVQTRASLIFCMKRGEADYQPIVISQSMITSMVLVNKMIVYTTVENLIHFASFRGKKMNTVKCPSKIKMLEPFIYPLKQLAAVIAVFDKEIRMYNEHYLLDTVQYEKPLAWVKYGCYGREDSTLVVAFKDGSIAIQIFRRKANFDTKLDYNQVPQAHALKLQIPKKTKVFIDLTQREVQLGNRIHKVYQKNLFDVKYRLAASYLELTSSASATVSTTTVLPVEISVDIHGFGPTFRMTIHLLSSSKQNLYDMHLSIISDPELYDFDTPLIPVHLLASGQSYSFTTLLYCKDPEKAANCDVRALLVHAKRATPIVTAVIKMPFSEFPLD