wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/arginine-rich-splicing factor SR34 (At-SR34) (At-SRp34) (AtSR34) (Pre-mRNA-splicing factor SF2) (SR1 protein) (O22315)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General splicing factor. Can promote splice site selection in vitro presumably by antagonizing the effects of the A1 heterogeneous nuclear ribonucleoprotein. May have an essential function during early plant development.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:16895966}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:16895966}.
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Serine/arginine-rich splicing factor RSZ21
- Serine/arginine-rich splicing factor RS2Z33
- Serine/arginine-rich SC35-like splicing factor SCL28
- Serine/arginine-rich SC35-like splicing factor SCL30A
- Serine/arginine-rich SC35-like splicing factor SCL30
- U1 small nuclear ribonucleoprotein 70 kDa
- Serine/arginine-rich splicing factor SR45
- Nuclear protein-like
- Splicing factor-like protein 1
Sequence:
MSSRSSRTVYVGNLPGDIREREVEDLFSKYGPVVQIDLKVPPRPPGYAFVEFDDARDAEDAIHGRDGYDFDGHRLRVELAHGGRRSSDDTRGSFNGGGRGGGRGRGDGGSRGPSRRSEFRVLVTGLPSSASWQDLKDHMRKGGDVCFSQVYRDARGTTGVVDYTCYEDMKYALKKLDDTEFRNAFSNGYVRVREYDSRKDSRSPSRGRSYSKSRSRSRGRSVSRSRSRSRSRSRSPKAKSSRRSPAKSTSRSPGPRSKSRSPSPRRSRSRSRSPLPSVQKEGSKSPSKPSPAKSPIHTRSPSR
Protein: Precursor RNA processing 3, isoform A (Q9VW52)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SD09427p
- U4/U6 small nuclear ribonucleoprotein Prp31
- RE11167p
- Pre-mRNA-processing factor 6
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing-splicing factor 8
- U6 snRNA-associated Sm-like protein LSm8
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- NHP2-like protein 1 homolog
- LD45152p
Sequence:
MSSIITRKDGDDQKLSKKRAAASDSKSGGGSALEAPKKSRFDVPEKNGGGGEKKEEVAVPASLSSTQIKLMMAHAQREIEERKRALSNLRDKDPLLASVPSIGMPVALATQALAKKPTPEDSEKARKIAELQAQIRAKLTGNLASLIQPTAVAAAAAAAAQAQERPKPLILDDEGRTVDKSGRTINIPTVTPTLKANIRAKKREVFQRQTGLGERSESGTSAQEEAIKYFDDRIALKPTVRTKRTLRFHEPGKFQQLAERMRMKSQLERLQNEISQIARKTGISSATKLALIAPKQDMPDDVPAMEWWDSVILTQDLETVDDASGKISIRQTAITNLIEHPTQMKPPNEPLKPVYLPVFLTKKERKKLRRQNRREAWKEEQEKIRLGLVAPPEPKLRISNLMRVLGSEAVQDPTKMEQHVRDQMAKRQKAHEDANNARKLTSEQKSEKKQRKLREDTSCGVHVSVYRIRDLQDNQSKKFKVETNAKQLQMTGSVVLFRDCCVVVVEGGPKQQKKYRRLMLTRIKWEEDNAKGNDGQDVPNSCVLVWEGTSQRRHFGEIKFKIFPMEKMAREFFQKHQVEHYWDLAYSGAVLEASTDQQ
Protein: Probable UDP-sugar transporter protein SLC35A4 (Complex leucine repeat protein) (Solute carrier family 35 member A4) (Q91ZR7)
Organism: Rattus norvegicus (Rat)
Function: Mediates the transport of CDP-ribitol (By similarity). Does not exhibit CMP-sialic acid, UDP-galactose and UDP-N-acetylglucosamine transport activity (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12124754}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 35 member B1
- Solute carrier family 35 member C2
- Solute carrier family 35 member C1
- Solute carrier family 35 member B4
- Adenosine 3'-phospho 5'-phosphosulfate transporter 2
- Solute carrier family 35 member D1
- Solute carrier family 35, member D3
Sequence:
MSVEDGGMPGLARPKQARWTLMLFLSTAMYGAHAPFLALCHVDGRVPFRPSSAVLLTELTKLLLCAFSLLVGWQTWPQGTPPWRQAAPFALSALLYGANNNLVIYLQRYMDPSTYQVLSNLKIGSTALLYCLCLGHRLSARQGLALLLLMAAGACYASGGFQEPGNTLPGPRSAAGARPMPLHITPLGLLLLILYCLISGLSSVYTELIMKRQRLPLALQNLFLYTFGVILNLGLYAGSGPGPGFLEGFSGWAVLVVLNQAVNGLLMSAVMKHGSSITRLFIVSCSLVVNAVLSAVLLQLQLTATFFLAALLIGLAVCLYYGSP
Protein: PIBF1 protein (Q4G0R1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRKISKESKKVNISSSLESEDISLETTVPTDDISSSEEREGKVRITRQLIERKELLHNIQLLKIELSQKTMMIDNLKVDYLTKIEELEEKLNDALHQKQLLTLRLDNQLAFQQKDASKYQELMKQEMETILLRQKQLEETNLQLREKAGDVRRNLRDFELTEEQYVKLKAFPEDQLSIPEYVSVRFYELVNPLRKEICELQVKKNILAEELSTNKNQLKQLTETYEEDRKNYSEVQIRCQRLALELADTKQLIQQGDYRQENYDKVKSERDALEQEVIELRRKHEILEASHMIQTKERSELSKEVVTLEQTVTLLQKDKEYLNRQNMELSVRCAHEEDRLERLQAQLEESKKAREEMYEKYVASRDHYKTEYENKLHDELEQIRLKTNQEIDQLRNASREMYERENRNLREARDNAVAEKERAVMAEKDALEKHDQLLDRYRELQLSTESKVTEFLHQSKLKSFESERVQLLQEETARNLTQCQLECEKYQEKLEVLTKEFYSLQASSEKRITELQAQNSEHQARLDIYEKLEKELDEIIMQTAEIENEDEAERVLFSYGYGANVPTTAKRRLKQSVHLARRVLQLEKQNSLILKDLEHRKDQVTQLSQELDRANSLLNQTQQPYRYLVESVRQRDSKIDSLTESIAQLEKDVSNLNKEKSALLQTKNQMALDLEQLLNHREVFFLFCHNCNHFRLF
Protein: Ribonuclease VapC35 (RNase VapC35) (EC 3.1.-.-) (Toxin VapC35) (P9WF67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB35.
Interaction partners:
- Antitoxin VapB35
- Antitoxin VapB46
- Transcriptional repressor Mce3R
- Antitoxin VapB47
Sequence:
MIYLETSALVKLIRIEVESDALADWLDDRTELRWITSALTEVELSRAIRAVSPEGLPAVPSVLARLDRFEIDAVIRSTAAAYPNPALRSLDAIHLATAQTAGSVAPLTALVTYDNRLKEAAEALSLAVVAPGQAR
Protein: Tartan protein (Q24250)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMIAFVGIWCILASIGVEPAAGLANCPPGCQCDDNTLVVQCGEGQLDVLPIALNPSIQRLVIKSNKIKTIDSSIQFYAELTFLDLSSNHLMTIPQRTFAYQKKLQEVHLNHNKIGQISNKTFIGLSAVTVLNLRGNQISELHQGTFTPLLKIEELNLGENRIGYLDPKAFDGLSQLRILYLDDNALTTVPDPVIFQAMPSLAELFLGMNTLQSIQAGAFQDLKGLTRLELKGASLRNISHDSFLGLQELRILDLSDNRLDRIPSVGLSKLVRLEQLSLGQNDFEVISEGAFMGLKQLKRLEVNGALRLKRVMTGAFSDNGNLEYLNLSSNKMLLEVQEGALSGLSQLKHVVLKANALTSLAEGLFPWKDLQTLDLSENPLSCDCRVMWLHNLLVAKNASQDDVSELLCEFPERLRGESLRHLNPAMMGCTHADPRKQALIGALLVGSAATITALALVLYRCRHKIRETIKGGLWGNSALGRKEREYQKTFCDEDYMSRHQHHPCSLGIHSTFPNTYTAPHHPGATHHYGMCPMPVNDLGAIDPQQKFQQLVVPTATMISEKKLNNNKALVSQGAIDDSASFVLHMKSATMGRDVHQQNPQLNHYTKPQFLSATATVGDSCYSYADVPMVHGAPLGGPNQPQLRLTQEHFKQRELYDQEMGSEILDHNYIYSNTHYSMPLEQLGRSKTPTPPPMPPALPLRNGLCATTGRRSFQQKSASQKQQQNNNTLRQFTH
Protein: 26S proteasome regulatory subunit rpn502 (P0CU18)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Required for proper proteasome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:12783882}.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit rpn12
- Probable 26S proteasome regulatory subunit rpn6
- Probable 26S proteasome regulatory subunit rpn9
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit 8 homolog
- Probable 26S proteasome subunit rpt4
- 26S proteasome regulatory subunit rpn8
Sequence:
MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKQVRQASDTSTNTKVLIYIADLLFRAGDFQGLNEQLVSLFKKHGQLKQSMTSLVQHVMTYLPGIDDLKTKINLIETLRTITDGKIYVEVERARLTQLLSQIKEEQGDIKSAQEILCNEPVETYGSFDLKEKVAFILDQVRLFLLRSDYYMASTYTKKINVKFFEKEDVQSLKLKYYEQKIRIGLHDDAYLDVCKYYRAVYDTAVVQEDPEKWKEILENVVCFALLTPYDNEQADLLHRINADHKLNSLPLLQQLVKCFIVNELMRWPKIAEIYGSALRSNPVFAENDEKGEKRWSELRKRVIEHNIRVVANYYSRIHCSRLGVLLDMSPSETEQFLCDLIAKHHFYAKIDRPAQVISFKKSQNVQEQLNEWGSNITELLGKLEKVRQLIIKEEMMNSIQQAVAK
Protein: Glycerol-3-phosphate dehydrogenase, mitochondrial (GPD-M) (GPDH-M) (EC 1.1.5.3) (P35571)
Organism: Rattus norvegicus (Rat)
Function: Calcium-responsive mitochondrial glycerol-3-phosphate dehydrogenase which seems to be a key component of the pancreatic beta-cell glucose-sensing device.
Subcellular location: Mitochondrion.
Interaction partners:
- Triokinase/FMN cyclase)
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- glycerol kinase
- Glycerol kinase
- glycerol kinase
- 1-acylglycerol-3-phosphate O-acyltransferase 6
- Glycerol-3-phosphate acyltransferase 3
Sequence:
MAFQKVVKGTILMGGGALATVLGLSQFAHYRRKQVSLAYVEAATCFSEPVNREPPSREAQLMTLQNTSEFDILVIGGGATGCGCALDAVTRGLKTALVERNDFASGTSSRSTKLIHGGVRYLQKAITNLDVEQYRMVKEALHERANLLEIAPHLSAPLPIMLPLYKWWQLPYYWVGIKMYDLVAGSHCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDPETGKERVSGARCKDVLTGHEFNVRAKCVINATGPFTDSVRKMDDNDVVPICQPSAGVHIVMPGYYSPENMGLLDPATSDGRVIFFLPWEKMTIAGTTDSPTDVTHHPIPSEDDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSANTQSISRNHVVEVSDSGLITIAGGKWTTYRSMAEDTVNKAVKLHNLNAGPSRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAKTYGDKAFDVAKMASVTGKRWPVVGVRLVSEFPYIEAEVKYGIKEYACTAVDMISRRTRLAFLNVQAAEEALPKIVELMGRELNWSELRKQEELETATRFLYYEMGYKSRTEQLTDSTEISLLPPDIDRYKKRFHMFDEDEKGFITIVDVQRVLESINVQMDEDTLHEILCEVDLNKNGQVELHEFLQLMSAVHTGRVSGSRLAILMKTAEENLDRRVPIPVDRSCGGL
Protein: Ankyrin repeat and SOCS box protein 15 (ASB-15) (Q8WXK1)
Organism: Homo sapiens (Human)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
Sequence:
MDTNDDPDEDHLTSYDIQLSIQESIEASKTALCPERFVPLSAQNRKLVEAIKQGHIPELQEYVKYKYAMDEADEKGWFPLHEAVVQPIQQILEIVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLLADHISQSYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLDPLNCLLVAVRANNYEIVRLLLSHGANVNCYFMHVNDTRFPSVIQYALNDEVMLRLLLNNGYQVEMCFDCMHGDIFGNSFVWSEIQEEVLPGWTSCVIKDNPFCEFITVPWMKHLVGRVTRVLIDYMDYVPLCAKLKSALEVQREWPEIRQILENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQELKLT
Protein: PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) (X2JDZ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
- GH23156p
- Glutamate receptor 1
- Protein kinase C, brain isozyme
- Glutamate receptor IB, isoform B
Sequence:
MLTDTEDDFFFEEDKMPEPLLIQLDGDGAQAVRQPKERTEQREHASGSVAPNEATVMLCSPAGFSCDSASGDRFGIESASRQKYELDRLGMTVSTNAVVITKDQSNLIGISIGGGAPMCPCLYIVQIFDGTPAAREGSLQSGDELLAVNSVSVKGKTKVEVAKMIQTATDEVVIHYNKLHADPEQGKTLDIILKKLKHRIVDNLSSNTADTLGLSRAILCNDSLVKRLEELEGTELMYKGLVEHARRMLKAYYDLLQTYKSFGDCFTQISVHEPQQRASEAFRTFGEFHRTLEKDGLGIIKQIKPVLADLGTYLNKAIPDTKLTVRRYADAKFTYLSYCLKVKEMDDEEHGFAALQEPLYRVETGNYEYRLILRCRQDARSKFAKLRTDVLEKMELLECKHAMDLNKQLRSLLESLAELHRSLVDRLDSLPPLFPIEVDFKETDFQYKSSTLKPQELDDDEIEANNHPHSTPSQVDCGFEAVEQPAAIINVEAAKASVDSSTLQSASENETLLKELGLYDVDLLSNPQTISNQKDSIAAQNDGYDFDLFLNQATAATTSLERDLMSSNAEEMDLLLQ
Protein: Negative elongation factor complex member E (A2ABK4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAG
Protein: Uncharacterized protein C132.03 (Q9USN6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MNPKRLRITGPEDLTDAYDTMPFRCLNGSMPPKTPLNFVFKENDSHVSNGVGLKKDCIESIDDLNLDDWSEQQESILLMCYENELQKPITCTPMGPICLWAPPEPVLRSVHNTLLKMGWSISEKKMKKKLLELLAKNKKRRTMRKLEIDTNLSFLTDVQRDSPIIENAPLQSPFHF
Protein: FI01426p (Heterochromatin protein 4, isoform A) (Q8IQ92)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heterochromatin protein 5, isoform B
- Heterochromatin protein 6
- Histone-lysine N-methyltransferase Su
- LD09786p
Sequence:
MSPKTKKMIVKIPRHPYFNVQGERSVEREVEYQVRKCRVNLERIKSSTSPNSRPFPLKPKPKRCIVRVARLPDVERSEISVTPASSIMNSDIDENSGSDQESNLTI
Protein: Uncharacterized protein (Q387Q9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEDTFFRRAANWMYGDSSYLQRTPPPELGDRHINELLSRHPFHPFDPEMSSEHPCSENNSLFYSCMTSDEVEGYELHMKHVTCYFPYKVNLMKCLSRERRLARAGASSDIDKQK
Protein: Ribosome maturation factor (F4JN76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein transport protein SEC24 C
- Protein transport protein SEC24 B
- Protein transport protein SEC31 homolog A
- Protein transport protein SEC31 homolog B
- Protein transport protein SEC24 A
- Protein transport protein SEC23 D
- Telomerase reverse transcriptase
- Protein transport protein SEC13 homolog B
- Protein transport protein SEC13 homolog A
- Mediator of RNA polymerase II transcription subunit-like protein
Sequence:
MDMSLDEIIKMEKSNTNVNKGKKQRVLNKKEKFSGAAKNSAVKAQRYMDSRSDVRQGAFAKKRSNFQGNQFPVTTTVARKAASATPRGRPYNGGRMTNTNQSSWSIVGRLKWVDARLLRQHEDSDAQIFMIEHATDHSSSCLLLIPDKVLKNYRETGVSVLVFFHSILHEPATYFLCTEGIRIMKFIAPPAQNRASQRGFVGKQQQQQREKIVQQQANGGGGGQRQWPQTLDSRFANMKEERMRMRRFADNRSNVGNNGAGSHQQQRSMVPWVRRATRFPN
Protein: Small ribosomal subunit protein uS8B (40S ribosomal protein S22-B) (RP50) (S24) (YP58) (YS22) (Q3E7Y3)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS8A
- Small ribosomal subunit protein uS11A
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS27B
- Small ribosomal subunit protein uS4A
- Small ribosomal subunit protein eS7A
- Small ribosomal subunit protein uS17A
- Small ribosomal subunit protein uS3
Sequence:
MTRSSVLADALNAINNAEKTGKRQVLLRPSSKVIIKFLQVMQKHGYIGEFEYIDDHRSGKIVVQLNGRLNKCGVISPRFNVKIGDIEKWTANLLPARQFGYVILTTSAGIMDHEEARRKHVSGKILGFVY
Protein: Uncharacterized protein, isoform B (A0A126GV06)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH11341p
- 26S proteasome regulatory complex subunit p50
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 4
- Proteasome subunit alpha type-5
- Large proline-rich protein BAG6
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
Sequence:
MSEPAAQQQQSQNGKERSKSTEEKEVPREPALVLKDIDIKTELESLVKLLDGKIYKEEEVAMEELHQYLIEDDGSWALGDNFLIFVQRVLRDNQAFSPDTRIHLIRTLAYAALKDDVIIILHQDRRDHTLMNYAQDIDKQTPEEQQAWAMFMCNLFENLGPSEWLLYISEWEYNGQTISNIRVTTKVAVHCILSNCPQLKNIGSMILYNIAIKEVKTVVFDDIAVELAMAILQFFQSSPNEDQIFRTLRALVRFLEVVSQDVPMIIQMIGPHPKQFAGKSERVDELIKIISRKVPA
Protein: D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) (L-galactono-gamma-lactone oxidase) (C8VJF3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MWYDTMCSDDPNTVIIQTENVNNIHDLDLEAGTVMIEAGVTFLQLAEYLHERGASAGYTLVNWNITLAGCVAMGAHRSSIREDSMVAAGVLALDIIDGEGNLRHLERDDSDEWLAASTSLGLLGVIARMKFKIYPDFKVYADQKTLDEAEVFDGDIYGMIAPYATANFWWWPYKRKFHWRYYDVVENSINEQQGFQNTFSVTGVEAAAIKVLWNSGRWLATSNMLAEEILFGQWEAPNFREKTTNKAIDTWPVYGWNYDVLIGGLYPDQKPVWEYGLSGYTLELAFPVTQANAVLKRARELFDAELKKGLVMTSTYRSGINIKFGRPYYDLLGQVTYNTSDGADWSKGAIMFDFPSFKPTVGDGSRFNEPFYGTLEKALIEEFPCRPHWTKNTREVFQLAKKNLDPDHIARFKAIREKFDPNGVYRSVVGEIIGVY
Protein: T cell receptor beta, variable 13-2 (A0A140T8N6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGSRLFFVLSSLLCSKHMEAAVTQSPRNKVAVTGGKVTLSCNQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQENFSLILELATPSQTSVYFCASGD
Protein: Paired amphipathic helix protein Sin3b (Histone deacetylase complex subunit Sin3b) (Transcriptional corepressor Sin3b) (O75182)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
Interaction partners:
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone deacetylase 2
- Histone deacetylase complex subunit SAP30
- Histone deacetylase 1
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- PHD finger protein 12
- Paired amphipathic helix protein Sin3a
- AT-rich interactive domain-containing protein 4B
- AT-rich interactive domain-containing protein 4A
Sequence:
MAHAGGGSGGSGAGGPAGRGLSGARWGRSGSAGHEKLPVHVEDALTYLDQVKIRFGSDPATYNGFLEIMKEFKSQSIDTPGVIRRVSQLFHEHPDLIVGFNAFLPLGYRIDIPKNGKLNIQSPLTSQENSHNHGDGAEDFKQQVPYKEDKPQVPLESDSVEFNNAISYVNKIKTRFLDHPEIYRSFLEILHTYQKEQLNTRGRPFRGMSEEEVFTEVANLFRGQEDLLSEFGQFLPEAKRSLFTGNGPCEMHSVQKNEHDKTPEHSRKRSRPSLLRPVSAPAKKKMKLRGTKDLSIAAVGKYGTLQEFSFFDKVRRVLKSQEVYENFLRCIALFNQELVSGSELLQLVSPFLGKFPELFAQFKSFLGVKELSFAPPMSDRSGDGISREIDYASCKRIGSSYRALPKTYQQPKCSGRTAICKELDHWTLLQGSWTDDYCMSKFKNTCWIPGYSAGVLNDTWVSFPSWSEDSTFVSSKKTPYEEQLHRCEDERFELDVVLETNLATIRVLESVQKKLSRMAPEDQEKFRLDDSLGGTSEVIQRRAIYRIYGDKAPEIIESLKKNPVTAVPVVLKRLKAKEEEWREAQQGFNKIWREQYEKAYLKSLDHQAVNFKQNDTKALRSKSLLNEIESVYDEHQEQHSEGRSAPSSEPHLIFVYEDRQILEDAAALISYYVKRQPAIQKEDQGTIHQLLHQFVPSLFFSQQLDLGASEESADEDRDSPQGQTTDPSERKKPAPGPHSSPPEEKGAFGDAPATEQPPLPPPAPHKPLDDVYSLFFANNNWYFFLRLHQTLCSRLLKIYRQAQKQLLEYRTEKEREKLLCEGRREKGSDPAMELRLKQPSEVELEEYYPAFLDMVRSLLEGSIDPTQYEDTLREMFTIHAYVGFTMDKLVQNIARQLHHLVSDDVCLKVVELYLNEKKRGAAGGNLSSRCVRAARETSYQWKAERCMADENCFKVMFLQRKGQVIMTIELLDTEEAQTEDPVEVQHLARYVEQYVGTEGASSSPTEGFLLKPVFLQRNLKKFRRRWQSEQARALRGEARSSWKRLVGVESACDVDCRFKLSTHKMVFIVNSEDYMYRRGTLCRAKQVQPLVLLRHHQHFEEWHSRWLEDNVTVEAASLVQDWLMGEEDEDMVPCKTLCETVHVHGLPVTRYRVQYSRRPASP
Protein: Transposon Ty1-DR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q03855)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPGINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGEGDNEIQYDILGLEIKYQRSKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGSLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: FAD/NAD(P)-binding domain-containing protein (A0A1D8PI22)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSKEKSKQIVIIGGSYAGILALKTLLKSSPIELNITLISPNDSGYFNAAAPRLLIEPESIEKTIFPIKPTIEKLTSGTIHTAKFLQGVVTKVDLTNQKVFVDNESEIDYDNLIIASGARAKSPAFKLTNNNDQNYTIKAILELGDEIKAANNIAVIGGGSTGVETSAEIAFKYSDKNVVLYTGASRPLPSFPKSTSSKATGKLNQLGIEIVNGERVNVKDKTIEFADGSTKSFDLIIETSGLLPNTDFLPKKVLNEYGYVDTDEYLRLKDHHNVICLGDVVASGANSIVDLVYTQKPVFEKTVEFEVVDNEATQLKAYQKASGITTFIPIGRNGGVGLLFGYCVPSFLIWFAKARDFMISKAGEHFT
Protein: NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (NEDD8-activating enzyme E1C) (Ubiquitin-activating enzyme E1C) (Ubiquitin-like modifier-activating enzyme 3) (Ubiquitin-activating enzyme 3) (Q8C878)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit
- Ubiquitin-like protein NEDD8
- NEDD8-conjugating enzyme Ubc12
- NEDD8-conjugating enzyme UBE2F
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Sentrin-specific protease 8
- Cullin-2
- Cullin-5
- RING-box protein 2
Sequence:
MADGEEPEKKRRRIEELLAEKMAVDGGCGDTGDWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFGDGVPLDGDDPEHIQWIFQKSIERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYLQSVTSIEERTRPNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFT