wanglab/gogpt-training-data huggingface dataset:
Protein: 7-methylguanosine phosphate-specific 5'-nucleotidase (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3B) (Cytosolic 5'-nucleotidase III-like protein) (cN-III-like protein) (EC 3.1.3.5) (N(7)-methylguanylate 5'-phosphatase) (Q969T7)
Organism: Homo sapiens (Human)
Function: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cytosolic 5'-nucleotidase 1B
- 5'
- Cytosolic 5'-nucleotidase 1A
- 5'
- Cytosolic purine 5'-nucleotidase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenosine deaminase
- Deoxycytidine kinase
- 5'-nucleotidase
- Adenosine kinase
Sequence:
MAEEVSTLMKATVLMRQPGRVQEIVGALRKGGGDRLQVISDFDMTLSRFAYNGKRCPSSYNILDNSKIISEECRKELTALLHHYYPIEIDPHRTVKEKLPHMVEWWTKAHNLLCQQKIQKFQIAQVVRESNAMLREGYKTFFNTLYHNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVSNYMDFNEDGFLQGFKGQLIHTYNKNSSACENSGYFQQLEGKTNVILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERRERYMDSYDIVLEKDETLDVVNGLLQHILCQGVQLEMQGP
Protein: Metchnikowin (Q24395)
Organism: Drosophila melanogaster (Fruit fly)
Function: Potent antifungal and antibacterial activity against Gram-positive bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:9736738}.
Interaction partners:
- Attacin-C
- Diptericin A
- Diptericin B
- Attacin-A
- Drosocin antimicrobial peptides
- Cecropin-C
- Peptidoglycan-recognition protein SB1
- Defensin
- Peptidoglycan-recognition protein SD
- Cecropin-B
Sequence:
MQLNLGAIFLALLGVMATATSVLAEPHRHQGPIFDTRPSPFNPNQPRPGPIY
Protein: Photosystem II reaction center protein J (PSII-J) (Q2LIJ8)
Organism: Oryza grandiglumis (Wild rice) (Oryza sativa var. grandiglumis)
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01305}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01305}.
Interaction partners:
Sequence:
MADTTGRIPLWLIGTVTGIAVIGLIGVFFYGSYSGLGSSL
Protein: Oligopeptide ABC transporter, ATP-binding protein (F9UN54)
Organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
Interaction partners:
- Oligopeptide ABC transporter, ATP-binding protein
- Oligopeptide ABC transporter, permease protein
- Oligopeptide ABC transporter, permease protein
- Oligopeptide ABC transporter, substrate binding protein
- ABC transporter, substrate binding protein
- Nitrate/sulfonate/bicarbonate ABC transporter,ATP-binding protein
- Oligopeptide ABC transporter,oligopeptide-binding protein
- Zinc/iron ABC transporter, ATP-binding protein
- ABC transporter, substrate binding protein
- Oligopeptide ABC transporter, substrate binding protein
Sequence:
MEKPENVIEVRNLEINFHTYAGEVKAIRDVSFDLRKGETLAIVGESGSGKSVTTRSLMGLLAPNAEIKRGSIMFHGEDIIKKSEKDMQHIRGKDIAMIFQDPMTSLDPTMRIGMQIAEPLMKHKGLKKKEAIAQALEMLKLVGITNPEGRINDYPYQFSGGMRQRIVIAIALVCYPEVLIADEPTTALDVTIQAQILDLMKDLQNRIDTSIIFITHDLGVVAGMADRVAVMYAGKIVEYGTVDEIFFNPQHPYTWGLLNSMPTLDTESGSLSAIPGTPPDLLEPPVGDAFAARSDYAMKIDTEKEPPFFKVSDTHYAATWLLHPDAPKVTPPAEIVRRQQKFAAMQKPQAPISNPVAKE
Protein: Tetraspanin (Q9VGV3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MSNHRYHQGGNYMHPRISTYPHHFSYVSSCVKYMIFLLNFLFWLFGGLLLAIGVYAFMDKLMDGNGWLRLDTIYDVIFNISLVMIIAGVIVFTVSFAGCLGALRENTWLLKLYSMCLLLFFILEMSLAIICFVFPQYMNSFLEYQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSNAGYQDWSKNEYFNCSSPSVERCGVPYSCCINATDISSGLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNLYVIAGVALGIALLQLFVIYLAKTLEGQIDLQKSRWS
Protein: Atypical chemokine receptor 2 (V9GYM0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLY
Protein: Putative lysine-specific demethylase JMJ16 (EC 1.14.11.-) (Jumonji domain-containing protein 16) (AtJMJ16) (Protein JUMONJI 16) (Lysine-specific histone demethylase JMJ16) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ16) (C0SUT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as histone H3 'Lys-4' (H3K4me) demethylase involved in the negative regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Not active on mono-, di- and trimethylated H3K9, H3K27 and H3K36 in somatic cells. However, also active on H3K9 when in complex with MMD1, a meiocyte-specific histone reader. Together with MMD1, promotes gene expression in male meiocytes in an H3K9me3-dependent manner, and contributes to meiotic chromosome condensation by triggering some condensin promoters (e.g. CAP-D3 and CAP-H). Together with JMJ14 and JMJ17, required for plant growth and development. Represses leaf senescence in an age-dependent manner by demethylating H3K4me3 activating histone marks at senescence-associated genes (SAGs) loci, including WRKY53 and SAG201, thus preventing their premature expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:32572214}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit delta, chloroplastic
- ATP synthase subunit O, mitochondrial
- ATPase, F1 complex, OSCP/delta subunit protein
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- ATP synthase subunit a-1
- ATP synthase subunit a.
- ATP synthase subunit a-2
- ATP synthase subunit a, chloroplastic
Sequence:
MGTELMRICVKEDSDDLPSVPPGFESYATFTLKRVVPATTSDKAKTPAIESVSATEQAKMEVESDEAKAARALRRRPWINHSGCDDDGDCAANNDNAASQNPDQNCDVKPALPKGVVRGCEECKDCQKVTARWHPDEARRPDLEDAPVFYPSEEEFEDTLNYIAKIRPEAEKYGICRIVPPPSWKPPCPLKEKQVWEGSKFTTRVQRVDKLQNRSSMKKISKLPNQMRKKKRKCMKMGMDSVTNGMGDPCSASTGMNELETFGFEPGPGFTLKDFQKYADEFKAQYFKKSETSTDDKCKVDNSIDCWEPALEDVEGEYWRIVDKATEEIEVLYGADLETGVFGSGFPKISSSHNASSSEDKYAKSGWNLNNFPRLPGSLLKYEGSDISGVLVPWLYIGMCFSSFCWHVEDHHLYSLNYMHWGAPKLWYGVGGKDAVKLEEAMRKHLPDLFEEQPDLLHKLVTQLSPSKLKTAGVPVHRCVQHAGEFVLTFPRAYHAGFNSGFNCAEAVNVAPVDWLPHGQIAIELYCQQGRKTSISHDKLLLGAAREVVKADWELNLLRKNTVDNLRWKAFSAKDGILAKTLKARIDMERTRREFLCNSSLALKMHSNFDATNERECCICFFDLHLSAAGCRCSPEKYSCLTHVKELCSCPWVTKYFLFRYDIDELNVLVEAVEGKLSSVYRWARQDLGLALSTDVSGSKMEIDEEGKVHKDPTPQTTALSGKDLQLKVTSKEVSKELEKTSKLSHVNLLLKEKEEQITSSHCMKPVKEETVCDSSDPNVSACQPSEGGIICMTAVKSASGKKNSQSLPNDVILLSDDEYDIPRKRGSVRRDAISSGKKLEIRERPTHVLALEASAKIAAPICQREGDSLRDTRNTISLPTNDQKTMRRDVPSSTSHAEVNAEATGLTQDICNRMATNSHGGGKPTSCKSKNSGGLAIVDVVDGTRSSSGTPSCSQNNSPDRFIRQKGPRIAKVVRRINCNVEPLSYGCVLSGKSWCSRRAIFPKGFRSRVKYINILDPTNMCFYISEILDAGRNSPLFMVYLESNPSEVFVHMSPTRCWEMVRERVNQEITKQHKAGKSDLPPLQPSGSPDGFEMFGYSSPAIVQAIEALDVNRVCTDYWDSRPYSRPQVQFPANPLLREANTSGRSNVGNLQLNPGHHISPTGINSILKVLFKKASMEELSSLQEVLSETNSDMVTELVKEEIQNRR
Protein: Small ribosomal subunit protein eS30z/eS30y/eS30x (40S ribosomal protein S30) (P49689)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS17z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein uS2z
- Large ribosomal subunit protein eL32z
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein uS12z
- Small ribosomal subunit protein uS10z/uS10x
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein uS13z/uS13y/uS13x
Sequence:
MGKVHGSLARAGKVRGQTPKVAKQDKKKKPRGRAHKRLQHNRRFVTAVVGFGKKRGPNSSEK
Protein: Alpha-actinin, sarcomeric (H2L2C9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLLEVISGEPLPKPDRGKMRFHKIANVNKALEYIESKGVKLVSIGAEEIVDGNVKMTLGLIWTIILRFAIQDINVEELSARDGLLLWCQRKTAPYNNVNVQNFHNSWKDGLAFCALIHRHRPDLLDYSQLHKGDPIHNLNLAFDIAEKHLDIPKMLDAEDVSRHPDEKSTMTYVSCFYHAFRNMRDPPPPVIRQPPPQRVVVAPPPERDWRKDAETAANRICRVLKVNQENEKMMEDYENLASDLLAWINRWMPWLANRSTDDTLQQAQQKLEDYRNYRRREKPPRIEDKGRLETLFNTLQTRLRLSNRPAFLPRDGHLIKDINAAWAGLEDSEKGFEEWLLSEIMRLERLEHLAEKFRRKCALHEEWAHGKEDALRSNDWRSCGLYKIKALRKRHEAFESDLGAHQDRVEQIAAIARELNNLRYPDIGPINARCQAICSQWDRLGQLSSKRRETLEDAERIAERLDSLYLDFAKRAAPFNNWLDGAREDLADLVIVHEMREIEELVNAHDQFKSTLGDADREFSSINQIEHEVEHLVTSHGLDRELLRNPYTDLSASDIRRKWGEVQNSVPRRDSQLQAELKRQQNNERLRTIFAEKANQVGPWLERELEQVLAIGLGGRGRLEDAIQQLRSIQRNVLGYKPNLDELERVHQEMQENFVFENRKSRYSMESLRVGWETLLTSINKTINEFENQVLLRDSKGISEEQIAEFRASFSHFDKERAGLDPEQLRSCLISVGYTIRPGREGDAELHRVLAHVDPNRMGRVPFEAFLDFMTKENSDQDTVEQMIDSFRILASGKTFITADELERELPRDQAAYCMARMAPSREPGAPPRSFDYVTFSRSLYSQ
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (A0A0B4J1T8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQFPSPPAARSSPAPQAASSSEAAAPATGQPGPSCPVPGTSRRGRPGTPPAGRVEEEEEEEEEDVDKDPHPTQNTCLRCRHFSLRERKREPRRTMGGCEVREFLLQFGFFLPLLTAWPGDCSHVSNNQVVLLDTTTVLGELGWKTYPLNGWDAITEMDEHNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNSIPWVLGTCKETFNLFYMESDESHGIKFKPNQYTKIDTIAADESFTQMDLGDRILKLNTEIREVGPIERKGFYLAFQDIGACIALVSVRVFYKKCPFTVRNLAMFPDTIPRVDSSSLVEVRGSCVKSAEERDTPKLYCGADGDWLVPLGRCICSTGYEEIEGSCHACRPGFYKAFAGNTKCSKCPPHSLTYMEATSVCQCEKGYFRAEKDPPSMACTRPPSAPRNVVFNINETALILEWSPPSDTGGRKDLTYSVICKKCGLDTSQCEDCGGGLRFIPRHTGLINNSVIVLDFVSHVNYTFEIEAMNGVSELSFSPKPFTAITVTTDQDAPSLIGVVRKDWASQNSIALSWQAPAFSNGAILDYEIKYYEKEHEQLTYSSTRSKAPSVIITGLKPATKYVFHIRVRTATGYSGYSQKFEFETGDETSDMAAEQGQILVIATAAVGGFTLLVILTLFFLITGRCQWYIKAKMKSEEKRRNHLQNGHLRFPGIKTYIDPDTYEDPSLAVHEFAKEIDPSRIRIERVIGAGEFGEVCSGRLKTPGKREIPVAIKTLKGGHMDRQRRDFLREASIMGQFDHPNIIRLEGVVTKRSFPAIGVEAFCPSFLRAGFLNSIQAPHPVPGGGSLPPRIPAGRPVMIVVEYMENGSLDSFLRKHDGHFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTTGGKIPIRWTAPEAIAYRKFSSASDAWSYGIVMWEVMSYGERPYWEMSNQDVILSIEEGYRLPAPMGCPASLHQLMLHCWQKERNHRPKFTDIVSFLDKLIRNPSALHTLVEDILVMPESPGEVPEYPLFVTVGDWLDSIKMGQYKNNFVAAGFTTFDLISRMSIDDIRRIGVILIGHQRRIVSSIQTLRLHMMHIQEKGFHV
Protein: V-type proton ATPase subunit e (V-ATPase subunit e) (Vacuolar proton pump subunit e) (Q69Z14)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:Q3E7B6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit a
- V-type proton ATPase subunit c
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit d
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c'
Sequence:
MGGLVVLLVGLLTALMSVVSYYVSPKGNNTSTWQMSLILTFSCCYLLWAITYLAQLHPLEAPSRVLE
Protein: cDNA FLJ61501, highly similar to SID1 transmembrane family member 2 (B4DZN7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MFQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVSRMDDFVLRTGEQFSFNTTAAQPQYFKYEFPEGVDSVIVKVTSNKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFAEDEPVDQGHRQKTLSVLVSQAVTSEAYVSGMLFCLGIFLSFYLLTVLLACWENWRQKKKTLLVAIDRACPESGHPRVLADSFPGSSPYEGYNYGSFENVSGSTDGLVDSAGTGDLSYGYQGRSFEPVGTRPRVDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLYVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLCALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSIIHIIATLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYVDRMVLLVMGNVINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVSGPPGRAGWVREGSSCLLLCG
Protein: Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homolog) (Q6NQ54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a deubiquitination module (DUB module) that specifically deubiquinates monoubiquinated histone H2B (H2Bub). Does not seem to be a component of the TREX-2 complex. Seems to act independently of the SAGA multiprotein complex. The DUB module is responsible for the major H2Bub deubiquitinase activity in Arabidopsis.
Subcellular location: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03046, ECO:0000269|PubMed:29588169, ECO:0000269|PubMed:30192741}. Note=Does not localize in nucleolus and displays a rather patchy distribution forming a speckled pattern in the nucleoplasm (PubMed:29588169, PubMed:30192741). Does not localize in the nuclear pore complex at the nuclear periphery (PubMed:29588169, PubMed:30192741). {ECO:0000269|PubMed:29588169, ECO:0000269|PubMed:30192741}.
Interaction partners:
- Ubiquitin C-terminal hydrolase 22
- SAGA-associated factor 11
- Transcription initiation factor TFIID subunit 10
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Transcription initiation factor TFIID subunit 9
- SAC3 family protein C
- SAGA-associated factor 29 homolog A
- Transcriptional adapter ADA2b
- SAC3 family protein B
Sequence:
MKHSVNRPPTPDEDDVADGFEKDKVTLREIINVKLVESGEKENLMELVRDRLVECGWKDEMRIACREHVKKKGRKDVTVDELIRVITPKGRASVPDSVKAELLNRIQNFIVSAAL
Protein: Photosynthetic NDH subunit of lumenal location 4, chloroplastic (FK506-binding protein 16-2) (AtFKBP16-2) (Immunophilin FKBP16-2) (Peptidyl-prolyl cis-trans isomerase FKBP16-2) (PPIase FKBP16-2) (EC 5.2.1.8) (Rotamase) (Q9SCY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Probable). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Seems to be essential for stabilizing the NDH subcomplex A.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11826309}.
Interaction partners:
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- Photosynthetic NDH subunit of lumenal location 1, chloroplastic
- Photosynthetic NDH subunit of lumenal location 5, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- NAD
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 6, chloroplastic
- Photosynthetic NDH subunit of lumenal location 3, chloroplastic
Sequence:
MAISTLTLTQSLYTRSFRPTIFFSSSSSSSFSCLCSSSSDCEPKLSVKKRVFGVGLGFLASSILSLTPLDADATRIDYYATVGDPLCEYSYAKSGLGFCDLDVGFGDEAPRGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGGEGVPPMRVGGKRKLQIPPKLAYGPEPAGCFSGDCNIPGNATLLYDINFVEIYPGSNTR
Protein: LP05923p (Polychaetoid, isoform F) (Q8MQQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFPDYVPNNMLVGDRTTWEYHTVAVTRVPGYGFGIAVSGGRDNPHFANGDPSIAVSDVLKGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNTVQLVVKRRVPLNPINAAGAVQHQHSHSLSSVGLMANGSGGVAPTPITSLSQPNSLNSSLVQNASSGQPIKVTLTKGGKKDDYGVVLGCRLFVKEISSKAREQLNANGYSLQEGDIITRIHNTNCGDTMSLKEAKKIIDGCKERLNLVVLRDITNQTAVSQLNLNNSASHQASGNIYATHQPQVSGCSSSNNNLEDPYLPGGASYSSQNLYVQPPTRTSNGPNINGNGLNDEKSNLTPRGRSRGPIMDGVSLQQLDRPVTPTRGRSAAIDEPPRPPPPRGSSGGAAQEDFYSSRRQLYEERQSAEPRFISFQKEGSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQYCKEEYDEVVTNQRGDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEELATAQFNATKKEMNANESRGNFFRRRRSTHRRSKSLSRENWDDVVFSDSISKFPAYERVVLRHPGFVRPVVLFGPVSDLARERLAKDFPDKFSTPLQDDDKSAATSGKCRIVRLSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKAAHKSSKKLLEQCQKLERVWSHIFSTQIALSDEESWYRKLRDSIDLQQSGAVWMSESKPVESLSDDFLFPMTTSRLSYASSPESDLELSPGPSASLSLGNLPQLVKASSDPSIATNQDNLDRDRDIIGEGLPPPYTVPYDHAVPANPNRRQTMDSSKYSIYGTNVPPQQQQPGVGGDTAAVRPQSLYGINAPDLPPRIDRQSKPGDIPLNTSGSSSRNGTLGRSAQERLFGKAVVQDDVQAEYITRNALVGSGAAETLDRQQQQQQQTHASLERQARLNAQLKANGVGAGGGGASTYDSVSSYDSYNNTQMAMQNLGRLGPNAPDDLKSVPNANGRPLPPTGQSHEYGRTPHDHRSFGGPNDLNRQSSPGRPHYHDMNASRNIDPRNGTPQRPSNLGLESSPRKPLVETKTDYGKYS
Protein: HLA class II histocompatibility antigen, DM alpha chain (MHC class II antigen DMA) (Really interesting new gene 6 protein) (P28067)
Organism: Homo sapiens (Human)
Function: Plays a critical role in catalyzing the release of class II-associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO.
Subcellular location: Late endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Localizes to late endocytic compartment. Associates with lysosome membranes.
Interaction partners:
- HLA class II histocompatibility antigen, DRB1 beta chain
- HLA class II histocompatibility antigen, DR alpha chain
- HLA class II histocompatibility antigen, DP alpha 1 chain
- HLA class II histocompatibility antigen, DM beta chain
- HLA class II histocompatibility antigen, DO beta chain
- HLA class II histocompatibility antigen, DP beta 1 chain beta chain)
- HLA class II histocompatibility antigen gamma chain
- HLA class II histocompatibility antigen, DO alpha chain
- HLA class I histocompatibility antigen, B alpha chain
- HLA class I histocompatibility antigen, C alpha chain
Sequence:
MGHEQNQGAALLQMLPLLWLLPHSWAVPEAPTPMWPDDLQNHTFLHTVYCQDGSPSVGLSEAYDEDQLFFFDFSQNTRVPRLPEFADWAQEQGDAPAILFDKEFCEWMIQQIGPKLDGKIPVSRGFPIAEVFTLKPLEFGKPNTLVCFVSNLFPPMLTVNWQHHSVPVEGFGPTFVSAVDGLSFQAFSYLNFTPEPSDIFSCIVTHEIDRYTAIAYWVPRNALPSDLLENVLCGVAFGLGVLGIIVGIVLIIYFRKPCSGD
Protein: Activation-induced cytidine deaminase (Single-stranded DNA cytosine deaminase (EC 3.5.4.38)) (Q5YF88)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MICKLDSVLMTQKKFIFHYKNVRWARGRHETYLCFVVKRRIGPDSLSFDFGHLRNRSGCHVELLFLRHLGALCPGLSASSVDGARLCYSVTWFCSWSPCSKCAQQLAHFLSQTPNLRLRIFVSRLYFCDEEDSVEREGLRHLKRAGVQISVMTYKDFFYCWQTFVARRERSFKAWDGLHENSVRLVRKLNRILQPCETEDLRDVFALLGL
Protein: Protein MSS51, mitochondrial (Mitochondrial splicing suppressor protein 51) (P32335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a dual role in the assembly of cytochrome oxidase subunit 1 (COX1). It has a regulative function on COX1 synthesis, acting as a translational activator specific for the COX1 mRNA, and it also binds to newly synthesized COX1 protein. Together with COX14, may act as a chaperone that binds efficiently unassembled COX1 and prevents it from unproductive aggregation. When bound to COX1, MSS51 is unable to interact with the COX1 mRNA and translation is halted. This may be a feedback control that ensures that COX1 is only produced as long as potentially harmful assembly intermediates are not accumulating.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10803883, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15306853}; Peripheral membrane protein {ECO:0000269|PubMed:10803883, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15306853}; Matrix side {ECO:0000269|PubMed:10803883, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15306853}.
Interaction partners:
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase assembly factor 3, mitochondrial
- Cytochrome c oxidase assembly protein COX14
- Cytochrome oxidase assembly protein SHY1
- Cytochrome c oxidase assembly factor 1
- Mitochondrial COX1 translation regulator PET309
- Cytochrome c oxidase subunit 2
- Oxysterol-binding protein homolog 1
- Import motor subunit, mitochondrial
- Oxysterol-binding protein homolog 2
Sequence:
MTVLYAPSGATQLYFHLLRKSPHNRLVVSHQTRRHLMGFVRNALGLDPPPSPEDPTPENRFHPWDQSPSVDLRERAAKIRTLAHCPVTGKDINYTCPLSGIPTHHSREAWEMDKAYHDSKKYEILKKVNIYEHDLRSGRPFPEFDFPQQQGYDKAVNLTNWDLFFYTRSFYSMDTEFQLAAVTKMLSYPITIGSLLHKFSPYSLNPKGPITLEGLKSLAALRYTLYPLENRSLPTTTKNRAMRIFILGARAEAQLPGHVWKQLQFLFPEQSFEIHFIGPECLYKRDKQEYVKSTTPVVQRVDETLKFIYRTNFFEVFHEAQDFFPYDPYMDVFFTFHPGYASPESHGSWMGETMKALLETKCAIFTTGFNKKDLTDDINLVKSKYGKEMDVLMEPVRNVFGSTKWELNDMNPQEVYQFNMYIAGFRGKRYHTIKRQ
Protein: Transcription factor IBH1 (OsIBH1) (Basic helix-loop-helix protein 175) (OsbHLH175) (Protein ILI1-BINDING BHLH 1) (bHLH transcription factor bHLH175) (Q7XR02)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Atypical and probable non DNA-binding bHLH transcription factor that acts as negative regulator of cell elongation and plant development. Binds the transcription factor ILI1 and forms a heterodimer of antagonistic bHLH transcription factors that function downstream of BZR1 to mediate brassinosteroid regulation of cell elongation and lamina inclination.
Interaction partners:
- Transcription factor ILI1
Sequence:
MDAKRTPPPPTPPNPNPSVIGSGAAADGGGFGRGEAAAATKHMLAFHFLRALSRIHRATPVTRRTRTIRRAAYSSMARAASPRRAWSRALLGQVRARRSRTLMRRAAVLVRRRVVAAPAPSPASARGVRIIAAGETSAAARAVPPPPRQQGEPPRAEALRRLVPGGAGMEYSSLLEETADYLRSLRAQVQLMQGLVDLFSYQ
Protein: Atypical kinase COQ8, mitochondrial (EC 2.7.-.-) (Activity of bc1 complex protein 1) (Coenzyme Q protein 8) (Ubiquinone biosynthesis protein COQ8) (P27697)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Affects the molecular organization and function of COQ3, possibly through kinase activity towards COQ3, COQ5 and/or COQ7. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11279158, ECO:0000269|PubMed:18801050, ECO:0000269|PubMed:21296186}; Peripheral membrane protein {ECO:0000269|PubMed:11279158, ECO:0000269|PubMed:18801050, ECO:0000269|PubMed:21296186}; Matrix side {ECO:0000269|PubMed:11279158, ECO:0000269|PubMed:18801050, ECO:0000269|PubMed:21296186}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- MIOREX complex component 2
- Coenzyme Q-binding protein COQ10
Sequence:
MVTNMVKLRNLRRLYCSSRLLRTIQNGRISSVSSISLSKKYTTKSAKEGEENVERKHEEEKKDTLKSSSVPTSRISRLFHYGSLAAGVGMNAAAKGISEVAKGNSPTWKSLILSDSNIDRITNKFSKMRGVALKIGQLLSFQDEKVLPKELYEILSRVQNSANHMPQRQLEKVMAKELGANWKTKFSKFDKIPMAAASIGQVHAAELPSGQRVVVKIQYPGVKESIDSDLNSLLMLLTASSLLPKGLFLDKTIANARTELKWECDYNREARALQKFEALLKDDPAFEVPHVFPEYTTDNIITMTRMEGTEIMKLPKASQETKNFISENIMRLCLEEIATFKYMQTDPNWANFLYNGRTKKIELLDFGASRPFAEDFILKYRKLLTYATLRDRKGAYEMSVQLGYLTGLESQSMKDAHVDSVLTLGEPFRGDVDKSFDFKDQTVSDRIRGNIGLMLNERLCPPPEETYSLHRKFSGIFLLCARMGASVHCAKLFKEIFAYKV