wanglab/gogpt-training-data huggingface dataset:
Protein: Protein CLEC16A (C-type lectin domain family 16 member A) (Q2KHT3)
Organism: Homo sapiens (Human)
Function: Regulator of mitophagy through the upstream regulation of the RNF41/NRDP1-PRKN pathway. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. The RNF41/NRDP1-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which regulates proteosomal degradation of PRKN. Plays a key role in beta cells functions by regulating mitophagy/autophagy and mitochondrial health.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q80U30}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q80U30}. Lysosome membrane {ECO:0000250|UniProtKB:Q80U30}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q80U30}. Note=Associates with the endolysosome membrane. {ECO:0000250|UniProtKB:Q80U30}.
Interaction partners:
- E3 ubiquitin-protein ligase NRDP1
- GPN-loop GTPase 1
- Dexamethasone-induced protein
- Dimethyladenosine transferase 1, mitochondrial
- SH2B adapter protein 3
- Tyrosine-protein phosphatase non-receptor type 2
Sequence:
MFGRSRSWVGGGHGKTSRNIHSLDHLKYLYHVLTKNTTVTEQNRNLLVETIRSITEILIWGDQNDSSVFDFFLEKNMFVFFLNILRQKSGRYVCVQLLQTLNILFENISHETSLYYLLSNNYVNSIIVHKFDFSDEEIMAYYISFLKTLSLKLNNHTVHFFYNEHTNDFALYTEAIKFFNHPESMVRIAVRTITLNVYKVSLDNQAMLHYIRDKTAVPYFSNLVWFIGSHVIELDDCVQTDEEHRNRGKLSDLVAEHLDHLHYLNDILIINCEFLNDVLTDHLLNRLFLPLYVYSLENQDKGGERPKISLPVSLYLLSQVFLIIHHAPLVNSLAEVILNGDLSEMYAKTEQDIQRSSAKPSIRCFIKPTETLERSLEMNKHKGKRRVQKRPNYKNVGEEEDEEKGPTEDAQEDAEKAKGTEGGSKGIKTSGESEEIEMVIMERSKLSELAASTSVQEQNTTDEEKSAAATCSESTQWSRPFLDMVYHALDSPDDDYHALFVLCLLYAMSHNKGMDPEKLERIQLPVPNAAEKTTYNHPLAERLIRIMNNAAQPDGKIRLATLELSCLLLKQQVLMSAGCIMKDVHLACLEGAREESVHLVRHFYKGEDIFLDMFEDEYRSMTMKPMNVEYLMMDASILLPPTGTPLTGIDFVKRLPCGDVEKTRRAIRVFFMLRSLSLQLRGEPETQLPLTREEDLIKTDDVLDLNNSDLIACTVITKDGGMVQRFLAVDIYQMSLVEPDVSRLGWGVVKFAGLLQDMQVTGVEDDSRALNITIHKPASSPHSKPFPILQATFIFSDHIRCIIAKQRLAKGRIQARRMKMQRIAALLDLPIQPTTEVLGFGLGSSTSTQHLPFRFYDQGRRGSSDPTVQRSVFASVDKVPGFAVAQCINQHSSPSLSSQSPPSASGSPSGSGSTSHCDSGGTSSSSTPSTAQSPADAPMSPELPKPHLPDQLVIVNETEADSKPSKNVARSAAVETASLSPSLVPARQPTISLLCEDTADTLSVESLTLVPPVDPHSLRSLTGMPPLSTPAAACTEPVGEEAACAEPVGTAED
Protein: DNA-directed RNA polymerase, mitochondrial (MtRPOL) (EC 2.7.7.6) (O00411)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Has DNA primase activity. Catalyzes the synthesis of short RNA primers that are necessary for the initiation of lagging-strand DNA synthesis from the origin of light-strand DNA replication (OriL).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}.
Interaction partners:
- Dimethyladenosine transferase 2, mitochondrial
- Transcription factor A, mitochondrial
- Dimethyladenosine transferase 1, mitochondrial
- Transcription elongation factor
- Large ribosomal subunit protein bL12m
- GA-binding protein subunit beta-1
- Serum response factor-binding protein 1
- Twinkle mtDNA helicase
- Single-stranded DNA-binding protein, mitochondrial
- DNA-directed RNA polymerase I subunit RPA2
Sequence:
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSLPPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKPTLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVVRMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASDAEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSSRLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHSGAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQLFQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEALYRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS
Protein: Transmembrane protein 198 (Q6DFQ7)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Promotes lrp6 phosphorylation by casein kinases and thereby plays a role in Wnt signaling. May be a membrane scaffold protein involved in the self-aggregation of lrp6 further enhancing its activity. Required for neural crest formation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:21536646}. Cytoplasmic vesicle {ECO:0000269|PubMed:21536646}. Note=Largely located to vesicle-like structures.
Interaction partners:
Sequence:
MLQNIDNRTVDTGQDDPFDGFCSLESERHYDVVPTVVCSLCCLFGLVYTFFGYRCFKAIMFLSGLLAGSAVIFLLCYKERIMDTQLSLELSAGIALGIGLLCGLVTMLVHSVGLFMTGLLLGLLLAIASLVGLEQFYHPPSAWIPVGLMMGSAMLFAVLTLQWQKLFTVVSTATFGAAILTVCTDYFIELMLLVQYVYDRLRLETSHPLCWYSWVILGMWPVLSVLGIVVQWKLTAEGFSHTDVIISRRQKRLQLLRIRQKDAKKRQNVASQEGTYRRKANPMKRYTGDILAPSYLQSLRERQTGTGTSMSSLSTNMQTIVDMDYECGSTVPLTATTPVIHV
Protein: Calvin cycle protein CP12-2, chloroplastic (CP12 domain-containing protein 2) (Chloroplast protein 12-2) (Q9LZP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20399532}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
- Phosphoribulokinase, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic
- CHP-rich zinc finger protein-like
- At5g27290
- Pentatricopeptide repeat-containing protein At1g31920
- Probable CCR4-associated factor 1 homolog 7
Sequence:
MATIATGLNIATQRVFVTSENRPVCLAGPVHLNNSWNLGSRTTNRMMKLQPIKAAPEGGISDVVEKSIKEAQETCAGDPVSGECVAAWDEVEELSAAASHARDKKKADGSDPLEEYCKDNPETNECRTYDN
Protein: Pro-thyrotropin-releasing hormone (Pro-TRH) (Prothyroliberin) [Cleaved into: Thyrotropin-releasing hormone (TRH) (Protirelin) (TSH-releasing factor) (Thyroliberin) (Thyrotropin-releasing factor) (TRF)] (Q62361)
Organism: Mus musculus (Mouse)
Function: Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems.
Subcellular location: Secreted.
Interaction partners:
- Thyrotropin-releasing hormone receptor
- Thyrotropin-releasing hormone receptor
- Oxytocin-neurophysin 1
- Hypocretin neuropeptide precursor
- Pro-neuropeptide Y
- Neurotensin/neuromedin N
- Prolactin
- Prolactin-6A1
- Progonadoliberin-1
- Pro-opiomelanocortin
Sequence:
MQGPWLMMALALIFVLTGIPKSCALLEAAQEEGAVTPDLPGLEKVQVRPERRFLRKDLQRVRGDLGAALDSWITKRQHPGKREEKEEDVEAEERGDLGEVGAWRPHKRQHPGRRANQDKDSWSDEGDSDWLPPSWLPDFFLDSWFSDAPQVKRQHPGRRSFPWMESDVTKRQHPGRRFIDPELQRSWEETEGEEGGLMPEKRQHPGKRAVGHPCGPQGICGQTGLLQLLGDLSRGQETLAKQTPQLEAWVREPLEE
Protein: Plexin A (Q8T6S7)
Organism: Drosophila simulans (Fruit fly)
Interaction partners:
Sequence:
TLQHYNVPDGAGLSLVPKQSSIYNFSILSDKNEKSHKYETLNISKYTSSSPTFSRAGSPLNNDMHENGLRYWHLVKHHDSDMQKEGERVNKLVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDDQAQLHGITDPEVVHTWKSNSLPLRFWVNLIKNPNFVFDIHKSNIVDSCLSVVAQTFMDSCSTSDHRLGKDSPSSKLLYAKDIPEYRKWVDRYYRDIRDMSPISDQDMNAMLAEESRLHTTEFNTNCALHELYTYAV
Protein: SD23103p (Q86PE8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MILLNCLVICLCIFSCGAQDSSLDKLISDIFKTDETPKPSSPPPPVVNPKDSSGSTGSQNGGSSSTQYQSCGDQKECVPRWLCANDTINTSGDGIIDIRLGTDAECKNYLDLCCDLPNKRKDPIFEFKPDHPEGCGYQNPNGVGFKITGAVNQEAEFGEFPWMLAILREEGNLNLYECGGALIAPNVVLTAAHCVHNKQPSSIVVRAGEWDTQTQTEIRRHEDRYVKEIIYHEQFNKGSLYNDVAVMLLESPFTLQENIQTVCLPNVGDKFDFDRCYATGWGKNKFGKDGEYQVILKKVDMPVVPEQQCETNLRETRLGRHFILHDSFICAGGEKDKDTCKGDGGSPLVCPIAGQKNRFKSAGIVAWGIGCGEVNIPGVYASVAKLRPWIDAKLKIWSIDPRHYTP
Protein: Immunoglobulin kappa constant (Ig kappa chain C region) (Ig kappa chain C region AG) (Ig kappa chain C region CUM) (Ig kappa chain C region EU) (Ig kappa chain C region OU) (Ig kappa chain C region ROY) (Ig kappa chain C region TI) (P01834)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Protein: Conserved oligomeric Golgi complex subunit 3 (Component of oligomeric Golgi complex 3) (Q38AZ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 8
- COG4 transport protein middle alpha-helical bundle domain-containing protein
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 7
Sequence:
MCTSFDAEMLTDAEFSRLLDISLAPLSKSFQHALPISYATGGPGVPLEGDPWCGRSFPSLSQRRSVSMGAASKGCDAVRRSVHEGDEIAAETVLRAVARTGCETAVEGLQQWLERARHGRQMGERCLRVLKGLVDCLDSMRGVTVAVQEQSNKLSSNASELMVRKARLEMVQEELQRMIKHFSHIDALVREVEQQTLSATSQRYSSILQEMEEEMQFLTCHPQFLSTKAYTTKLAAAYQQAYQCLKDAIIFSIRTAQNCTLSADVYRSIFYGNQQRHQEGQETVTPSVDTGSNPLVMLLQAVLGGDMTSAHHLMAGMLASVDNVFCARLNEKASLRRLMEAHGGGRQPFEETNDDDIFDTYRDARVLIIGPVLKNWLEMMCGTSGGSVKEGNKTVPQFVGHLVGMMKLALEHEKEVFDGVWLREDFSARLFPQIVSDISGEEYHVFRSHLLQVDDLEVLAQTIEEIQRASAKQYSSAELSGLLTKMIQDTQERLVFRTSVFLRHSISQYTLTRDAAQQFLNHEASASDTYIPALTNCVTLLQLLYPSLEFPIFSVFAEEAINCTLLQVQELSKLVGQQAVEHAPLKGILCQLRHLLHLRDELSLIDENIIVVEKGIDLSKIALRRLEIVQSSRESKKDVESEIKLCTERAAQAILTAASSPLIGIARKAPGAVEPAVECARRLLADQEELLTIFITHASIRNAIMGPVRSRMDELLAEADTIRQQPQERRE
Protein: SNW domain-containing protein 1 (Nuclear protein SkiP) (Ski-interacting protein) (Q9CSN1)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Is required in the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13573}.
Interaction partners:
- Crooked neck-like protein 1
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-processing-splicing factor 8
- Pleiotropic regulator 1
- Peptidyl-prolyl cis-trans isomerase-like 1
- Protein BUD31 homolog
- Pre-mRNA-splicing factor RBM22
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor SYF2
Sequence:
MALTSFLPAPTQLSQDQLEAEERARSQRSLQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDPEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKEPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPIDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLEARIKTNRFVPDKEFSGSDRKQRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE
Protein: FCS-Like Zinc finger 17 (P0DO11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}. Cytoplasm {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}. Note=Shuttles from the cytoplasm to the nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
Interaction partners:
- FCS-Like Zinc finger 16
- FCS-Like Zinc finger 11
- FCS-Like Zinc finger 8
- FCS-Like Zinc finger 10
- FCS-Like Zinc finger 18
Sequence:
MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP
Protein: Cytochrome b-c1 complex subunit 1, mitochondrial (Complex III subunit 1) (Core protein I) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase 44 kDa protein) (P07256)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 10, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b
- Respiratory supercomplex factor 2, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW
Protein: Ripped pocket, isoform B (A0A0B4K691)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Pickpocket 17, isoform A
Sequence:
MTISDSELDSSKGIDLTFRRRRKAGSVACEGFITTYHEYCRNTSIHGVQYLGEQERPFRERIFWLFVFLISIYGCSTLIQSAYTKWTETPVIVSFAEKSTPVWNIPFPAVTVCSETKRVLKQKGKETTYADLYSQFSEDMRASRVFRPENVSALEMEEFRTLLHVCNTQIIEEDIPLIAGDDLDYFDVLQRMLPQFDRYFFYCRWLSRFGECETFFRKTLTEEGICYTFNGLRATEIYRDDTYQYQHSGEPLEMENISSQHTAWTLETGYALDSDVETFPARVLSAGARSGIFLALQSFKQEVDYACRGPVQGFKVGKFENVLLHAPDDVPQVSKQFVRIPMGKEVLIAVKPNMITMSSGIAEYHPVRRQCFLSHERSLRFFKVYTESNCQLECLANFTLTKCGCVKFSMPRNVDMPVCGEDKIHCYDRAERELLVREFKRVKALNAGRENSRSVESACNCMPACTSLVYNTEISQANFDLEEMLVAEGDTEFLKEYPGSQMSRLSIYFKQSQFITSKRSELYGMTEFLANCGGIFGLFMGFSILSLVEMIYHFTLRLFTNLKRLVKG
Protein: Transcriptional adapter 1 (SPT3-associated factor 42) (STAF42) (Transcriptional adapter 1-like protein) (Q96BN2)
Organism: Homo sapiens (Human)
Function: Probably involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11564863}.
Interaction partners:
- Transcription factor SPT20 homolog
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
- Transcription initiation factor TFIID subunit 9
- Transformation/transcription domain-associated protein
- TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L
- STAGA complex 65 subunit gamma
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcription initiation protein SPT3 homolog
- Histone acetyltransferase KAT2B
Sequence:
MATFVSELEAAKKNLSEALGDNVKQYWANLKLWFKQKISKEEFDLEAHRLLTQDNVHSHNDFLLAILTRCQILVSTPDGAGSLPWPGGSAAKPGKPKGKKKLSSVRQKFDHRFQPQNPLSGAQQFVAKDPQDDDDLKLCSHTMMLPTRGQLEGRMIVTAYEHGLDNVTEEAVSAVVYAVENHLKDILTSVVSRRKAYRLRDGHFKYAFGSNVTPQPYLKNSVVAYNNLIESPPAFTAPCAGQNPASHPPPDDAEQQAALLLACSGDTLPASLPPVNMYDLFEALQVHREVIPTHTVYALNIERIITKLWHPNHEELQQDKVHRQRLAAKEGLLLC
Protein: L-ornithine N(5)-monooxygenase (OMO) (EC 1.14.13.196) (L-ornithine N(5)-oxygenase) (Q9P7T0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as ferrichrome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Hydroxamate-type ferrichrome siderophore peptide synthetase
- Putative lysine N-acyltransferase C17G9.06c
- Iron-sensing transcriptional repressor
- Iron transport multicopper oxidase fio1
- 4-nitrophenylphosphatase
- Low affinity heme transporter str3
Sequence:
MTEPLDLAIIGFGPASLSFLIALHDHSEEPLKNKKIRVFEKLPTFSWHEGMLIPGSNMQISFVKDLATPRDPTSYFTFLNYLHSHGQERLSGFLNMSTLEPSRYEYHDYLCWAASHFSKFVEYNANINKLHYDAATDLYIVGHGDTQWQAKNIIITTGCQPYIPPLYKSVDSPLIVHSSKFMSDHSQKLLRNSKHGILVVGCGQSAAEIWKHCHYSLDPKTPLAMCFRNLAPVPSDSSPFVNSLYFDSHNSHWWYNLPTEARLKGLSVGRTTNYSVVKESLLEEMFKECYLQKLRYGQEFHQIMGDTDIQSIKNEGDHLVVQLTSQMDKSKKPETRKIDVLYVATGYDHESFDVLMSSLFPNSQGAQISEEYCVLNAPSKQGKVYVAGITSNQHGIGETLLSWAAIRAGGLAKELFGPSKPTARVPASYLN
Protein: R3H-associated N-terminal domain-containing protein (Q583V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTVSANDDPVNESFCTAYNSSKKEGDETTSAQVSDSTAPRVTPVPLTTPRHAKKQRLNRRIEVTDTSADRITVTDALQQHTREVLTVHNGPVVYEEQMIFHPYELYKHGKNKIHTGSVGYSSGADLVMLRDAVSEPSDADLAYVRRSAEIGSVICLDPKAQRPLTETEEEEQKKNKKRLAGAGYRKYPGIRAPKNRKVRNRLLNTYLATELGREILDNYREMQENGETDADQTPPLRPIFSDLPQVFYDILDLDEDAQTAALERYGVKIHAPAGNAQPKDPDSGEVRFQNLNSRLRGELVHAINSEFLSKQIEDLEQNFTAFIKSGDPSKSLTYRFRDGYGRLVCHGVAAYYKLVSQSHQQADGSKTTVVSWPKRKRKNTSSLTLPKITLKSLLRKKRNEMPHTPLQSSTLDTPLFDFNDGPTDMEPLDLGAAASNDANPDDWLQPLEPDGIMPVYQPFSLAYSIGNENSGTKQKGKKSKGTKTSN
Protein: Protein associated with UVRAG as autophagy enhancer (Pacer) (Protein Rubicon-like) (Q3TD16)
Organism: Mus musculus (Mouse)
Function: Regulator of autophagy that promotes autophagosome maturation by facilitating the biogenesis of phosphatidylinositol 3-phosphate (PtdIns(3)P) in late steps of autophagy. Acts by antagonizing RUBCN, thereby stimulating phosphatidylinositol 3-kinase activity of the PI3K/PI3KC3 complex (By similarity). Following anchorage to the autophagosomal SNARE STX17, promotes the recruitment of PI3K/PI3KC3 and HOPS complexes to the autophagosome to regulate the fusion specificity of autophagosomes with late endosomes/lysosomes (By similarity). Binds phosphoinositides phosphatidylinositol 3-phosphate (PtdIns(3)P), 4-phosphate (PtdIns(4)P) and 5-phosphate (PtdIns(5)P) (By similarity). In addition to its role in autophagy, acts as a regulator of lipid and glycogen homeostasis. May act as a tumor suppressor (By similarity).
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9H714}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H714}. Note=Associates with late autophagic structure. Recruitment to autophagosome membrane is promoted by autophagic stimuli. {ECO:0000250|UniProtKB:Q9H714}.
Interaction partners:
- Transmembrane and coiled-coil domain-containing protein 5B
- AFG2-interacting ribosome maturation factor
- Phosphopentomutase
- Pre-mRNA-splicing factor CWC25 homolog
- Protein limb expression 1 homolog
- Syntaxin-17
Sequence:
MVSQSIGWGDSPVDLCEGSNRAFQDTDQPACQLDVRLLRHKASWINPLCVQQPLQELCPQRPTVQSSENHVVLDTPSPLRLSILSYRDSLAEMPLSENTADVICSNSAHCSGGKEGDFFLATEEQEVHLQQESLLKNPKTVATSPSPKEGSARSESPHLTASTDDGDARSSSRSHAWNFFPLETFMLPADVEKENLHFYAADIIISVIENMKCNLPNQQQPERWDTEDASRLRGTGAEMTFYTHIKQEPGSSASSHTGCEGCAALQVSPVAETLSYCPVAGEACKHDLNKLVMLELGKYNDITKGCRCSYNSSKSATCESNLSPAGCLARELFRGFCKCWMLSEVNCQLPGSPTTASSGVGDEEYAEEDFDSSVDAAREVMLKSRVPGTEDWVLPRCQIILTVHPPIKRDIAVVAQNFFCAGCGTPIQPKFVKRLRYCEYLGKYFCASCHSSAESCIPARILTMWDFRKYQVSDFSKWLLDSVWHQPVFKLLGGHHSLYAKAKELDRVKDLQEQLFHIKKLLKTCRFADSVLKEFEQVPSHLTDECHIFSMDDFLRTKKGLLAPLLKDILRASLAHVDSCELCQGKGFICEFCQSTTVIFPFQTTTCRRCAACRACFHKQCFQSSRCPRCARIIARRQHLESLPTAAT