wanglab/gogpt-training-data huggingface dataset:
Protein: Scavenger receptor class A member 5 (Scavenger receptor hlg) (Q6ZMJ2)
Organism: Homo sapiens (Human)
Function: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific cell types, suggesting the existence of cell type-specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways. Ferritin mediates iron uptake in capsule cells of the developing kidney. Preferentially binds ferritin light chain (FTL) compared to heavy chain (FTH1).
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03070}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_03070}.
Interaction partners:
- Ferritin light chain
- Ferritin heavy chain
Sequence:
MENKAMYLHTVSDCDTSSICEDSFDGRSLSKLNLCEDGPCHKRRASICCTQLGSLSALKHAVLGLYLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESFRDLQLRLLQAPLQADLTEQVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAVALLRDRTGQQSDTAQLELYQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLNHSLSYDVALHRTRLQDLRVLVSNASEDTRRLRLAHVGMELQLKQELAMLNAVTEDLRLKDWEHSIALRNISLAKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDRAGDASGVEAPMMIRLVNGSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRTARFGQGTGRIWMDDVACKGTEETIFRCSFSKWGVTNCGHAEDASVTCNRH
Protein: Stomatin-like protein 3 (SLP-3) (Stomatin-related olfactory protein) (Q6PE84)
Organism: Mus musculus (Mouse)
Function: Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12122055, ECO:0000269|PubMed:24662763}; Single-pass type III membrane protein {ECO:0000269|PubMed:12122055}. Note=Detected in lipid rafts, in apical dendrites and in olfactory cilia.
Interaction partners:
- Acid-sensing ion channel 3
- Acid-sensing ion channel 1
- Piezo-type mechanosensitive ion channel component 2
- Piezo-type mechanosensitive ion channel component 1
Sequence:
MDSPEKLEKNNLVGTNKSRLGVCGWILFFLSFLLMLVTFPISVWMCLKIIKEYERAVVFRLGRIQADKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLKSASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMNILEGIGGISYGNNKKVTAKA
Protein: Trafficking protein particle complex subunit 6A (TRAPP complex subunit 6A) (O75865)
Organism: Homo sapiens (Human)
Function: May play a role in vesicular transport during the biogenesis of melanosomes.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 12
Sequence:
MADTVLFEFLHTEMVAELWAHDPDPGPGGQKMSLSVLEGMGFRVGQALGERLPRETLAFREELDVLKFLCKDLWVAVFQKQMDSLRTNHQGTYVLQDNSFPLLLPMASGLQYLEEAPKFLAFTCGLLRGALYTLGIESVVTASVAALPVCKFQVVIPKS
Protein: Thioredoxin (Q4WV97)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Thioredoxin reductase
- Tryptophan synthase
- tryptophan synthase
- AhpC/TSA family protein
- peptide-methionine
Sequence:
MSHNVEKITDAKVFKEKVQEGSGPVIVDCSATWCGPCKAISPVFQRLSTSEEFKNAKFYEIDVDELSEVAAELGVRAMPTFMFFKDGQKVNEVVGANPPALEAAIKAHVA
Protein: LIM domain-containing protein (Q8INR0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPVQVQAANMSLGAMHCTRCADGFEPTEKIVNSNGELWHTQCFVCAQCFRPFQDGIFYEFEGRKYCERDFHVLFAPCCNKCGEFVIGRVIKAMSASWHPQCFRCQLCAKELADCGFIKNQNRALCHECNAKVKAEITGRYVCQKCHGLIDEEPLRFRGEVYHGYHFSCTACGTELDSTAREVKSRPGLAANDMNELYCLRCHDKMGIPICGACRRPIEERVVTALGKHWHVEHFVCAKCEKPFLGHRHYEKRGLAYCETHYHQLFGNLCFVCNQVIGGDVFTALNKAWCVHHFACSVCDTKMTQKSKFYEYDEKPVCKKCYDRFPNELRRRLRTAHEMTMKKNT
Protein: Auxin-responsive protein IAA15 (Indoleacetic acid-induced protein 15) (Q6AT10)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Auxin response factor 7
- Auxin response factor 1
- Auxin response factor 9
- Auxin response factor 14
- Auxin response factor 3
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 16
- Auxin response factor 2
- Auxin response factor 15
Sequence:
MSVETERSSTESSAASGLDFEDTALTLRLPGSSSSSSSSSSSSSSSSPSEPDRKRASATDDDPDNRLGSTATESPPSPKARVVGWPPVRAFRKNALAALAAASSSKAKFVKVAVDGAPYLRKVDLEAYRGYDQLLAALQDKFFSHFTIRKLGNEEMKLVDAVSGNEYVPTYEDKDGDWMLVGDVPWKMFVETCQRLRLMKSSEAVNLAPRSA
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (A0A060XK41)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Cardiolipin synthase
- Lysophospholipid acyltransferase 5
- Lysophospholipid acyltransferase 5
- Phospholipid/glycerol acyltransferase domain-containing protein
- Cholinephosphotransferase 1
- Cholinephosphotransferase 1
- Phospholipid/glycerol acyltransferase domain-containing protein
- Phospholipid/glycerol acyltransferase domain-containing protein
- Haloacid dehalogenase-like hydrolase domain-containing protein 3
- Phosphatidylethanolamine N-methyltransferase
Sequence:
MTVTVFPVRLFFAVFLMLLAWPFAFAASLGRSELAVETETWWRRICDIALRVIMRAMWFCGGFHWVTVKGEPAPPSQAPILTLAPHSSYFDAIPITMTMASIVMKTESKNIPVWGTLIKFIRPVFVSRSDQDSRRKTVEEIKRRAHAGGEWPQIMIFPEGTCTNRSCLITFKPGMCSSLC
Protein: Pentatricopeptide repeat-containing protein At3g26782, mitochondrial (Q9LW32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MKVRSKKALFCSVSRLLHTERHTERQNLTTLFNRYVDKTDVFSWNSVIADLARSGDSAEALLAFSSMRKLSLYPTRSSFPCAIKACSSLFDIFSGKQTHQQAFVFGYQSDIFVSSALIVMYSTCGKLEDARKVFDEIPKRNIVSWTSMIRGYDLNGNALDAVSLFKDLLVDENDDDDAMFLDSMGLVSVISACSRVPAKGLTESIHSFVIKRGFDRGVSVGNTLLDAYAKGGEGGVAVARKIFDQIVDKDRVSYNSIMSVYAQSGMSNEAFEVFRRLVKNKVVTFNAITLSTVLLAVSHSGALRIGKCIHDQVIRMGLEDDVIVGTSIIDMYCKCGRVETARKAFDRMKNKNVRSWTAMIAGYGMHGHAAKALELFPAMIDSGVRPNYITFVSVLAACSHAGLHVEGWRWFNAMKGRFGVEPGLEHYGCMVDLLGRAGFLQKAYDLIQRMKMKPDSIIWSSLLAACRIHKNVELAEISVARLFELDSSNCGYYMLLSHIYADAGRWKDVERVRMIMKNRGLVKPPGFSLLELNGEVHVFLIGDEEHPQREKIYEFLAELNRKLLEAGYVSNTSSVCHDVDEEEKEMTLRVHSEKLAIAFGIMNTVPGSTVNVVKNLRVCSDCHNVIKLISKIVDREFVVRDAKRFHHFKDGGCSCGDYW
Protein: Ribosomal protein L1p/L10e family (Q38CE8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPQDKRLIITRAVLHKVQRVCGSADAASAEGIFIEFVVPAVVVTQCPELTGKYVFQLPNRTYVMNGRTTCLIVPRLLSGGAFKVNKRHGYYDAVVTAEAICKRGDTEAARRAAQVAKTFAHFVVDSRIVSKLPSCITDGAVVTKVATMKVPSTVADEKSDRKNEQGRKGSQKPPDGAIVKGSQQYVETEKAPVGMPPLVKLSRKCITPLHNLDEQGNLTLRLAQGASGSVVRVRQAGQLVVRVGHGGMVPGEVCDNAKSFVYTLKREFPTVWKYIHEFQMTSAVTEPIRFMEVHIQK
Protein: Protein/nucleic acid deglycase 2 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) (P45470)
Organism: Escherichia coli (strain K12)
Function: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. In vitro, prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures at 55 degrees Celsius, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Is a general stress protein; is required for the protection of bacterial cells against many environmental stresses, including oxidative, thermal, osmotic, UV, and pH stresses. And plays an important role in protection against electrophile/carbonyl stress.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:16380269}.
Interaction partners:
- Protein/nucleic acid deglycase 3
- Protein/nucleic acid deglycase 1
- Uncharacterized oxidoreductase YghA
- Glyoxalase ElbB
- Catalase HPII
- Osmotically-inducible protein Y
- Uncharacterized protein YbgS
- Thiol peroxidase
Sequence:
MSKKIAVLITDEFEDSEFTSPADEFRKAGHEVITIEKQAGKTVKGKKGEASVTIDKSIDEVTPAEFDALLLPGGHSPDYLRGDNRFVTFTRDFVNSGKPVFAICHGPQLLISADVIRGRKLTAVKPIIIDVKNAGAEFYDQEVVVDKDQLVTSRTPDDLPAFNREALRLLGA
Protein: Growth hormone-releasing hormone receptor form a (P78470)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
CKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLF
Protein: Activating transcription factor 7 interacting protein (F5H8I0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSLEEPQKKVFKARKTMRVSDRQQLEAVYKVKEELLKTDVKLLNGNHENGDLDPTSPLENMDYIKDKEEVNGIEEICFDPEGSKAEWKETPCILSVNVKNKQDDDLNCEPLSPHNITPEPVSKLPAEPVSG
Protein: Alkaline phosphatase (APase) (EC 3.1.3.1) (P00634)
Organism: Escherichia coli (strain K12)
Subcellular location: Periplasm.
Interaction partners:
- Protein translocase subunit SecA
- Protein-export protein SecB
- Trigger factor
- Chaperone protein DnaK
- Dihydroneopterin triphosphate 2'-epimerase
- Phosphate regulon transcriptional regulatory protein PhoB
- Ornithine carbamoyltransferase subunit F
- Dihydroneopterin triphosphate diphosphatase
- Phosphate regulon sensor protein PhoR
- Phosphate-binding protein PstS
Sequence:
MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
Protein: Thioredoxin domain-containing protein plp1 (Phosducin-like protein 1) (O14095)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inhibits early G-protein signaling events following pheromone stimulation. May help create heterodimerizable beta-tubulin by facilitating the efficient transfer of nascent beta-tubulin polypeptides to the folding apparatus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosducin-like protein C2A9.09
- Queuine tRNA-ribosyltransferase catalytic subunit
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
Sequence:
MTSFPASHGFGPRKRGYQMDLTNVQPVENKPAWISMKSPLEKEIANEYEALKVTERKEDTQDYNEPELHNSNDPTVDLYADTYATQAATESDSELEDALFSQLDEFDDTAYREQRLEMLKKEFARVEAAKEKGHMQFLTVENEREVMDFTLSSKKVVIHFYHPDFIRCKIIDSHLEKIAKVHWETKFIRIEAANAPFLVVKLGLKVLPAVLCYVNSQLVDKIIGFADLGNKDDFETSLLEFRLLKSSAIDRLKEESSSNKSIYHDELQNNQSDDSDFFE
Protein: Hexosyltransferase (EC 2.4.1.-) (Q57Y31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MAPALRGNRIGRCTAHKRRYWLIIILLAVSAAIVTFRTLLEDVERVRRRERKKITERCTYWKRPLWVKQSLTYVPAPVVSAWEERRYLVVIGIPSIDLDVRRRRRDLQRAACWTYAGVAVRANGFSGEMLPLYILARHPENGYTYTKALVEEATQWSDILTLPMNEGRPSGRKRVGQGGKWGIDAEIGMSRKTFLWFDMSVCLFPYAPYIAKADDDMFLRVPQYLADLRNLPRRGLYWGTIDVHTVQGFRFNYAYGACYTLGRDVAERFVSYKPLRTIIHVPYTAIRDEEFQSLCVMVEDAMVGITLRRAMYHTNITYVHEPKCSFHDVHAGTTLGAVTKSSIMVHHVNESDYNELRRRFNNEKNISHRSLTGSQGPLREMSCL
Protein: dATP triphosphohydrolase (dATPase) (DatZ) (A0A7U3TCA2)
Organism: Cyanophage S-2L (Cyanobacteria phage S-2L)
Function: Catalyzes the hydrolysis of dATP, dADP and dAMP into dA. This step is essential for Z-genome synthesis (containing aminoadenine instead of adenine). Specifically removes dATP and its precursor dADP from the nucleotide pool of the host, preventing the incorporation of A into the phage genome and favoring the integration of the Z-base into the viral genome.
Interaction partners:
Sequence:
MTLQITETYERLRASHISRWGIVQTTYPQNIAEHMWRVWLLCRDWGAAAGMPQHTVRQACEFALVHDLAEIRTGDAPTPHKTPELKELLAGIEAQIVPEVAELEATMAPEARELWKFCDTAEAVLFLKVNGLGAHAYDVQHLLMEQMKRRLMDSVLDVEVQDELMFQFERTIKKT
Protein: GDP-mannose transporter (GMT) (Q6FRE5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GDP-Man:Man
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MSELKSRIGNSGSIANSGPVSILCYCASSILMTVTNKFVVNTDGFNMFFVMLFAQSLVCTMCLMVLKMFGYAKYRPLNLIDVKNWLPISFLLVFMIFTSAKALKYMPVPIYTIFKNLTIILIAYGEVLFFGGSVTPMELSSFILMVLSSVVASLGDQQAAKIAQPLANNSILSPEYYWMFLNCICSASFVLIMRKRIKLTNFKDYDTMFYNNALALPILLGFSFLSEDWSSENLAQNFSGESLSAMIISGMTSVGISYCSGWCVRATSSTTYSMVGALNKLPIALAGLIFFDAPRNFLSIMSIFIGFASGLSYAVAKQKKVQKN
Protein: Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Q9VN77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Rab proteins geranylgeranyltransferase component A
- LD45906p
- FI07418p
- Rab32, isoform B
- FI01544p
- LD34211p
- Ras-related protein Rab-36
Sequence:
MHGRVKVRTTEEERERKKKEQALKVRAYRAAMGRIQKKREAGELDNEMLSLTVQILLRNPDVSMLWNIRRECVLEKLFRLKEEEATCETPSEEKPEKENQTGENKPSEKKAAGEDKAHSIFTCELDLTEQCLMVNPKSYNAWHHRCWTLEQNPRADWQQEVKLCNKYLKFDERNFHTWDYRRYVTGKAMVPATQELDFCTEKIRANFSNYSSWHHRSLLLPELYPNQQRDRPMSEEKLQKELEMVLTAAFTDPNDSSAWFYQRWLLGSGAQLDRAPRIAAFRLESHGAVLALDKPYPDIKQLKTELVGGGQTILLEFWLPVDKRGTSWKCQQNFDYQRNSAYSLRLSDQKVDLSPLSGSENGAYYIAPPHGTTSCSKDLLAELQTQLQSCLDLLEFEPDSKWTLLTSALLMRAIDFSANHETSLAHLAKLEKVDFLREGYYKDLAARWTLEWELAKWPQSADFPKRFDIANAVLLESLPYDQYLVIADEITLPNKLRDKLGESVPKTFADLKLQS
Protein: Large ribosomal subunit protein P2B (60S acidic ribosomal protein P2B) (O24415)
Organism: Zea mays (Maize)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- 60S ribosomal protein L5-1
- 60S ribosomal protein L3-1
- Putative inactive leucine-rich repeat receptor-like protein kinase
- 60S ribosomal protein L27a-3
- 60S ribosomal protein L27a-2
- 60S ribosomal protein L13a-1
- 60S ribosomal protein L13a-1
- Ribosomal protein L37
- Ribosomal protein L37
- 60S ribosomal protein L28-1
Sequence:
MKVIAAYLLAVLGGNTSPTADDVKSILESVGAEADEEKLEFLLTELKDKDITEVIAAGRERLSSVPSGGGAIDMGAPAAVAGGGAAPAEEAKKEEKVEEKEESDEDMGFSLFD
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FII8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MNKNMNAFKSLYFLTFLFMSSVLAANLPKLTNICQIPDNVKKTSGFKGEIRRIGLFPPGGDYTYLLKFPSTGSTASDTISLTTKPQLSTSGWFPSLFGHTYFIKADLLVYMVAYFVPTETGEYTFKLVNSDDAAVMYVGNPSAFPCGSIDTWPEPRKEDINVCDKISASTKLYMEKGLAYPVRLVWYNGGGDGQFNAQFIDPSGTTHTDWNGYVWQYDACTDCDYKPIPDASTTTSAGYVLSTTTTRTSESSYTDVNGYATAEDFFWEEIPTSTESISIPDPTTSSFTNSKDYGEEIISFYSTTASNGKPITGTTTTTVIHTYDPLSIPDPITSSFTNSQDYGEEIISFYSTHEANGRPIVGSTTTTVIHTYDPLSIPDPITSSFTNSQDYGEEIISFYSTNEANGRPIVGSTTTTVIHTYDPLSIPSPTTSSFTHSDEYGEEIISFYKTNEKNGKPIIGSNTTTVVHPIVHSSSVSPLSSKNQAASSNRASMVNSTITHASTTVMSDSIITSTSTTWYSSDDWRVEEIVSWYGTTDAYNHTVQGVGTAYFRDRVDALPVMVNSSETVSTSSQSSSTASETSSSSISSSNTLNMPTYRNVSDNNVPPLSPSQVYTTVTTKSTSYSRITITSCDDMACNVITTTTSDVVTLTTTYCPETAMNEMHASSPDSASASSGNNDLTKQVSQSAITTVINGMTVTTVTDCPESSSVSSSASAVQNANVNTGYDNKIPTIDVIKTFKTTVTIIETPDQPNTQNIPSKIDTTSTKTETVVVTEKDNGNVASTKIAGDHGSIVTRSTTKASGAQIHSDTTLSHVRAETTTDKTGFQYSAPSNHVVQQTVNGADMITAKSANFFTAVFISLLWYFI
Protein: Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17) (Q91VC7)
Organism: Mus musculus (Mouse)
Function: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 12A
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 12B
- Protein phosphatase 1 regulatory subunit 12C
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Transforming protein RhoA
- Serine/threonine-protein kinase N1
- Myosin regulatory light chain 12B
Sequence:
MAAQRLGKRVLSKLQSPSRARGPGGSPSGLQKRHARVTVKYDRRELQRRLDVEKWIDGCLEELYRGRESDMPDEVNIDELLELDSEEERCRKIQGLLEACANPTEDFVQELLAKLRGLHKQPGFPQPSPSDDPSLSPRQDRAHTAPP
Protein: Transmembrane protein 43 (Protein LUMA) (Q9BTV4)
Organism: Homo sapiens (Human)
Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10. Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32614325}. Nucleus inner membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:34050020}. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.
Interaction partners:
- Desmocollin-2
- Plakophilin-2
- Desmoglein-2
- Junction plakoglobin
- Desmocollin-3
- Emerin
- SUN domain-containing protein 2
- Transforming growth factor beta-3 proprotein
- Ryanodine receptor 2
- Prelamin-A/C
Sequence:
MAANYSSTSTRREHVKVKTSSQPGFLERLSETSGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSVAPENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDGQVKKETRYSYNTEWRSEIINSKNFDREIGHKNPSAMAVESFMATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLRVSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMFMGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPILVARTRVPAKKLE
Protein: Calpain-3 (EC 3.4.22.54) (A0A0S2Z3E6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367132}.
Interaction partners:
Sequence:
MHGNKQHLQKDFFLYNASKARSKTYINMREVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVW
Protein: Probable aquaporin PIP2-8 (Plasma membrane intrinsic protein 2-8) (AtPIP2;8) (Plasma membrane intrinsic protein 3b) (PIP3b) (Q9ZVX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Aquaporin PIP2-7
- Probable aquaporin PIP2-5
- Aquaporin PIP2-3
- Probable aquaporin SIP1-2
- PAMP-induced secreted peptide 1
- Probable aquaporin SIP2-1
Sequence:
MSKEVSEEGRHGKDYVDPPPAPLLDMAELKLWSFYRAIIAEFIATLLFLYVTVATVIGHKNQTGPCGGVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLPRAVAYMVAQCLGAICGVGLVKAFMMTPYKRLGGGANTVADGYSTGTALGAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNNEKAWDDHWIFWVGPFVGALAAAAYHQYILRAAAIKALASFRSNPTN
Protein: Polyadenylate-binding protein-interacting protein 2 (PABP-interacting protein 2) (PAIP-2) (Poly(A)-binding protein-interacting protein 2) (Q9BPZ3)
Organism: Homo sapiens (Human)
Function: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11172725}.
Interaction partners:
- Polyadenylate-binding protein 1
- Polyadenylate-binding protein-interacting protein 1
- E3 ubiquitin-protein ligase UBR5
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 3 subunit J
- ELAV-like protein 1
- Polyadenylate-binding protein 5
- Polyadenylate-binding protein 4
Sequence:
MKDPSRSSTSPSIINEDVIINGHSHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNDLVISDGSSLEDLVVKSNLNPNAKEFVPGVKYGNI
Protein: CDC16 (O96679)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPGDTENTSTDTTNEHIDLALYRQLVKQFIDMRRYSTALFWAEKVAVLGGLEPRDIYYQAQCMYLLGEYHRAAHTIQHHKLEKNSLPCFNLLLESLYAAKEFTEAANVIQNVEVEVMTTSLINQPVDASSGCYLESNSVFGGEENHRNELLSSIYLMKGKVYEALDNRGMAMDFYVQALHKSIYCFEALEALVQHEMLMAWEEFELMHHLPLAQQSSEADAKFILKLYESRLKKYYELISARNAEEMSPIVNSLTYSSLSRNLQLECQQSGSSDTQMPKVSAVKVPLTPSQFMSPAQKVLEDLKAPTFSLQTSLSKASSLIDASHRSMFDSSSRRRSRDHDTDTLIPIAECLDRVQRSTDLMAAEAEKCFYDCDYKQCLKILNELLKVDPFHNTALTIQIACLVENGDFNRLFYVAHKLVDRYPDKAISWYAVGCYYDMIGKSDPARRYLSKATALDRLYGPAWLAYGHSFANENEHEQAMAAYFKATQLMRGCHLPLLYIGVECGLTKNLELAEKFFLQAMNIAPLDVYVLHELGVIKYEYEFFDGAATIFQCTVDIVKQRAKSNNEEISSRWEPLFINLGHSLRKVHKYEEALYNFQYALLLKPQSPTTYTSIGFIHALLGNLDPAIEAFHKSLALNRDCIVTSTILKSCIEDLMDDSATIDEICSAALRDVAKNITANSRRVLNSDKFNGMKLKFDEEEEFANSDSNMVVEMSFDT