wanglab/gogpt-training-data huggingface dataset:
Protein: Rhodopsin kinase GRK1 (RK) (EC 2.7.11.14) (G protein-coupled receptor kinase 1) (Q63651)
Organism: Rattus norvegicus (Rat)
Function: Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade (By similarity). This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination (By similarity). May play a role in the maintenance of the outer nuclear layer in the retina (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P28327}; Lipid-anchor {ECO:0000250|UniProtKB:P28327}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9WVL4}. Note=Subcellular location is not affected by light or dark conditions. {ECO:0000250|UniProtKB:Q9WVL4}.
Interaction partners:
- Rhodopsin
- Recoverin
- Beta-arrestin-1
- Beta-arrestin-2
- S-arrestin
- Neuronal calcium sensor 1
- G protein subunit alpha transducin 1
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Guanylyl cyclase-activating protein 1
- C-X-C chemokine receptor type 2
Sequence:
MDFGSLETVVANSAFIAARGSFDGSSTPSSRDKKYLAKLRLPPLSKCEGLRDSISLEFDNLCSEQPIGKRLFQQFLKTDERHVPALELWKDIEDYDTADDDLRPQKAQAILAEYLDPQGTLFCNFLDQGMVARVKEGPTGSQDGLFQPLLQATLEHLSQGPFQEYLGSLYFLRFLQWKWLEAQPIGEDWFLDFRVLGKGGFGEVSACQMKATGKMYACKKLNKKRLKKRKGYQGAIVEKRILAKVHSRFIVSLAYAFETKTDLCLVMTIMNGGDVRYHIYNVDEENPGFPEPRAIYYTAQIISGLEHLHQRRIVYRDLKPENVLLDNDGNIRISDLGLAVELKEGQNKTKGYAGTPGFMAPELLRGEEYDFSVDYFALGVTLYEMIAARGPFRARGEKVENKELKQRIISEPVKYPEKFSQASKDFCEQLLEKDPEKRLGFRDGTCDALRANVLFKDISWRQLEAGMLIPPFIPDSRTVYAKNIQDVGAFSTVKGVVFDKADTEFFQEFASGNCSIPWQEEMIETGFFGDLNVWRPDGQMPDDMKGITVEEAAPTAKSGMCLIS
Protein: Carbohydrate sulfotransferase 9 (EC 2.8.2.-) (GalNAc-4-O-sulfotransferase 2) (GalNAc-4-ST2) (GalNAc4ST-2) (N-acetylgalactosamine-4-O-sulfotransferase 2) (Q7L1S5)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin.
Subcellular location: [Isoform 1]: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Beta-1,4-N-acetylgalactosaminyltransferase 3
- N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1
- Carbohydrate sulfotransferase 8
- Carbonic anhydrase 6
Sequence:
MQPSEMVMNPKQVFLSVLIFGVAGLLLFMYLQVWIEEQHTGRVEKRREQKVTSGWGPVKYLRPVPRIMSTEKIQEHITNQNPKFHMPEDVREKKENLLLNSERSTRLLTKTSHSQGGDQALSKSTGSPTEKLIEKRQGAKTVFNKFSNMNWPVDIHPLNKSLVKDNKWKKTEETQEKRRSFLQEFCKKYGGVSHHQSHLFHTVSRIYVEDKHKILYCEVPKAGCSNWKRILMVLNGLASSAYNISHNAVHYGKHLKKLDSFDLKGIYTRLNTYTKAVFVRDPMERLVSAFRDKFEHPNSYYHPVFGKAIIKKYRPNACEEALINGSGVKFKEFIHYLLDSHRPVGMDIHWEKVSKLCYPCLINYDFVGKFETLEEDANYFLQMIGAPKELKFPNFKDRHSSDERTNAQVVRQYLKDLTRTERQLIYDFYYLDYLMFNYTTPFL
Protein: Kinetoplast ribosomal PPR-repeat containing protein 3 (Q583F7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVLAEVCSVSWRRFAVLKAPVWKRFPIAEKRLCVSSWGNRIGVSAEANHLRPLQRGKTVRVKPFKQVKHRELRADKELLPQNEALNEHIIRSAGGSQAAARSAAEASCIGEDKAESGNARLVQHDPATVVTLDSQREELHLDRSQRELLWNARRRQYQQLLVRIVTCMESHLAPIEKCHVLLALHDEVIDKRIRLRVDTYEDIFHVFYAVGTLGSSSPSLDAEEVAGRTAKAAPSLLPAEFVSPIIAAASLLTGPMLQSLWRVYRYMIDSGTNPTSRVVQHVMGILERHRKKDVVVEARAHSLMMDLDRFHLAPTEYTIASYIGVCDVNAVMHLAVARVTDYRTRHERQVSAGVCARLLFGLMHNQQHDEALACLSSIDSTVITPQLLNAALHVTCHSRDPLSAFAIYKSVMGRPGGRASGMAPSEHTFTILLEAMEKAQSYGELNYFLREMRRFRVKGNGVTLNKILRVLLKLNRYEEASALLVTMDKKGVTVFDELRQEYATAVRAPLREEMCKITEDANAATGR
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Q6FHV6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
Protein: T. brucei spp.-specific protein (Q383I7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWLFFGTLCRGALVVLLTFLLYFDSSRLPTPDYVAGEMCNMLERHAECSSCQKLLSHFDVDGKGDESPIWQTLRRLDKPRMPAVQPCDGKTRSVECNHFLENSLIEKWSMVSALVHEMKKFYATTDPDAVGIVNTRHDELVEFILNEREARESEQRELQKWEDCSSIVDVESDTSELSTNKLRRHTYESSACSISFSNDRQRSFCWCHCAGKLPFMERTRIWLLHIYLSYDMRMKIIILQHQRNTLFCLLLELCLLGIVMRHQTVEAAVEVAGAVHPTNGKLSNELTDVFMSQVHTGKSTTRRVAPPRLRGSSHRKD
Protein: Mitotic spindle assembly checkpoint protein MAD2B (Mitotic arrest deficient 2-like protein 2) (MAD2-like protein 2) (Q4KWZ6)
Organism: Gallus gallus (Chicken)
Function: Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also play a role in signal transduction in response to DNA damage. May regulate the activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection (By similarity). Through transcriptional regulation may play a role in epithelial-mesenchymal transdifferentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UI95}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UI95}. Cytoplasm {ECO:0000250|UniProtKB:Q9UI95}. Chromosome {ECO:0000250|UniProtKB:Q9UI95}.
Interaction partners:
- Shieldin complex subunit 2.
- DNA repair protein REV1
- REV3 like, DNA directed polymerase zeta catalytic subunit.
- Shieldin complex subunit 1.
- Shieldin complex subunit 3
- Mitotic spindle assembly checkpoint protein MAD2A
- DNA polymerase kappa
- DNA polymerase delta subunit 3
- Pachytene checkpoint protein 2 homolog
- Uncharacterized protein.
Sequence:
MTTLTRQDLNFGQVVADVLSEFLEVAVHLILYVREVYPIGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHHPVERFVFEITQPPLLSISSESLLSHVEQLLRAFILKISVCDAVLDNNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGT
Protein: Zgc:172049 (A8WFZ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLCSDQNFDIAQVIRFFRSKPGELAIYYELESGEKSYSRGIVKVCPNTHRVTRFLEKPQEGVTASRLASVVFYCLRKESLTYISEFLNKHPDVKDRTFGKFWEWLVNEEKVPVYGMKLPTGFQLIGQVGLSDYTKWLAHYSSKQQLSPSKPITCRSYARVGLMGNPSDGFNGKTIAMSISNFWAEVTLMESQTLVLLPHPLNDPTEFGGLQDLFRISRKEGYLGGLRLLQATCKKFYQFCSEQGIALSKQNFTLKYDTNIPRQVGLAGSSAIVSATLKCLMKFYNITDNDLPQPVRANFILNVETDELFITAGLQDRVVQVYEGLVYMDFSKQLMDERGYGEYIPLDMRDLPMFWLAYLSDPSDSGRIHSNVRQRWLNGEPAVVEAMKSFAELTDQSRAAFQCKDWARLAQLMDENFELRRSVYTDDCLGPGNLKMVQLARQFGSAVKLPGSGGAVVGLCMDQERLMEMKRAFQEAGCVFCLIVPYDPSVQGQN
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (Q05G10)
Organism: Mycoplasma suis
Interaction partners:
Sequence:
MTIHKVAINGFGRIGRLLFRNLLSSQGVQVVAVNDVVDIKVLTHLLVYDSAQGKLKDWEVSCDSEYIRLKNVNTGEVREVRVFNFNTEKIYHWGELEIDCVVECSGRFLTKEAVKCHLDAGAQKVLISAPAKDDTKTVVYNVNHTQITSSDNVISGASCTTNALAPIVKIIHRKFGINSGFMTTVHAFTSDQRLQDSPHSDLRRARAAAGSIIPTTTGAAAAIGRVIPELNGKLDGIAHRVPVLTGSLVDLCLKINKSVSAEEINEAIKDGENETLAYVEDPIVSADIIGDTHGSVFDSSLTKVLPTGEVKLYAWYDNESSYVNQLARTLKYYISL
Protein: N-terminal acetyltransferase A complex catalytic subunit ard1 (NatA complex subunit ARD1) (EC 2.3.1.255) (Q9UTI3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-terminal acetyltransferase A complex subunit nat1
- Uncharacterized N-acetyltransferase C663.13c
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase A complex subunit-like protein C418.02
- N-terminal acetyltransferase B complex subunit arm1
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Pre-mRNA-splicing factor cwf24
- N-alpha-acetyltransferase 40
- N-terminal acetyltransferase B complex catalytic subunit naa20
Sequence:
MDIRPARISDLTGMQNCNLHNLPENYQLKYYLYHAISWPMLSYVATDPKGRVVGYVLAKMEEEPKDGIPHGHITSVSVMRSYRHLGLAKRLMVQSQRAMVEVYGAKYMSLHVRKSNRAAIHLYRDTLQFDVQGIESKYYADGEDAYAMHKDFSTLKFDTPETNDELAKTVQSLALNN
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (Q6P8L2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALEAVGKSENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDQKKKKKKKKK
Protein: Protein cereblon (zcrbn) (Q68EH9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 (Probable). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus {ECO:0000250|UniProtKB:Q96SW2}.
Interaction partners:
- Damage-specific DNA-binding protein 1.
- Cullin 4A
- Cullin-4B
- E3 ubiquitin-protein ligase RBX1
- Casein kinase I isoform alpha
- E3 ubiquitin-protein ligase ZFP91
- IKAROS family zinc finger 1
- Spalt-like transcription factor 4.
- Bromodomain-containing protein 4
- Zinc finger protein 692.
Sequence:
MGNQLQLLPENEEEEEDDMETEDRDGEDVEKPSIINFDTSLPTSHAYLGSDMEEFHGRTLHDEDSVQNLPVLPHVALILIPGQTLPLQLFRPQEVSMFRNLVSQDRTFAVLAHSPDPSGTETKAEFGTTAEIYAFREEQEYGIETVKIKAVGRQRFRVHDIRTQADGIRQAKVQILPERILPDPLCALQFLPRLHTHSPQTKHTQTTPPQKRCSQNYRQKKLHCASMTSWPPWVYSLYDSKTLMSRVKKQLHEWDENLKDESLPTNPTDFSYRVAACLPIDDALRLQLLKIGSAIQRLRCELDIMDRCTSLCCKQCQDTEITSKNEIFSLSLYGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTLHSWFPGYAWTIAQCRTCSSHMGWKFSAVKKDLSPPRFWGLTRSALLPTIPQGEEGVEGSRLLCL
Protein: Coexpressed With Polycystins (B6VQ88)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTPTSTTTCAYIKTSSSGLVFDSCSIDANVLCDRPLQKQDYCSIIANCSSTTTFLSTTTPVSSTTSNISLTSSSTQSYSSSTAGATSSLFTIKVTQSTTAAGNGQGGSGSGSATTTCKCSAGDVSATTAASACSEKSGCLKNQWKIFGMCVDWRAMLALLLIGLLLFLCCCICHCCMHACMFCTPGKREKEIRDPILPNRSVVAPIPIVAPGKMDYDVEKSEAVILPPPAIQPEPVYITVPEKHESVYGFHTKEIIHVMPEKPTTREIGTMTDPMDTELSTIMPVPVAAPVMKRKKVVKKPKKMFIPATEDPIEEDLAADIPIEMPESPGARSVAPLGDVVEPAPMIPLNFSRNPKPMMPEPQSHDDIPLPVNKSRNTVPPPVMQQKPNNASNNEEFDPSGLRSPPIPAGKPNNGTPKRMTFSPIADESEEENGARIPSPPRERRASGGRPGNNDGPNLSPNAALDPHPTLKNQRLNEMPSPTPANAPVPSKSPVSGASNNPFANLGGPSPAPAADGAGRAPQDDVGMRAARGRLGGAVRGGGGGGEAPNGWKPWAKGGARR
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q7ZV29)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSLSNKLHLDKVDVKGKRVIMRVDFNVPMKNNVITNNQRIKAAVPSIQHCLDNCAKAVALMSHLGRPDGVPMPDKYSLEPVAAELKNLLGKDVQFLKDCVGPDVEKACADPPAGSVILLENLRFHVAEEGKGKDASGNKTKASQAEIDAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAAGFLMKKELDYFAMALEKPQRPFLAILGGAKVKDKIQLINNMLDKVNEMIIGGGMAFTFLKVLKNMEIGTSLFDEEGSTIVKDLMAKAEKNGVKITLPVDFITADKFDEKATTGTATVAEGIPAGWMGLDCGPESSKLYAEAVARAKQIVWNGPVGVFEWDNFAHGTKNMMDKVVEATKNGCITIIGGGDTATCCAKWDTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV
Protein: A kinase anchor protein 200, isoform D (A kinase anchor protein 200, isoform G) (Q86BM5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGKAQSKRSIDITTDPKKVGEGDEVAGKVEKIDVDQKTDAPAVNGDAATPKEGGDEAAAVEKKETEEHSENDKDLTTEKSAAVAEGGDAVAETAKGEEGSPKEAAAGEDITPLADESIKSKSKKDKVKKKWSFRSISFGKKDKQKPAKSEEATSPTSGTTSPTTAEAEAAPAGDAAVAEPSVATNGEAEKPAETATATSEPASKDEKPAENGSATEQEKQANGETEKAAPAPSTVEEAAKPKPAEEPATVTATESNTTATEEVPVKESQPEPEVVTNGHGAGEALTNGSSNGLAESPVTETAPVADNIPSNVDDEPPHQNGTNGTTTPPPTPVATEIEKGQQIEVNNHTRTDNTTQHNSKNITVNTSTTTTKTTEITENTALKTISTDTERTCTSTVTETVVAAAELVQTQTILTKTTNTILPTSHTQASSEVIETVTPSQAEEEVVAAIIKAVSSEPEAETETETEAEGFVLVAPVSTEVEVPVSISPIEPVAEVSQVKIEPLVEIPEVEAKSVADVSEADTESVPKVSELKTEVSEIEFESVIVETRSSSPPPPLPKSPPPSRVSAFVLSEDVIEEQVTPNVPEVNDVKPDEIEQQAISIVAEITEQAAEIVTEQEKQQEEAKVDSVPETIEESSSTVVVEEVLPVQNDEVTAPSPTPDDVQKPIEDQDTPDEKESYPVPDPIDPAAVNDEVAVTEAVDCEVEKETGSISSNVAESSSVSDEQAAIENQVEILEEQTVAVEETTEQETSDQQVISEEAHSDNDKENEIDLVENIISDLDAPITKAGGDLLVELDARSAEQEGESNNKVDLAKDLKEKNAAAADVTTQEQLPVTCE
Protein: Spermidine synthase (Q57X26)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAFATSPGQRPQKQYINKFTAFFFREVDRGFSSPYVVFSTGTVLALAGWKFFKRRVEPERQINAVLRQPRSRVPLSDAHNVFWGFRTNSGTDNTSPRSLGEAMSEDMEEALRRPRLLHSEPSELQDSRTESSGGTQANVACMELQEYDPQYGDDVVFRSVHYIYSERDGSTSQVDNKTEEVVEKGEDSSYLSRMPGHGLSVIHGMVKCKFVTAQNNCVPYAGHLESEYARKMMLALGPVHILRDIARTSFPIRFTTVKETPVSTLVCGLHSGEAPRWLSNAFPNFQIDVVERDGALVRVCRRFMGLQESSNLRLFIADPVDFLRRNALVDVSSGKRYDLIMIDTLDGAGRLSTQYGRLEFINSVRNSLSPAGCVVAALPNRDAAFLYHMVQNWRLAFAGRTVLLVHCVTSPHTMLITFQDDAERGRANFGSVGGVDEFKDLLRTKISHYGVKRIPFDLPAEVSRDNFRVLHPGKTYQMDAYLPSGHPQLRSIAEGNFVFGGASNGGSWTEWLRRLGGSWLTPTQRTDLKWMEK
Protein: EG:BACR25B3.10 protein (Q9NEG0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MFLATLDTNDPTDIGTEDPVLTQIIVSIQKPEITIVPVGGSMTLSCSGRMRWSNSPVIVNWYKENSRLPENVEVQGGNLYLYDLQVSDSGVYICQAVNNETASVFKDTVSITITKKDQLSPAEIVNLPSHVTFEEYVNNEIICEVLGNPAPRVTWARVDGHADAQSTRTYDNRLIFDSPRKSDEGRYRCQAENDQNRDEKYVIVYVQSNPPQPPPQQDRLYITPEEINGLAGESFQLNCQFTSVASLRYDWSHNGRSLSSSPARNVEIRGNTLEVRDASESDSGVYTCVAYDVRTRRNFTESARVNIDRREEQPFGVLMRMMILTDSLINHSNKPIIESLEQNILIIQGEDYSITCEASGSPYPSIKWAKVHDFMPENVHISGNVLTIYGARFENRGVYSCVAENDHGSDLSSTSIDIEPRERPSVKIVSAPLQTFSVGAPASLYCTVEGIPDPTVEWVRVDGQPLSPRHKIQSPGYMVIDDIQLEDSGDYECRAKNIVGEATGVATITVQEPTLVQIIPDNRDLRLTEGDELSLTCVGSGVPNPEVEWVNEMALKRDLYSPPSNTAILKIYRVTKADAGIYTCHGKNEAGSDEAHVRVEVQERRGDIGGVDDDSDRDPINYNPPQQQNPGIHQPGSNQLLATDIGDNVTLTCDMFQPLNTRWERVDGAPLPRNAYTIKNRLEIVRVEQQNLGQYRCNGIGRDGNVKTYFVKELVLMPLPRIRFYPNIPLTVEAGQNLDVHCQVENVRPEDVHWSTDNNRPLPSSVRIVGSVLRFVSITQAAAGEYRCSAFNQYGNRSQIARVAVKKPADFHQVPQSQLQRHREGENIQLQCTVTDQYGVRAQDNVEFNWFRDDRRPLPNNARTDSQILVLTNLRPEDAGRYICNSYDVDRGQQLPEVSIDLQVLSE
Protein: Large ribosomal subunit protein bL33c (50S ribosomal protein L33, chloroplastic) (P0C457)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein bS16c
- Large ribosomal subunit protein uL14c
- Large ribosomal subunit protein bL36c
- Os01g0278900 protein
- Large ribosomal subunit protein bL32c
- Large ribosomal subunit protein bL20c
- Small ribosomal subunit protein uS14c
- DNA-directed RNA polymerase subunit alpha
- Small ribosomal subunit protein bS18c
- Small ribosomal subunit protein uS11c
Sequence:
MAKGKDVRIRVILQCVSCVRKGANEESAGISRYSTQKNRHNTPGQLELRKFCRYCRKHTIHAEIKK
Protein: Vacuolar protein sorting-associated protein 52 homolog (Q9VMQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 54
- FI23003p1
- Ras-related protein Rab6
- HL02043p
- Conserved oligomeric Golgi complex subunit 8
- Syntaxin 16
- Protein hedgehog
- ADP-ribosylation factor-like 5
Sequence:
MAEVPSPQMTEQLDNEEVREILKNTTDLRQYSRQIEKEFKEVENKSIEDYIAESQNIANLHNQINDCDDVLERMENMLMSFQSVLNNISTEITQLQRKSVSMSLQLTNRQSVKAQLSQFIEDMAVSEEMINIIMETPVTERDFSTQLNVLNHKLSLVKELSFKESKSTSDVSDVLQKLRLKAMAKIRSYLLEQIYKFRKPMTNYQIPQNAMLKHKFFFEFILSNERHVAQEICSEYIDTMGKIYYSYFKSYSTRLTSLKFEESCTKDDLMGIEDNASKGLFSKTTSLKHKSTIFTIGKRGDILNQQLEAPIIVPHAQLKNRYTAEALFRSEQYALVDNACREYLFVTEFFMVRGTQAQDLFNQIMGKTLTLMIKNLETSIHDCFDTIAMFLCIHLIFRYQLMCHKRCVPALDKYWDSLQAVIWPRFELVFRLNIQSIHDCDPTKFNKELGPHYITRRYAEFSAAIVGISEHFPNELVSRLLLELQNEVECFILRMAAIFPTRKDQLIYLINNYDLVLGVLMEHTRDNSKEAEAFREQLNSRSAEYVEEILAPHFGGIIQFVKECEHFFEKEQMDELRKQERRSLALVASFSANWKKSLEELNREVLLSFPSLLTGSQLLQLALASLVQYYHRFHKLLTPNARAQLTNIHVVMVEIKKYKSNY
Protein: Protein SSO1 (P32867)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vesicle fusion with the plasma membrane.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Protein transport protein SEC1
- Synaptobrevin homolog 2
- Synaptobrevin homolog 1
- Protein transport protein SEC9
- Sporulation-specific protein 20
- Protein transport protein SEC22
- Protein MSO1
- Alpha-soluble NSF attachment protein
- Synaptobrevin homolog YKT6
- Vacuolar v-SNARE NYV1
Sequence:
MSYNNPYQLETPFEESYELDEGSSAIGAEGHDFVGFMNKISQINRDLDKYDHTINQVDSLHKRLLTEVNEEQASHLRHSLDNFVAQATDLQFKLKNEIKSAQRDGIHDTNKQAQAENSRQRFLKLIQDYRIVDSNYKEENKEQAKRQYMIIQPEATEDEVEAAISDVGGQQIFSQALLNANRRGEAKTALAEVQARHQELLKLEKSMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQLDVEQGVGHTDKAVKSARKARKNKIRCWLIVFAIIVVVVVVVVVPAVVKTR
Protein: Peptidase S1 domain-containing protein (Q9VEM7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peptidase S1 domain-containing protein
- FI19613p1
- Uncharacterized protein, isoform A
- Peptidase S1 domain-containing protein
Sequence:
MAVRLSLIWLLLLGTSIDVTRGKRLDNRKLLDNRIVGGQEAEDGVAPYQVSIQTIWKTHICSGVILNEQWILTAGHCALDFSIEDLRIIVGTNDRLEPGQTLFPDEALVHCLYDIPYVYNNDIALIHVNESIIFNDRTQIVELSREQPPAGSTVTLTGWGAPESSYPTVQYLQTLNLTIIAHEECRERWDFHDGIDIGHICTFTREGEGACSGDSGGPLMWEGKLVGLVNWGRACGVGMPDMYANTVYYQDWIRRTHSGCKNRVN
Protein: Ras-like protein B (EC 3.6.5.2) (Q4X241)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Adenylate cyclase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- RAS small monomeric GTPase RasA
- Rho GTPase activator Rga, putative
- GTPase activating protein
- Rho guanyl nucleotide exchange factor, putative
Sequence:
MTLYKLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVVIDQQSCMLEVLDTAGQEEYTALRDQWIRDGEGFVLVYSITSRASFTRIQKFYNQIKMVKESAHSGSPSGASYLGSPMNAPSGPPLPVPVMLVGNKSDKAVERAVSAQEGQALAKDLGCEFVEASAKNCINVEKAFYDVVRMLRQQRQQQQGGRAQDRRPTGLGPMRDRDAGPEYPKTFRPDRARHRGGIKCVIL
Protein: Protein-arginine deiminase type-2 (EC 3.5.3.15) (Peptidylarginine deiminase II) (Protein-arginine deiminase type II) (Q08642)
Organism: Mus musculus (Mouse)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J8}.
Interaction partners:
Sequence:
MQPPIRENMLRERTVRLQYGSRVEAVYVLGTQLWTDVYSAAPAGAKTFSLKHSEGVKVEVVRDGEAEEVVTNGKQRWALSPSSTLRLSMAQASTEASSDKVTVNYYEEEGSAPIDQAGLFLTAIEISLDVDADRDGEVEKNNPKKASWTWGPEGQGAILLVNCDRDTPWLPKEDCSDEKVYSKQDLQDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRQKLYHVVKYTGGSAELLFFVEGLCFPDESFSGLVSIHVSLLEYMAEGIPLTPIFTDTVMFRIAPWIMTPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYMNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPIKQLLGPDFGYVTREPLFETVTSLDSFGNLEVSPPVTVNGKEYPLGRILIGSSFPLSGGRRMTKVVRDFLQAQQVQAPVELYSDWLTVGHVDEFMTFIPIPGKKEFRLLMASTSACYQLFREKQKAGHGEAVMFKGLGGMSSKRITINKILSNESLTQENQYFQRCLDWNRDILKRELALTEKDIIDLPALFKMDENHQARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLETHVRGLLEPLGLACTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVP
Protein: Acyl-coenzyme A oxidase acox-3 (EC 1.3.3.-) (Q20992)
Organism: Caenorhabditis elegans
Function: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior. Specifically, shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon (IC-asc-C7) or 9-carbon (IC-asc-C9) side chains and contributes to the shortening of ascarosides with 13-carbon (asc-C13) and 15-carbon (asc-C15) side chains.
Subcellular location: Peroxisome {ECO:0000269|PubMed:29863473}.
Interaction partners:
- MaoC-like domain-containing protein
- SCP2 domain-containing protein
- Non-specific lipid-transfer protein-like 2
- Enoyl-CoA Hydratase
- Probable 3-ketoacyl-CoA thiolase
- Acetyl-coenzyme A synthetase
- 3-ketoacyl-CoA thiolase
- Acetyl-CoA C-acetyltransferase
- Ethylmalonyl-CoA decarboxylase
- Acetyl-CoA acetyltransferase homolog, mitochondrial
Sequence:
MSAPLIDKYRKMATFDWKKLKAAVEGEEHVRLKSEVVAKMKSEPVFHRDYRVLSREEQREVVHQRWKKIVEWGLFKDPYSDLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKDLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGCWQGVENGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPVKGAENEIPVLEYPLQQYRLFPYLSAAICIRIFQKKFVGHFTEYMMRVIMGEKSDELSEFSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSIETPMSTMSFLNQKPSKFSSWSSNPVNDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQIHRAVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPVLQKVLNLFSLFLLERHLATLYITGYASGGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIMEEFRKYTNEQPRWVCDLAQFLQKRSQGSKL
Protein: Protein disulfide isomerase-like 1-6 (AtPDIL1-6) (EC 5.3.4.1) (Protein disulfide isomerase 4) (AtPDI4) (Protein disulfide isomerase-like 3-2) (AtPDIL3-2) (Q66GQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305}.
Interaction partners:
- Endoplasmic reticulum oxidoreductin-2
- Endoplasmic reticulum oxidoreductin-1
- Protein disulfide-isomerase 5-3
- Protein disulfide-isomerase 5-1
- Protein disulfide-isomerase 5-4
- Transcription factor MEE8
- At5g58530
- Thioredoxin-like 1-3, chloroplastic
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein BIP3
Sequence:
MLTKPKPNSKFSILFTFLLLLSFLIFVARSSDVAVEAGSEEELDDLEQLLAVDEQLQEERPEQQSEAETVSKAQRIVVELNGDNTKRLIDGNEYVMVLGYAPWCARSAELMPRFAEAATDLKEIGSSVLMAKIDGERYSKVASQLEIKGFPTLLLFVNGTSQSYTGGFSSEEIVIWVQKKTGASTIKLDTVDEASGFLKKHHTFILGLFEKSEDSSGHDEFVKAASLDNEIQFVETSSIDVAKLLFPNLKTNNVFVGLVKTEAEKYTSYDGPCQAEKIVEFLNSNKFPLVTKLTESNTVRVYSSPVKLQVMVFSKTDDFESLAQPLEDIARKFKSKLMLIYIDISNENLAMPFLTLFGIEDAKKTVVAAFDNNLNSKYLLESDPSPSNIEEFCFGLAHGTVSAYYKSQPIPDNQNASVVAVVGRTFDEVVLRSSENVLLEVHTPWCINCEALSKQVEKLSQHFKGFENLVFARIDASANEHPKLTVDDYPTILLYKTGEKENPLKLSTKSSAKDMAVLINKELKWKDQSGKDEL
Protein: SH3 and cysteine rich domain 3 (G3V5D4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTEKEVLESPKPSFPAETRQSGLQRLKQLLRKGSTGTKEMELPPEPQANGEAVGAGGGPIYYIYEEEEEEEEEEEEPPPEPPKLVNDKPHKFKDHFFKKPKFCDVCARMIVLNNKFGLRCKNCKTNIHEHCQSYVEMQRCFGKIPPGFHRAYSSPLYSNQQYACVKDL