wanglab/gogpt-training-data huggingface dataset:
Protein: Small RNA 2'-O-methyltransferase (EC 2.1.1.386) (A3DJ37)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Interaction partners:
- Metallophosphoesterase
- TROVE domain-containing protein
- Nucleotidyltransferase
Sequence:
MILTITYTQPPATDLGYLLHKNPSRPQTFELNHGKAHIFYPEATSERCTVALLLDIDPIDLARGKKGSSGEGGLFDYVNDRPYVSSSFMSVAISRVFGTAMSGKCKEKPELAAIKLPLKAKIMMLPCKGGEEIIYRLFEPLGYKVDVEGYMLDEKFPEWGKSRYYTVSLEGEVRVRDLLNHIYVLIPVLDSEKHYWVGEDEIDKLFQHGEGWLVDHPEKELITGRYLIRKKRLVNQALKRLLEASDVVDDENEDDEPLKNEETEKKLNLNQQRLGTVVAVLKSVNAKKVIDLGCGEGNLLSLLLKDKSFEQITGVDVSYSVLERAKDRLKIDRLPEMQRKRISLFQSSLVYRDKRFSGYDAATVIEVIEHLDENRLQAFEKVLFEFTRPQTVIVSTPNKEYNFHYQNLFEGNLRHRDHRFEWTRKEFETWAVKVAEKYGYSVRFLQIGEIDDEFGSPTQMGVFTL
Protein: G-protein coupled receptor family C group 5 member D (Q9JIL6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Centrosomal protein of 70 kDa
- Keratin-associated protein 21-1
Sequence:
MYEDCVKSTEDYYLFCDNEGPWAIVLESLAVIGIVVTILLLLAFLFLMRKVQDCSQWNVLPTQFLFLLAVLGLFGLTFAFIIQLNHQTAPVRYFLFGVLFAICFSCLLAHASNLVKLVRGRVSFCWTTILFIAIGVSLLQTIIAIEYVTLIMTRGLMFEHMTPYQLNVDFVCLLIYVLFLMALTFFVSKATFCGPCENWKQHGRLIFATVLVSIIIWVVWISMLLRGNPQLQRQPHWDDAVICIGLVTNAWVFLLIYIIPELSILYRSCRQECPTQGNVCQVPVYQRSFRMDTQEPTRARDSDGAQEDVALTAYGTPIQLQSADPSREYLIPSATLSPQQDAGL
Protein: Heparan sulfate 2-O-sulfotransferase 1 (2-O-sulfotransferase) (2-OST) (2OST) (EC 2.8.2.-) (Q8R3H7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Required for metanephric development of kidney formation, suggesting that 2-O-sulfation within HS is essential for signaling between ureteric bud and metanephric mesenchyme. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11687650}; Single-pass type II membrane protein {ECO:0000269|PubMed:11687650}.
Interaction partners:
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Heparan-sulfate 6-O-sulfotransferase 3
- Heparan-sulfate 6-O-sulfotransferase 2
- Exostosin-2
- Exostosin-like 3
Sequence:
MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRAKLERAIARHEVREIEQRHTMDGPRQDATLDEEEDIIIIYNRVPKTASTSFTNIAYDLCAKNRYHVLHINTTKNNPVMSLQDQVRFVKNITTWNEMKPGFYHGHISYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKSNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATDLYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
Protein: 6-phospho-beta-galactosidase (EC 3.2.1.85) (Beta-D-phosphogalactoside galactohydrolase) (PGALase) (P-beta-Gal) (PBG) (P50978)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Interaction partners:
- PTS system lactose-specific EIICB component
- PTS system lactose-specific EIIA component
- Galactose-6-phosphate isomerase subunit LacB
- Galactose-6-phosphate isomerase subunit LacA
- Tagatose 1,6-diphosphate aldolase 1
- Tagatose-6-phosphate kinase
- Lactose phosphotransferase system repressor
- Mannose-6-phosphate isomerase
Sequence:
MSKTLPKDFIFGGATAAYQAEGATHADGKGPVAWDKYLEDNYWYTAEPASDFYHQYPVDLKLAEEFGVNGIRISIAWSRIFPKGYGAVNPKGLAFYHNLFAECHKRHVEPFVTLHHFDTPEALHSNGDFLNRENIEHFVNYAEFCFKEFPEVNYWTTFNEIGPIGDGQYLVGKFPPGIQYDLAKVFQSHHNMMVAHSKAVKLFKDGGYSGEIGVVHALPTKYPYDPNNPADIRAAELEDIIHNKFILDATYLGKYSEKTMEGVNHILAVNGGQLDLREEDFAALEAAKDLNDFLGINYYMSDWMRAFDGETEITHNAKGEKGSSKYQIKGVGRREAPVNVPKTDWDWIIYPQGLYDQIMRVKQDYPNYKKIYITENGLGYKDEFVNHTVYDDARIDYVKKHLEVLSDAIADGANVKGYFIWSLMDVFSWSNGYEKRYGLFYVDFDTQERYPKKSAYWYKKLAETQIID
Protein: FI23955p1 (Pruning defect 1, isoform A) (Q9VGI1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP01065p
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like domain-containing protein
- GH17761p
- Polyubiquitin
Sequence:
MESPLLPKANNNLGMDKMSSSLNSSTMEDTTPSDSGVQLLDSENSDVMVESICSYEENVRPMPLPLVDPNSNVTAAPDESMTISECSTFDTTEKIVYRRKVHKASSASKTPKKRVSFHEDILKNTRTDNIHIEHGFITYKNGRKLAFANSAGVAGAPGRYSWCPDRERPEGPNELSAAGREDDGEEATGGGGARRKRHLVYRNACSDVLDYDNIFDTDEAPGLHYDTSGVFEYGPATQKQEEQPQLYKCVCSSSNSSLDSDEQDKNSNANCKQYEQAKSSSCDCIGMSNANNNLIGDNCYYSEPNIGDADSPKVKSVWNKEKKPKSSCLKKTKLHTNVILEQDLNGRVKKFNVHDIKHQLLDNSSKMIFGSLKSIFTMPLPERGVPEGSEDLQAVVECVPELEQTPEHKSRPAAESPPLRAKPFLSKSLDGSKQAQPVKKFVHNVDEQLRHKNEDDGASSTEASPMESKQSLMLHRQEEFDKETVPMGSAQGEFRSKFIINCESTVFEHTGVSYETGDLQSELSSGIQHTSVASLLEQNTPIAEPAASQIKKSFLDAPIAKTFSNFFRSFKDSTPVAKDEQAVTDNYFASKIAKPQQQAPAAGKLQRNFSSSTISEPSSNTNTSSNHQIAMNPQLGNAERQSRHLPSPLKKRGQPLQPPRYYDQQHPHQSRSLHSPSAYLAAGRGGPGGSGRDSKSTILSEEFDDILTITTTDTTNARSMDSDLVIVDYTDVDYAHLLKPPAPAAKTSLINRFLRNVTQKKIMETSIRKNNFFADKLRTEQRHAGSDLYVKGARPKNYELIDDLNAEIAMEIEMCGTNSPRRELAISLDNDFQGNLSNFELGIGEISIDVFKGKSLFNLKQSNEQLMKAFKLYTGYNVDGIMTPVLVLLTDKTLYVVNMEGNSLCVKFVLAYKDLDVILMGPFGNTVLLSNSNRDMQQVLLAGGPYPAGSLVANLELCARRSGSTLPAVGQLTLEHLAPLQAFVRANSCVGVAEHWMLYAVVNVPAGGSMRVESPSELLGPSMKGFLMHRRLRQTISTSAANRIFWQPGYFLLKAGVLYMFNDSTQRLPSWAMALAECQGARRTVKSERPHCFEITLKGEVLQMAAPDEYVASEWLQALLQSASGLVVQEEKHKTLGCTLIVTDNHLITLREDFSAPLRKISQQADNNAAVQGNKETMLEEDMLSVFETSSLMGSTISTPTRGTQHSYSSLSSTPTKQTNEDAAPKETVASPEKSQRMTSVYGKNSGLAILTCADIKEMTGIKITSRSETWWCILEFSCQEAPLENQDDLVIFFASSMEMQRFLRLLEQLWQSKNNDLFPITILDDGDSLAEQYNKLYMDTNRAWEPLLSAALG
Protein: ZIP Zinc transporter, putative (Q4WPK3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAKALLLLSLLGGLGLAHAQYVTYTGCHNHGSTEYCFGPDGKETPFPTPTESASRTVPVTVAAAAAATTTSSADASAVTGCHSHGSDVFCIDGDGNEVQVILPSTPTGELPAQYTGCHSHGSETFCMDPEGNDVQIVGEEGSTEGSSSSGSSGESQSGSKEGMNCHFHAGVEHCIGAGESESGSSQKSCGLRTRDYDVPLRIGTLFVVLVTSSIGVFLPMLLVKLPSAKINGVVSTVIKQFGTGVILSTAFVHLYTHANLMFTNECLGELEYEATTSAVVMAGIFLSFLFEYIGHRIILARATRCASPCPEQTGDMSPSSTSKELPASQPPPPPPQQQQQPPTLAALGHHHGPPLDPTNPNTKLSVLVMEAGVVFHSILIGLTLVVAGDSFYKTLLVVIVFHQFFEGLALGARIAMLPGPLLGSKALMAGTFAVITPIGMAIGLGVLHSFNGNDQSTLVALGTLDALSAGILVWVGLVDMWARDWVMDGGEMMNARLSIVAVGGFSLIAGMVLMGVLGKWA
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 (Complex I-MWFE) (CI-MWFE) (NADH-ubiquinone oxidoreductase MWFE subunit) (Q02377)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:18721790}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MWFEVLPGIAVMGVCLFIPGMATARIHRFSNGGKEKRVAHYPYQWYLMERDRRVSGVNRSYVSKGLENID
Protein: Transducin/WD40 repeat-like superfamily protein (F4IQ10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g05090/T12H1_5
- Ubiquitin carboxyl-terminal hydrolase 3
- Ubiquitin carboxyl-terminal hydrolase 4
- Holliday junction resolvase
- Mitotic spindle checkpoint protein MAD2
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 2
- Anaphase-promoting complex subunit 6
- Ubiquitin C-terminal hydrolase 22
Sequence:
MMNTSNGMISGPSSSSASAANPQSPGIKTYFKTPEGKYKLHYEKTHPSGLLHYTHGKTVTQVLCKNIKCTFHFYVLKVVSENGFVKFWCQVTLAHLKDKPAPSTPTGTSSSSTASSGFRSATARLLGGGNGNRALSFVGGNGGAKNVGASSRIGASFAASSSNTSATNTNFDGKGTYLVFNVGDAIFISDLNSQDKDPVKSIHISNSNPMCHAFHPDAKDGHDLLIGLNSGDVYTVSLRQQLQDVGKKLVSAQHYNKDGSVNNSRCTSIAWVPGGDGSFVAAHADGNLYVYEKNKEGATDSSFSAIRDPTQFSVDKAKYSKSNPVARWHIGQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWGEGHNSWVSGVAFDSYWSSPNSEGSGENVMYRFGSVGQDTQLLLWDLEMDEIVVPLRRPPGGSPTYSTGSQSAHWDNIVPMGTLQPAPCMRDVPKLSPVVAHRVHTEPLSGLIFTQESLITACREGHLKIWTRPDTQPSSSSEATNPTTSKPSLTSKVGGSS
Protein: Astrotactin-2 (Q80Z10)
Organism: Mus musculus (Mouse)
Function: Mediates recycling of the neuronal cell adhesion molecule ASTN1 to the anterior pole of the cell membrane in migrating neurons. Promotes ASTN1 internalization and intracellular transport of endocytosed ASTN1. Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting it is recruited to membranes that contain lipids with a phosphoinositide headgroup (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:20573900}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:20573900}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20573900}. Early endosome {ECO:0000269|PubMed:20573900}. Late endosome {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305|PubMed:20573900}. Cytoplasmic vesicle {ECO:0000269|PubMed:20573900}. Note=Integral membrane protein not detected at the cell membrane. Detected in cytoplasmic vesicles in the cell cortex, close to the anterior pole of migrating neurons. Detected at the base of the leading process in migrating neurons. {ECO:0000269|PubMed:20573900}.
Interaction partners:
Sequence:
MAAAGARRSPGRGLGLRGRPRLGFHPGPPPPPPPPLLLLFLLLLPPPPLLAGATAAAASREPDSPCRLKTVTVSTLPALRESDIGWSGARTGAAAGAGAGTGAGAGAAAAAASAASPGSAGSAGTAAESRLLLFVRNELPGRIAVQDDLDNTELPFFTLEMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVALYAQRRWQKRRRIPQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDYEEEEEPPRRANHVSREDEFGSQMTHALDSLGRPGEEKVEFEKKAAAEATQETVESLMQKFKESFRANTPVEIGQLQPASRSSTSAGKRKRRNKSRGGISFGRTKGTSGSEADDETQLTFYTEQYRSRRRSKGLLKSPVNKTALTLIAVSSCILAMVCGNQMSCPLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPDTGECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELSINPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMKDGSGCYDHSKGIDCSDGFNGGCEQLCLQQTLPLPYDTTSSTIFMFCGCVEEYKLAPDGKSCLMLSDVCEGPKCLKPDSKFNDTLFGEMLHGYNNRTQHVNQGQVFQMTFRENNFIKDFPQLADGLLVIPLPVEEQCRGVLSEPLPDLQLLTGDIRYDEAMGYPMVQQWRVRSNLYRVKLSTITLSAGFTNVLKILTKESSRDELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQKETTELGSKKELKSMPFITYLSGLLTAQMLSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKNALMSSYWCSGKGDVIDDWCRCDLSAFDASGLPNCSPLPQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLSFADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRTACPLVDDNKAEEIADKIYNLYNGYTSGKEQQTAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRRLERVSSHCSSLLRSAYIQSRVDTIPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNTYGETKGR
Protein: Salicylate/benzoate carboxyl methyltransferase (Benzoate O-methyltransferase) (EC 2.1.1.273) (S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase) (S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase) (SABATH methyltransferase) (Salicylate carboxymethyltransferase) (EC 2.1.1.274) (Q6XMI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methyltransferase involved in the biosynthesis of methylsalicylate in response to stresses. Utilizes salicylic acid (SA) more efficiently than benzoic acid (BA). Can also use anthranilic acid and m-hydroxybenzoic acid as substrate.
Interaction partners:
- NAC domain-containing protein 19
- DNA
- Isochorismate synthase 1, chloroplastic
- UDP-glycosyltransferase 74F2
- NAC domain-containing protein 55
- NAC domain-containing protein 72
- Regulatory protein NPR1
Sequence:
MDPRFINTIPSLRYDDDKCDDEYAFVKALCMSGGDGANSYSANSRLQKKVLSMAKPVLVRNTEEMMMNLDFPTYIKVAELGCSSGQNSFLAIFEIINTINVLCQHVNKNSPEIDCCLNDLPENDFNTTFKFVPFFNKELMITNKSSCFVYGAPGSFYSRLFSRNSLHLIHSSYALHWLSKVPEKLENNKGNLYITSSSPQSAYKAYLNQFQKDFTMFLRLRSEEIVSNGRMVLTFIGRNTLNDPLYRDCCHFWTLLSNSLRDLVFEGLVSESKLDAFNMPFYDPNVQELKEVIQKEGSFEINELESHGFDLGHYYEEDDFEAGRNEANGIRAVSEPMLIAHFGEEIIDTLFDKYAYHVTQHANCRNKTTVSLVVSLTKK
Protein: Thioredoxin (Trx) (ATL-derived factor) (ADF) (Surface-associated sulphydryl protein) (SASP) (allergen Hom s Trx) (P10599)
Organism: Homo sapiens (Human)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Cytoplasm {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Secreted {ECO:0000269|PubMed:1332947}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA) (PubMed:9108029). Predominantly in the cytoplasm in non irradiated cells (PubMed:11118054). Radiation induces translocation of TRX from the cytoplasm to the nucleus (PubMed:11118054). Secreted by a leaderless secretory pathway (PubMed:1332947). {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:1332947, ECO:0000269|PubMed:9108029}.
Interaction partners:
- Thioredoxin-interacting protein
- Thioredoxin reductase 1, cytoplasmic
- Mitogen-activated protein kinase kinase kinase 5
- Peroxiredoxin-1
- DNA repair nuclease/redox regulator APEX1
- Nuclear factor NF-kappa-B p105 subunit
- Peroxiredoxin-5, mitochondrial
- Peroxiredoxin-2
- Thioredoxin, mitochondrial
- Glutaredoxin-1
Sequence:
MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Protein: Colony-stimulating factor 1 (D8UWE0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MPRLGSQVSLFRCTLLSSLLLVCSIHETEQNSYCQQIITERHLDHLQELADTQMQQPGTVSFRFISKMRLSDSVCYVKAAFPLLGTILNRTTFKENSTNANKMKTVRKMYENIDEDVDPCIRDEDDEEHALSEMCFEEFTTSPYEMLVLVRQFFQDIKQLLQNKETFEKDCSQVYRSACAGPRQHSSSPEQRRKEPPAASGGHRELLVYVTVASVVAVLLAMGGLLFYKYKSKVLQRGAALKEGGCDPEEPESRALQGAQGCAELETQEL
Protein: RNA binding (RRM/RBD/RNP motifs) family protein (F4JXH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription regulator
- Cell differentiation, Rcd1-like protein
- Probable NOT transcription complex subunit VIP2
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- Carbon catabolite repressor protein 4 homolog 1
- Transcription regulator NOT2/NOT3/NOT5 family protein
- NOT2 / NOT3 / NOT5 family
- Probable CCR4-associated factor 1 homolog 11
- RNA binding
Sequence:
MSDHGEKTCPLCAEEMDLTDQQLKPCKCGYQICVWCWHHIVDMAEKDQIEGRCPACRTPYDKEKIVGMTVNCDSLASEGNMERKKIQKSKSKSSEGRKQQLTSVRVIQRNLVYIVGLPLNLADEDLLQHKEYFGQYGKVLKVSMSRTASGVIQQFPNNTCSVYITYGKEEEAVRCIQAVHGFILDGKPLKACFGTTKYCHAWLRNVACVNPDCLYLHEVGSQDDSFTKDEIISAYTRSRVQQITGATNILQHHSGNMLPPPLDAYCSDSSSAKPIIKVPSTNATSVPRYSPPSGSGSSSRSTALPAAASWGTHQSLATSVTSNGSSDIQRSTSVNGTLPFSAVVANAAHGPVSSNDILKRPSRKEESQIVMDKVKPSVLKPLQHNVVVSGSERITAPDRDPTSNRLSSSVDSAYGGRDIDQPSAYSGRDIDKPSSTVSSFDAANEAVEDVPTVSNLLDGVACMRITMNCRDERPDITMAIGSQSDQGSIRQPGSEVSKLPDLEQCRIDSSINTDKKAISLEDRIPRTRPGWDWISDLQSQMQGSSKLQVEDISTLDSQRPHPEEDIIHSRLLSNLSSSSLDTNHMASRSSLPCEVRGSDRLHLPNGFGEKSMSSVEHSLFANEGRNKVNNAEDAILSNILSLDFDPWDESLTSPHNLAELLGEVDQRSSTLKPSNFLKQHNNQSRFSFARYEESSNQAYDSENYSIYGQLSRDKPIQESAMSRDIYRNNLGSVNGFASNFAGGLDNFAASPLFSSHKNPVSRPQVSAPPGFSAPNRLPPPGFSSHERVGLSSDTTLGNRFLDSTSLRNAYQVPPPVGNSNGASDIDFVDPAILAVGRGMVNADLDMRSGFSSQLNSFENETGLHMLRQQSLSSAQQVNGFHHDLRNLSPSLNDPYGFSSRLMDQTQGSSLSPFSQLPRQQPSANSILSNGHHWDKWNEGQSVNNIGMAELLRNERLGFNGSLYNNGYEEPKFRIPSPGDVYNRTYGI
Protein: E3 ubiquitin-protein ligase PIB1 (EC 2.3.2.27) (Phosphatidylinositol 3-phosphate-binding protein 1) (RING-type E3 ubiquitin transferase PIB1) (Q06651)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as an E3 ubiquitin-protein ligase. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate.
Subcellular location: Endosome membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein.
Interaction partners:
- Transmembrane E3 ubiquitin-protein ligase 1
- Protein SSH4
Sequence:
MVIKEDCINNLARWQADEEAHSCFQCKTNFSFLVRRHHCRCCGRIFCSSCTENFVNYNKKRVHALQKKNSDVESPPYRTCNECYDNLLHLNLLVSSTNRDVRLSQTSVPPNALALSAPDSNTDEDAEILEDSVDQSGTACRSEESSQNEEDHFCPICNSDLTQFPDEEETRKHVEDCIQRAENAQQHTNTSDAADDSVKESPAFQNRMLVYKISPNTTDNAIKECPICFENMEPGEKVGRLECLCVFHYKCIKNWFHKRAQMTAAQKGNGHAFVKRNFCPFHDAVF
Protein: VWFA domain-containing protein (Q8TBN2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
GQGTGGEGRALLTPPPPAECKCGPIDLLFVLDSSESIGLQNFEIAKDFVVKVIDRLSRDELVKFEPGQSYAGVVQYSHSQMQEHVSLRSPSIRNVQELKEAIKSLQWMAGGTFTGEALQYTRDQLLPPSPNNRIALVITDGRSDTQRDTTPLNVLCSPGIQVVSVGIKDVFDFIPGSDQLNVISCQGLAPSQGRPGLSLVKENYAELLEDAFLKNVTAQICIDKKCPDYTCPITFSSPADITILLDGSASVGSHNFDTTKHFAKRLAERFLTAGRTDPAHDVRVAVVQYSGTGQQRPERASLQFLQNYTALASAVDAMDFINDATDVNDALGYVTRFYREASSGAAKKRLLLFSDGNSQGATPAAIEKAVQEAQRAGIEIFVVVVGRQVNEPHIRVLVTGKTAEYDVAYGESHLFRVPSYQALLRGVFHQTVSRKVALG
Protein: GDSL esterase/lipase At4g01130 (EC 3.1.1.-) (Extracellular lipase At4g01130) (Q9M153)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Nitrogen regulatory protein P-II homolog
- Oleosin 14.9 kDa
- Biotin carboxylase, chloroplastic
Sequence:
MASDINRRRSFSLLVLIIVMLYGHKGDSKCDFEAIFNFGDSNSDTGGFWAAFPAQSGPWGMTYFKKPAGRASDGRLIIDFLAKSLGMPFLSPYLQSIGSDFRHGANFATLASTVLLPNTSLFVSGISPFSLAIQLNQMKQFKVNVDESHSLDRPGLKILPSKIVFGKSLYTFYIGQNDFTSNLASIGVERVKLYLPQVIGQIAGTIKEIYGIGGRTFLVLNLAPVGCYPAILTGYTHTDADLDKYGCLIPVNKAVKYYNTLLNKTLSQTRTELKNATVIYLDTHKILLDLFQHPKSYGMKHGIKACCGYGGRPYNFNQKLFCGNTKVIGNFSTTAKACHDPHNYVSWDGIHATEAANHHISMAILDGSISYPPFILNNLCSP
Protein: RING-type domain-containing protein (Q965F9)
Organism: Caenorhabditis elegans
Interaction partners:
- Bifunctional glyoxylate cycle protein
- Partitioning defective protein 3
- Partitioning defective protein 6
- Probable citrate synthase, mitochondrial
- Protein kinase C-like 3
- Probable fumarate hydratase, mitochondrial
- Pyruvate kinase
- Pyruvate kinase
- Pyruvate carboxylase 1
- Zinc finger protein mex-5
Sequence:
MTDLDTSSAQIRASQSDLSIANSSPRLLESNATTSTACINDVQQPVRRDLSSELLCPLCDQLFDRMVRKLKNQENIESSYDDLFICEEKLQKAPTPPISEEIPAQKMTRSLSQRSKRRLFFSIAGPTICSSPITPHRRRPLSPSARPAKSSLKIPPEPLNHSLSPPGFHNSHHHRDDSLVLAGGNFRRNGFGRRSERFTAATTSAQSFAESSQISTGNSSKIDDESDGTKLKRNSFLRRSLNAFRSKSSGKEQKSFRVFAQIPEHPTEHHDVPEGDVEHLLPEKPTKSSIRSLWKRLFMPKKVSKVSPAAVQLLSQSPSTTDERSHHHTTISFVRLENEHDDPEYDEPLQLSKFSALGYYTGIGRKFERVASGCEITLVVFGHSGAGKTTFVRAIRQLFLEGTDRIRIIPIAERYRLAGIGMMPFPEGDNRLPHIVSMVLNNDETDMEYVLDIIDPEYDNSNLPQAYMDACDAAYLLVDTRNPASILSAHQIHRNMKHAQHIHVQCEMLMNVPSEASGQTRVLSANALETTMKTIPIRDVCANQLDKGVVEEMLLSICERVTTARNPQTPTSSPIATSSSPS
Protein: Trafficking regulator of GLUT4 1 (Dispanin subfamily B member 1) (DSPB1) (Tumor suppressor candidate 5 homolog) (Q8C838)
Organism: Mus musculus (Mouse)
Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:29787242}; Single-pass membrane protein {ECO:0000305|PubMed:29787242}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Single-pass membrane protein {ECO:0000305|PubMed:29787242}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
Interaction partners:
- Class A basic helix-loop-helix protein 9
Sequence:
MANPAQPPLQDPGSTSPLELPEMEKLLTKVENKDDQALNLSKSLSGALDLEQNGHSLPFKVISEGHRQPSLSGSPSRVSSRRASSVITTSYAQDQEAPKDYLVLAIASCFCPVWPLNLIPLIFSIMSRSSVQQGDLDGARRLGRLARLLSITFIILGIVIIIVAVTVNFTVPK
Protein: Polyadenylate-binding protein-interacting protein 1 (PABP-interacting protein 1) (PAIP-1) (Poly(A)-binding protein-interacting protein 1) (Q8VE62)
Organism: Mus musculus (Mouse)
Function: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Polyadenylate-binding protein 1
- Eukaryotic initiation factor 4A-I
- E3 ubiquitin-protein ligase UBR5
- Heterogeneous nuclear ribonucleoprotein Q
- Eukaryotic initiation factor 4A-II
- Polyadenylate-binding protein 1-like
- Polyadenylate-binding protein
- Polyadenylate-binding protein 5
- Polyadenylate-binding protein
- Polyadenylate-binding protein 5
Sequence:
MSDSFDRAPEQTKPQRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSANAPEFYPSGYSSNYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGWVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEAKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDTWKEKGKTDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ
Protein: Palmitoyl-[acyl-carrier-protein] 4-desaturase 2, chloroplastic (EC 1.14.19.11) (Acyl-[acyl-carrier-protein] desaturase 2) (Stearoyl-[acyl-carrier-protein] 9-desaturase 2) (Stearoyl-ACP desaturase 2) (EC 1.14.19.2) (E3PZS2)
Organism: Ophrys sphegodes (Early spider orchid) (Arachnites aranifera)
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. Catalyzes the desaturation of saturated fatty acid 18:0 and 16:0 to generate 18:1 (delta-9) and 16:1 (delta-4) intermediates, expected to give rise to 9-alkenes and 12-alkenes, respectively.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:P22337}.
Interaction partners:
Sequence:
MELHLALRASPLPAADPGRRPPPPRGNFATNCTAAINSTHISQEKFRSLDSWVEHNMLTFLKPVEKCWQPQDFLPDPSHLSAEELGDAVREIHERAAEIPDEVWVCMVGNMVTEEALPTYQSLISSVLGGTVAGSTPWDRWIRGWSAEENRHGDLLNKYLYLTGRLDMRQVEKTIQYLIGSGMDVGVGNSILCGFIYTCFQEKATFISHGNTARLAKHHGDTTLAKICGLVAADEKRHAVAYTNLMKKLFEVAPNESMLAFAHIMRAHVTMPASRMFDGRDPRLFTHFSAVTQKIGVYTVRDYGEMLDFFLKEWEISAVVDDLSPEGRQAQEYVCGLPEVMGKMAERADDRRKKLVNVGEPRYIPFSWIFNKQVCV
Protein: Trophinin (A2AFN3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDRRNDHGHRVPTFQGPLPPAGSLGLPFSPDVQSETTEKDPPIASRSKKNKNKKNSIKPMDKTTPAPPPVPSANDNASNKPKVTLQALNLPMFTQISQASATTEAPNIQASVTSQTQKAKTMRVTPKVSLTGSEDATTQLKPPLQALNLPVTTPTIQTPVANESANSLASTAVNKSKKASTANNAANKTVPSAAEISLASAATHTVTTQGQAAKETGSIQTIAATARSKKNSKGKRTPAKTTNTDNEYVEASNAIEASSRQIGASGRQTEASNRQIEASSRQTEASNRQTEASSRQTEASSRQTETSNRQIGASNRQIMASNRQIGASNRQIEASNRQIGASNRQTEVSSRQIEASNRQIGASNRQTEASNRQIGASNRQTEASNRQIGASNRQTDASNRQTDASNRQTEASSRQTEASSRQTEASSRQTEASSRQIEASAAAVRPKKPRGKKGNNKGSNSASEPSEAPPAIQTVTNHALSVTVRIRRGSRARKAANKNRATESQAQIAEQGAQASEASISALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKH