wanglab/gogpt-training-data huggingface dataset:
Protein: Thioredoxin domain-containing protein 9 (ATP-binding protein associated with cell differentiation) (Q9CQ79)
Organism: Mus musculus (Mouse)
Function: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15009089}. Nucleus {ECO:0000269|PubMed:15009089}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15009089}. Midbody {ECO:0000269|PubMed:15009089}. Note=Co-localizes with beta-tubulin in the centrosome. {ECO:0000269|PubMed:15009089}.
Interaction partners:
- Small ribosomal subunit protein uS17m
- Endoplasmic reticulum-Golgi intermediate compartment protein 2
Sequence:
MEGNGSVDMFSEVLENQFLQAAKLVENHLDSEIQKLDQIGEDELELLKEKRLAALRKAQQQKQEWLSKGHGEYREIGSERDFFQEVKESEKVVCHFYRDTTFRCKILDRHLAILAKKHLETKFLKLNVEKAPFLCERLRIKVIPTLALLRDGKTQDYVVGFTDLGNTDDFTTETLEWRLGCSDVINYSGNLMEPPFQSQKKFGTNFTKLEKKTIRGKKYDSDSDDD
Protein: Sensor protein RstB (EC 2.7.13.3) (P18392)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system RstB/RstA. RstB functions as a membrane-associated protein kinase that phosphorylates RstA (Probable).
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Transcriptional regulatory protein RstA
- Transcriptional regulatory protein PhoP
- DNA-binding dual transcriptional regulator OmpR
- Phosphate regulon transcriptional regulatory protein PhoB
- Aerobic respiration control sensor protein ArcB
- Phosphotransferase RcsD
- Transcriptional regulatory protein BaeR
- Transcriptional regulatory protein CpxR
- Uncharacterized serine protease YdgD
- Sensory histidine kinase/phosphatase NtrB)
Sequence:
MKKLFIQFYLLLFVCFLVMSLLVGLVYKFTAERAGKQSLDDLMNSSLYLMRSELREIPPHDWGKTLKEMDLNLSFDLRVEPLSKYHLDDISMHRLRGGEIVALDDQYTFLQRIPRSHYVLAVGPVPYLYYLHQMRLLDIALIAFIAISLAFPVFIWMRPHWQDMLKLEAAAQRFGDGHLNERIHFDEGSSFERLGVAFNQMADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDNLSAAESQALNRDISQLEALIEELLTYARLDRPQNELHLSEPDLPLWLSTHLADIQAVTPDKTVRIKTLVQGHYAALDMRLMERVLDNLLNNALRYCHSTVETSLLLSGNRATLIVEDDGPGIAPENREHIFEPFVRLDPSRDRSTGGCGLGLAIVHSIALAMGGTVNCDTSELGGARFSFSWPLWHNIPQFTSA
Protein: BAG family molecular chaperone regulator 1 (BAG-1) (Bcl-2-associated athanogene 1) (B0K019)
Organism: Rattus norvegicus (Rat)
Function: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- BAG cochaperone 2.
- Heat shock cognate 71 kDa protein
- Apoptosis regulator Bcl-2
- Hsp70-binding protein 1
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 4L
- STIP1 homology and U-Box containing protein 1, isoform CRA_b.
- Hsc70-interacting protein
Sequence:
MADRGGARRPRGDQEPLGPRLRAPRSARETRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAASGACKPRVKKKVRPRSSQSEKVAHSKELTRSKKLTRSKKVTGTQEATQVEEVTTIEEATQTEEITVAEEVTQTENMAQTEEMVQTEEMEPPTLSVVVTHSNERYDLLVTPQQGNSEPIVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEAELKKLKDLEVSVEKTANHLEELNKELSDIQQGFLAKELQAEALCRLDRKIKATIEQFMKILEEIDTMVLPENFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALPE
Protein: Inactive rhomboid protein 1 (iRhom) (Rhomboid family protein rhomboid-5) (Q76NQ1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21439629}; Multi-pass membrane protein {ECO:0000269|PubMed:21439629}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- DSec61alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- GH11935p
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Malectin domain-containing protein
Sequence:
MSSNGSDLGHNNRRNEKGNPDSVHSSMRGSMSSTRRKSINFQNQLQLALESNECDVMYCSLSSGRFRAPNGENFPPHGGKLKLSPLEKYDDANRGVPPPSPAPNSDCFATCVANQLPSQSCSVGSAKPETSVMQKHGMAGNGMVGSGMSGNGMAANGTNYHQRGVSPNSRYRLERYRESQSTPQSKLMDNMGGMPSAVPSVSATRLLLPSNVPLPLAQCENYNAYLGSTVHTPVKRYVPTPPPAMELYSDLSISSSPAANLPTPAAAVASSASTSASAMQSQYANMPYNYRSKCCHSEASHGSLSRTSQTYASCSPACTSPSPAPSTSMSMVFSAASSCSPIMTATSSARSGNHRGDDSDSVIVVPPGGGAMAQIEAENPSGTCLHCNTVRRTTGVHQTTQTTGPISPVPISLPVPMAMPVMSGLNEQMPSQSLESSMVSVQAKRLEGGGNMAVPPGSNQHQLYRSQMASNPRLQHIHHQTQQHQSLQVLPQPQNHHLSCKKRIGMYMRRTTSQFFGVEPSTEAADCALWQGRHRRLAIRCFGMFDTELEYHMQQAIGGGNEDAGQSNGTNGNYAPDRPDILPVQDAIGMDMTMSGDSRRQKCYTNRDFLAGEFVERKASVGYMFVAMVSYLVHMFNKRRPIQMHRVRCPWQWSRSFAPIHVQSHSNQQTDADGCLTDGLEAIIDDEVFFDSPCEITTSAVNDESSDIGRQAAKPRPCADQSGVGVSVYMAERQQNGWRTSALNSGGNATSDINLTGDQSSHQPGAAHIPLCSSVSSQMQPAMRSSHSTTSTCNRGNRITAQLLDGVLENSRRPPLRCIKYFSVNDLDDRTDHRPFFTYWINTVQVVVLILSIICYGIAPIGIGSEQKTGQVLVTSLSLQTVQHVEQRNLWIGPRNIDLVHMGAKFAACMRRDIKITEVVTKTRRHERETACCIRNDDSGCVQSSQAECSIRGLYPTKSISTWKKWSPSESGPGGRISGSVCGLDPKFCDAPASIAPYEWPDDITKWPICRKTNSFTQRYRYKDHTSEHMVCEVIGHPCCTGLYGECRITTREYCDFIKGYFHEEASLCSQISCLNNVCGMFPFISVETPDQLYRLLTSLCMHAGILHLAITLIFQHLFLADLERLIGTVRTAIVYIMSGFAGNLTSAILVPHRPEVGPSASLSGVVASLIALLVWMHWKYLHKPHIALFKLLLLCSVLVGIGTLPYQLNFLGLLAGVICGCLLTMSLVPFTTFSKYGRKKKINLIWTCVLFHVVVYTAMIVTFYIHPSEFHSISFVDMFSNSNGYDNFTNADHHGVDVVSSNTRYSQTQNSQYYYHHHSDDIIRKSVTFTEKALVSHILYPTAPRKTSAQQWQEVEYSRSFNHLSNYSDRIKKSIGNISKLKQVFTSPIRFSNKNNHSNLMTELTSVHSENKQKYLGYINNNTEFNVL
Protein: Putative phospholipase B-like 2 (EC 3.1.1.-) (76 kDa protein) (p76) (LAMA-like protein 2) (Lamina ancestor homolog 2) (Phospholipase B domain-containing protein 2) [Cleaved into: Putative phospholipase B-like 2 32 kDa form; Putative phospholipase B-like 2 45 kDa form] (Q8NHP8)
Organism: Homo sapiens (Human)
Function: Putative phospholipase.
Subcellular location: Lysosome lumen {ECO:0000269|PubMed:17105447}.
Interaction partners:
Sequence:
MVGQMYCYPGSHLARALTRALALALVLALLVGPFLSGLAGAIPAPGGRWARDGQVPPASRSRSVLLDVSAGQLLMVDGRHPDAVAWANLTNAIRETGWAFLELGTSGQYNDSLQAYAAGVVEAAVSEELIYMHWMNTVVNYCGPFEYEVGYCERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKFTIKPLGFLLLQLSGDLEDLELALNKTKIKPSLGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQFREGPWGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGCVLEWVRNIVANRLASDGATWADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPGSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACNPQPNGENAISARSDLNPANGSYPFQALRQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSPFSGLLHMGQPDLWKFAPVKVSWD
Protein: Glycine N-methyltransferase (EC 2.1.1.20) (V9HW60)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMTLDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNYDHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSKFRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
Protein: Keratin, type I cuticular Ha3-I (Hair keratin, type I Ha3-I) (Keratin-33A) (K33A) (O76009)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type I cuticular Ha1
- Keratin, type I cuticular Ha3-II
- Keratin, type I cuticular Ha4
Sequence:
MSYSCGLPSLSCRTSCSSRPCVPPSCHGCTLPGACNIPANVSNCNWFCEGSFNGSEKETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLVCASYQSYFKTIEELQQKILCSKSENARLVVQIDNAKLASDDFRTKYETELSLRQLVESDINGLRRILDELTLCRSDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNVEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCKLPSNPCATTNACDKSTGPCISNPCGLRARCGPCNTFGY
Protein: Polypyrimidine tract-binding protein 2 (Neural polypyrimidine tract-binding protein) (PTB-like protein) (Q66H20)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q91Z31}.
Interaction partners:
- RNA-binding protein Nova-1
- NOVA alternative splicing regulator 2
- Serine/arginine-rich splicing factor 1
- Splicing factor proline and glutamine-rich.
- Transformer-2 protein homolog beta
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
Sequence:
MDGIVTEVAVGVKRGSDELLSGSVLSSPNSNMSGMVVTANGNDSKKFKGEDKMDGAPSRVLHIRKLPGEVTETEVIALGLPFGKVTNILMLKGKNQAFLELATEEAAITMVNYYSAVTPHLRNQPIYIQYSNHKELKTDNTLNQRAQVVLQAVTAVQTANTPLSGTTVSESAVTPAQSPVLRIIIDNMYYPVTLDVLHQIFSKFGAVLKIITFTKNNQFQALLQYGDPVNAQQAKLALDGQNIYNACCTLRIDFSKLVNLNVKYNNDKSRDYTRPDLPSGDGQPALDPAIAAAFAKETSLLAVPGALSPLAIPNAAAAAAAAAAGRVGMPGVSAGGNTVLLVSNLNEEMVTPQSLFTLFGVYGDVQRVKILYNKKDSALIQMADGNQSQLAMNHLNGQKMYGKIIRVTLSKHQTVQLPREGLDDQGLTKDFGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVAEEDLRTLFANTGGTVKAFKFFQDHKMALLQMATVEEAIQALIDLHNYNLGENHHLRVSFSKSTI
Protein: Prostaglandin E receptor 2b (subtype EP2) (Prostaglandin E receptor 2b subtype EP2) (Q5RI92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Magnesium transporter
Sequence:
MASQNVSCREQISVSGGSPTIPAFMFSTGVLGNVVALILLEMRRRKQPASLFHVLVSSLVITDLLGTFSLSPLVLTAYFRNASLLGMNENRLACGHFAYAMTFFSVVTLAILLSMAVERWLSIGHPFFYEKYSSKRCGYITIALIYLLCALFCVTPFLGFGKYVQYCPGTWCFIDMDPSASEHKAFNIIYASCLLLMIVCTVLCNASVIYHISRMYRRLKAHRSSVRRQRGHKRHRSMTKEVEHLVLLWFMTIAFVFCSLPLVIQVYHNTLYHRDRHRNNVIPLLFLSANPIIDPWVFIILSPPVPRLLWDKICKAAKSKPIREKVHSIHPVLYHSSPPAD
Protein: Large ribosomal subunit protein uL15B (60S ribosomal protein L28-B) (P57728)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS14
Sequence:
MPTHTSKTRKLRGHVSAGHGRIGKHRKHPGGRGKAGGLQHLRSHFDKYHPGYFGKVGMRRFHLMKNPLWRPTVNLDRLWTLVPNETREKYLGKNTEVAPVINVLQSGYGKVLGKGRLPDTPVIIQTRYVSRRAEEKIKQAGGVVELIA
Protein: Required for respiratory growth protein 9, mitochondrial (O14211)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNIFNYTTLIFRRLSSTFKASNKASIEWKKQNIAVKRKIGGYWNPKKKLPLESMDEIRRLKKEKSSMSCSELAKLYGVSPESIRRILKSSNRPLDDREKSRKEKRWLNSLKSNRDFA
Protein: Sarcoplasmic reticulum histidine-rich calcium-binding protein (P23327)
Organism: Homo sapiens (Human)
Function: May play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle.
Subcellular location: Sarcoplasmic reticulum lumen.
Interaction partners:
- Triadin
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Sulfotransferase 2A1
Sequence:
MGHHRPWLHASVLWAGVASLLLPPAMTQQLRGDGLGFRNRNNSTGVAGLSEEASAELRHHLHSPRDHPDENKDVSTENGHHFWSHPDREKEDEDVSKEYGHLLPGHRSQDHKVGDEGVSGEEVFAEHGGQARGHRGHGSEDTEDSAEHRHHLPSHRSHSHQDEDEDEVVSSEHHHHILRHGHRGHDGEDDEGEEEEEEEEEEEEASTEYGHQAHRHRGHGSEEDEDVSDGHHHHGPSHRHQGHEEDDDDDDDDDDDDDDDDVSIEYRHQAHRHQGHGIEEDEDVSDGHHHRDPSHRHRSHEEDDNDDDDVSTEYGHQAHRHQDHRKEEVEAVSGEHHHHVPDHRHQGHRDEEEDEDVSTERWHQGPQHVHHGLVDEEEEEEEITVQFGHYVASHQPRGHKSDEEDFQDEYKTEVPHHHHHRVPREEDEEVSAELGHQAPSHRQSHQDEETGHGQRGSIKEMSHHPPGHTVVKDRSHLRKDDSEEEKEKEEDPGSHEEDDESSEQGEKGTHHGSRDQEDEEDEEEGHGLSLNQEEEEEEDKEEEEEEEDEERREERAEVGAPLSPDHSEEEEEEEEGLEEDEPRFTIIPNPLDRREEAGGASSEEESGEDTGPQDAQEYGNYQPGSLCGYCSFCNRCTECESCHCDEENMGEHCDQCQHCQFCYLCPLVCETVCAPGSYVDYFSSSLYQALADMLETPEP
Protein: Probable phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) (AtCoaC2) (Halotolerance protein Hal3b) (AtHal3b) (P94063)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant growth and salt and osmotic tolerance. Catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine, a key step in coenzyme A biosynthesis. The enzyme is also able to decarboxylate pantothenoylcysteine to pantothenoylcysteamine.
Interaction partners:
- Phosphopantetheine adenylyltransferase
- Phosphopantothenate--cysteine ligase 1
- Pantothenate kinase 2
- Pantothenate kinase 1
- Phosphopantothenoylcysteine decarboxylase
- Alkaline-phosphatase-like family protein
- FAD/NAD
- T1B9.12 protein
- Cytochrome c-1
- Dephospho-CoA kinase
Sequence:
MNMEVDTVTRKPRILLAASGSVASIKFSNLCHCFSEWAEVKAVASKSSLNFVDKPSLPQNVTLYTDEDEWSSWNKIGDPVLHIELRRWADVMIIAPLSANTLAKIAGGLCDNLLTCIVRAWDYSKPLFVAPAMNTLMWNNPFTERHLVLLDELGITLIPPIKKKLACGDYGNGAMAEPSLIYSTVRLFWESQARKQRDGTS
Protein: Col6a2 protein (Q5EB88)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
EKFIDDMEDVLCPDPQIVCPELPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFYKARRFVEEVSRRLTLARRDDDPLNARMALLQYGSQNQQQVAFPLTYNVTTIHEALERTTYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFVFLTDGVTGNDSLEESVHSMRKQNVVPTVVAVGGDVDMDVLTKISLGDRAAIFREKDFDSLAQPSFFDRFIRWIC
Protein: Rifin (O96112)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILEHNKNEPHTTPHHPPNTRLLCECELYSPANYDSDPEMKRVMQQFVDRTTQRFHEYDERMKTTRQKCKDKCDKEIQNIILKDKLEKQMEQQLTTLETKIDTNDIPTCVCEKSLADKTEKFCLNCGVQLGGGVLQASGLLGGIGQLGLDAWKAAALVTAKELAEKAGAAKGLAEGNAHGMKIVIHHLKELHIDKLVPGICEKISSTGHYANITNFANTIIQQRGTMCGASGKNLGKDMCTKISIKLGTLKPDGIRPGLPDKDAVTKVLNGLVEQADKAAAHVTKTTSESVTAAIKARETALIEGRFESSITSINASIIAIIVIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (15-PGDH) (EC 1.1.1.141) (Eicosanoid/docosanoid dehydrogenase [NAD(+)]) (EC 1.1.1.-, EC 1.1.1.232) (Prostaglandin dehydrogenase 1) (Short chain dehydrogenase/reductase family 36C member 1) (P15428)
Organism: Homo sapiens (Human)
Function: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
Subcellular location: Cytoplasm.
Interaction partners:
- 11-beta-hydroxysteroid dehydrogenase type 2
- 11-beta-hydroxysteroid dehydrogenase 1
- Solute carrier organic anion transporter family member 2A1
- Prostaglandin E synthase
Sequence:
MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ
Protein: EARP and GARP complex-interacting protein 1 (Endosome-associated recycling protein-interacting protein) (Golgi-associated retrograde protein-interacting protein) (Tumor-suppressing STF cDNA 1 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 1 protein) (Q53HC9)
Organism: Homo sapiens (Human)
Function: Acts as a component of endosomal retrieval machinery that is involved in protein transport from early endosomes to either recycling endosomes or the trans-Golgi network. Mediates the recruitment of Golgi-associated retrograde protein (GARP) complex to the trans-Golgi network and controls early endosome-to-Golgi transport of internalized protein. Promotes the recycling of internalized transferrin receptor (TFRC) to the plasma membrane through interaction with endosome-associated recycling protein (EARP) complex. Controls proper insulin distribution and secretion, and retention of cargo in mature dense core vesicles (By similarity). Required for the stability of the endosome-associated retrograde protein (EARP) complex subunits and for proper localization and association of EARP with membranes (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:27440922}.
Interaction partners:
- Syndetin
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Coiled-coil domain-containing protein 186
Sequence:
MEDDAPVIYGLEFQARALTPQTAETDAIRFLVGTQSLKYDNQIHIIDFDDENNIINKNVLLHQAGEIWHISASPADRGVLTTCYNRTSDSKVLTCAAVWRMPKELESGSHESPDDSSSTAQTLELLCHLDNTAHGNMACVVWEPMGDGKKIISLADNHILLWDLQESSSQAVLASSASLEGKGQLKFTSGRWSPHHNCTQVATANDTTLRGWDTRSMSQIYCIENAHGQLVRDLDFNPNKQYYLASCGDDCKVKFWDTRNVTEPVKTLEEHSHWVWNVRYNHSHDQLVLTGSSDSRVILSNMVSISSEPFGHLVDDDDISDQEDHRSEEKSKEPLQDNVIATYEEHEDSVYAVDWSSADPWLFASLSYDGRLVINRVPRALKYHILL
Protein: Immunoglobulin kappa constant (Ig kappa chain C region MOPC 21) (P01837)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
Protein: 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) (p31) (P48556)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit beta type-2
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 5
- 26S proteasome non-ATPase regulatory subunit 13
Sequence:
MFIKGRAPRAPPRERRRATRGGLRQVVAPPRALGSTSRPHFRRASVCRRRCRKSGGLLAASRKMAAAAVNGAAGFSSSGPAATSGAVLQAATGMYEQLKGEWNRKSPNLSKCGEELGRLKLVLLELNFLPTTGTKLTKQQLILARDILEIGAQWSILRKDIPSFERYMAQLKCYYFDYKEQLPESAYMHQLLGLNLLFLLSQNRVAEFHTELERLPAKDIQTNVYIKHPVSLEQYLMEGSYNKVFLAKGNIPAESYTFFIDILLDTIRDEIAGCIEKAYEKILFTEATRILFFNTPKKMTDYAKKRGWVLGPNNYYSFASQQQKPEDTTIPSTELAKQVIEYARQLEMIV
Protein: PDS5 cohesin associated factor B (A9IYQ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
IKQTKDAQGPDDAKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTTNVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSSEMDHSENEDYTMSSPLPGKKSDKRDDSDLSELEKPRGRKKTPVTEQEEKLGMDDLTKLVQEQKPKGSQRSRKRGHTASESDEQQWPEEKRLKEDILENEDEQNSPPKKGKRGRPPKPLGGGTPKEEPTMKTSKKGSKKKSGPPAPEEEEEEERQSGNTEQKSKSKQHRVSR
Protein: Zinc finger protein GFI1 homolog pag-3 (Pattern of reporter gene expression abnormal protein 3) (Transcription factor pag-3) (G5EDE1)
Organism: Caenorhabditis elegans
Function: Transcription factor. Plays a role in the determination of neuroblast cell fate and neuronal differentiation. Negatively modulates expression of several components of dense-core vesicles (DCVs), thereby, in a DCV membrane protein ida-1-dependent manner, regulating neurosecretion. Negatively modulates the transcription of its own gene, the mechanosensory gene mec-3, and also other touch neuron-specific genes in the BDU neurons; required for coordinated movement. Required to determine the identity of BDU sensory neurons in concert with transcription factor unc-86, regulating expression of a number of genes, including transcription factors ceh-14 and ahr-1, neuropeptides flp-10, nlp-1 and nlp-15, and tyramine receptor-encoding ser-2. Acts in concert with non-canonical WNT signaling to negatively modulate transcription of mec-3 gene in BDU neurons. May act in concert with transcription factor unc-3 in motor neuron fate determination. May play a role programmed cell death.
Subcellular location: Nucleus {ECO:0000269|PubMed:9169852}. Cell projection, axon {ECO:0000269|PubMed:9169852}. Perikaryon {ECO:0000269|PubMed:9169852}.
Interaction partners:
- ET module
- Transcription factor unc-3
- Transcription factor unc-86
- Mechanosensory protein 3
Sequence:
MSTEHVSNVYSVESLLSNVEKSSVSPTESIEDRNEFMITEDVMSSWQRMAATISLQQKLLMMQQTMPRPPPVNILGNFPFGFLNAPMFWQQYLRSMAMGIIPQNPESPSASVWNRTPTPPVEIKPFHCQKCTKLFSTIAALEQHQQVHVSDKQFECKQCGKTFKRSSTLSTHLLIHSDTRPYPCEYCGKRFHQKSDMKKHTYIHTGEKPHKCTVCGKAFSQSSNLITHTRKHTGFKPFACDVCGRTFQRKVDRRRHRESHHPGHPEECVSASQISSDLSPKGYMTPPTSNGYLDSSDEFLNVFRLPAELLAIKAEMGEEMEEADDEEEKVLNLSVS
Protein: RNA binding protein (Q54WA7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable serine/threonine-protein kinase yakA
- Cytochrome c oxidase copper chaperone
- C2 domain-containing protein
Sequence:
QQQQQHHHHHHHQQSHQQQQQQQSQHQQRSSIHHQQPPQYGIYSSLQQQQFQNGGNGYRGQINTNDFYINEQQQLQQQQQQQHHHHQQPPQHHQQQQHAQKPYITSIHNGHQVGVSQQTHMVPQQQQQTTSLHHQHPQQIREFQPKRKPLTNNTVSQSPPQPVNIINNHTQYNSNNNNNNNNNNQYYSSSPQQNIGLSPNSLSPSMIQQHHHHQQQQHHHHHQHHHQQQHHNQHPVVTLSSSPTSSSLSHSPSTIVTLNNNNSNSNINSNITNNATGNNGGMNKPVSINLNTSTHSSPNSQSSPNTPNSLSTPTPLSASTVVANNNNGNFNDSANGNGLKPVEINQTLSPSSTIVANAPAPNVVLSNNSTNSVVSSSSPPPTTSSPSSLSSSSLSSAATTTTTTTTTTTATATQSTTPPPPPVTSTPSSPTQQQTNEYTTRSQLLEDFRNLKMKLELSDIKGHIAEFSKDQVGSRIIQQKIENASLEEKQLVFDEVVVAVHSLMTDVFGNYVLQKFFEHGTTEQKRILADKLSGHILSLTLQMYGCRVIQKAIESIELDKQILLIGELNGHIVQCVTDQNGNHVIQKCIEKIPTHLIQFIIDSFHGHIYQLATHPYGCRVIQRILEHCAEKQVAPILDELMRCAVSLVQDQYGNYVIQHVLENGTPRDKSAIVCKLQGQIYNLSQHKFASNVIEKCVQHGCTAERILIINEILGDANSPNSSNVLLKILKDPYANYVIQKILDIVEPAQRDMIINRIQPFVPTLKKVTPGKHIISRIEKYSANNN
Protein: Metallophosphoesterase 1 (Post-GPI attachment to proteins factor 5) (K7ES91)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00004457}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004457}. Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004257}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004257}.
Interaction partners:
Sequence:
MAMIELGFGRQNFHPLKRKSSLLLKLIAVVFAVLLFCEFLIYYLAIFQCNWPEVKTTASDGEQTTREPVLKAMFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLKVVAGNHDIGFHYEMNTYKVERFEKVFSSERLFSWKGINFVMVNSVALNGDGCGICSETEAELIEVSHRLNCSREARGSSRCGPGPLLPTSAPVLLQHYPLYRRSDANCSGEDAAPAEERDIPFKENYDVLSREASQKLLWWLQPRLVLSGHTHSAC