wanglab/gogpt-training-data huggingface dataset:
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) (Q61578)
Organism: Mus musculus (Mouse)
Function: Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Adrenodoxin, mitochondrial
- Ferredoxin-2, mitochondrial
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Cysteine desulfurase
- Bis
- LYR motif-containing protein 4
- Electron transfer flavoprotein subunit beta
- Cytochrome b5 reductase 4
- Steroidogenic acute regulatory protein, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
Sequence:
MAPRCWHWWRWSAWSGLRPSPSRSTPTPGFCQKFSTQEKTPQICVVGSGPAGFYTAQHLLKHHTHAHVDIYEKQLVPFGLVRFGVAPDHPEVKNVINTFTQTARSDRCAFQGNVVVGRDVSVPELREAYHAVVLSYGAEDHQPLGIPGEELPGVVSARAFVGWYNGLPENQELAPDLSCDTAVILGQGNVALDVARILLTPPEHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQVAFTIKELREMIQLPGTRPILDPSDFLGLQDRIKDVPRPRRRLTELLLRTATEKPGVEEAARQALASRAWGLRFFRSPQQVLPTPDGQRVAGIRLAVTSLEGVGESTRAVPTGDVEDLPCGLLLSSVGYKSRPIDPSVPFDPKLGVIPNTEGRVVNVPGLYCSGWVKRGPTGVITTTMTDSFLTSQALLEDLKAGLLPSGPRPGYVAIQALLSNRGVRPVSFSDWEKLDAEEVSRGQGTGKPREKLVDRREMLRLLGH
Protein: Transcriptional activator PmfR (Q8GAH9)
Organism: Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans)
Function: Transcriptional regulator involved in the activation of the purU-mabO-folD-nepA-nepB and mao-ORF55-nbr operons implicated in the nicotine catabolic pathway. The sequence GTTT-14 bp-AAAC seems to be the core binding site of the regulator upstream of the -35 promoter region of the operon.
Interaction partners:
Sequence:
MEQQVLTVRDLVTAQSLGMKVLSGAGGLDRQVLWAHSCELSDPDRWLGPHELLMTVGLCVPHSAVEQRNFIVKLDEAGLSGVALGDHNSLPPLTRELYEEADRRSFPVLLTNQATPFAAIGRTVAAATATTQTMQVLKLSKLYQLSTYARTDPLRMMNDLQALLRAGLSVFDVQTGLTIVEGAPLEFMPTSVRERTYALPGDSDSRLMISEYPGEEVSSFLLIHVLQVIDVALSQLLRSLRRRSERSTQMLASIFEGRSPDGLGSILGPSGTSSGYQFVAVALEDSEKVARAASIKSLPVLAGPGSSSFFILMPEQSRNDVRNLLHGLDVRAGVSSTYLDLRDAKAAADEAAKIFSSGGTNGLWTDFTGVPVSLLTRSRKEASAIVQQVLGRLAGTDPKITVLRETLFAFLANDRRWNETAAALGIHRQTLSYRLTRIKEITGRDIASSADLSAFWLAFQAWPSFSDRSD
Protein: Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10) (P0A7E3)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Ribose-phosphate pyrophosphokinase
- Carbamoyl phosphate synthase small chain
- NAD
- Dihydroorotase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
Sequence:
MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDLDLPYCFNRKEAKDHGEGGNLVGSALQGRVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV
Protein: Cleavage and polyadenylation specificity factor subunit 4 (EC 3.1.-.-) (Cleavage and polyadenylation specificity factor 30 kDa subunit) (Protein clipper) (Q9VPT8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity. Binds RNA polymers with a preference for G- and/or C-rich clusters. Binds single-stranded DNA non-specifically.
Subcellular location: Nucleus {ECO:0000269|PubMed:9512528}.
Interaction partners:
- Factor interacting with poly
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 1
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor 73
- Cleavage stimulation factor 64 kD subunit
- LD24014p
- polynucleotide adenylyltransferase
- Cleavage stimulation factor subunit 1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MDILLANVSGLQFKAERDLIEQVGAIPLPFYGMDKSIAAVCNFITRNGQECDKGSACPFRHIRGDRTIVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSRFNACHNKECPFLHIDPQSKVKDCPWYKRGFCRHGPHCRHQHLRRVLCMDYLAGFCPEGPSCKHMHPHFELPPLAELGKDQLHKKLPTCHYCGELGHKANSCKQYVGSLEHRNNINAMDHSGGHSGGYSGHSGHIEGADDMQSNHHSQPHGPGFVKVPTPLEEITCYKCGNKGHYANKCPKGHLAFLSNQHSHK
Protein: Nuclear pore complex protein Nup75 (Nucleoporin Nup85) (A1YK11)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
Sequence:
MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVKHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAEANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQSNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKSMPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPDLEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKPFELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLPALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKRSYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSASELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENVDEIMNLLRLACARNLARALIIENTLPVV
Protein: Outer membrane lipoprotein RcsF (P69411)
Organism: Escherichia coli (strain K12)
Function: Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00976, ECO:0000269|PubMed:16740933, ECO:0000269|PubMed:23813676}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00976, ECO:0000269|PubMed:16740933, ECO:0000269|PubMed:23813676}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_00976, ECO:0000269|PubMed:16740933, ECO:0000269|PubMed:23813676}.
Interaction partners:
- Phosphotransferase RcsD
- Outer membrane protein assembly factor BamA
- Sensor histidine kinase RcsC
- Outer membrane protein A
- Putative membrane protein IgaA homolog
- tRNA
- Transcriptional regulatory protein RcsB
- Lipoprotein-releasing system transmembrane protein LolC
- Lipoprotein-releasing system transmembrane protein LolE
- Transcriptional regulatory protein RcsA
Sequence:
MRALPICLVALMLSGCSMLSRSPVEPVQSTAPQPKAEPAKPKAPRATPVRIYTNAEELVGKPFRDLGEVSGDSCQASNQDSPPSIPTARKRMQINASKMKANAVLLHSCEVTSGTPGCYRQAVCIGSALNITAK
Protein: Ependymin (B5X393)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MRTFVLLMCLAVGCLAQVPHTCRSPPLLTGALSVANEKFYANAKYTYDAMLKRIRFKEIGSYENKTFGVDALLLFREGVMYTINHRNKTCKKERLKREDFHPMEIPADAALLGQVILGSSSGPGQGLLVNTWYGEVATPSGEDKWMSTFTEFGCIPVSSTYYTDKTGWILTTFFNIVVGITDPQEFFPPKFCQDAKLDETAEAANFYSIFKNLTKYS
Protein: RE23868p (Q9VB93)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Peptidase S1 domain-containing protein
- Jonah 25Bii, isoform A
- IP10831p
- Serine protease 3
- Zinc carboxypeptidase A 1
- Lipase
- RE56633p
- Trypsin beta
- Jonah 25Biii
- Trypsin epsilon
Sequence:
MMKLFLALAFCVLAANAVEVRVNGENGWYVPQADGTMEWMDREFAEAYLETKNRMEGRNVLNPVTFYLYTNSNRNSPQEIKATSASISGSHFNPNHPTRFTIHGWSSSKDEFINYGVRDAWFTHGDMNMIAVDWGRARSVDYASSVLAVPGVGEQVATLINFMRSNHGLNLDNTMVIGHSLGAHVSGYAGKNVKNGQLHTIIGLDPALPLFSYDSPNKRLSSTDAYYVESIQTNGGTLGFLKPIGKGAFYPNGGKSQPGCGVDLTGSCAHSRSVIYYAESVTENNFPTMRCGDYEEAVAKECGSSYSSVRMGATTNAYMVAGDYYVPVRSDAPYGMGN
Protein: Zinc finger protein 950 (A0A0U1RNP3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAVTYDEVHVNFTQEEWALLDHSQKSLYRDVMLETYKNLTAIGYNWDDHNIEEHCQSSRRHGRHETSHPGEKPSQYTHCGKAFVYWSHPQRHERIHTGEKPYGCNHCGQHFLNLPQILPTEKD
Protein: ITPR interacting domain containing 2 (E7EUL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEDHLLRTASQHSDSSGFAEDSTDCLSLNHLQVQESLQAMGSSADSCDSETTVTSLGEDLATPTAQDQPYFNESEEESLVPLQKGLEKAAAVADKRKSGSQDFPQCNTIENTGTKQSTCSPGDHIIEITEVEEDLFPAETVELLREASAESDVGKSSESEFTQYTTHHILKSLASIEAKCSDMSSENTTGPPSSMDRVNTALQRAQMKVCSLSNQRMGRSLLKSKDLLKQRYLFAKAGYPLRRSQSLPTTLLSPVRVVSSVNVRLSPGKETRCSPPSFTYKYTPEEEQELEKRVMEHDGQSLVKSTIFISPSSVKKEEAPQSEAPRVEECHHGRTPTCSRLAPPPMSQSTCSLHSIHSEWQERPLCEHTRTLSTHSVPNISGATCSAFASPFGCPYSHRHATYPYRVCSVNPPSAIEMQLRRVLHDIRNSLQNLSQYPMMRGPDPAAAPYSTQKSSVLPLYENTFQELQVMRRSLNLFRTQMMDLELAMLRQQTMVYHHMTEEERFEVDQLQGLRNSVRMELQDLELQLEERLLGLEEQLRAVRMPSPFRSSALMGMCGSRSADNLSCPSPLNVMEPVTELMQEQSYLKSELGLGLGEMGFEIPPGESSESVFSQATSESSSVCSGPSHANRRTGVPSTASVGKSKTPLVARKKVFRASVALTPTAPSRTGSVQTPPDLESSEEVDAAEGAPEVVGPKSEVEEGHGKLPSMPAAEEMHKNVEQDELQQVIREIKESIVGEIRREIVSGLLAAVSSSKASNSKQDYH
Protein: Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3) (A4Q9E5)
Organism: Mus musculus (Mouse)
Function: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction. Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions. Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development. Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:33414192}.
Interaction partners:
Sequence:
MQGVSSALLLSAGQLGPGAAWYRQEGSSECSWLRRSQPSELRTNFSSRWPWPRNSESRRSERLQWPGPASAKPEVASCGDSRRDYSSLPARHLSSARESSMPGALGTVNPQPVRTLVPPTLDEPLPDALRPPDDSLLLWRGLTKGPNHMGRLRNAKIHVERAVKQKKIFMIHGRYPVIRCLLRQRGWVEKKMVHPPGTALPAPQKDLDSSMLGDSDATEDEDEEENEMFRESQLLDLDGFLEFDDLDGIHALMSRMVRNETPYLIWTTRRDVLDCRFLSKDQMINHYARAGSFTTKVGLCLNLRNLPWFDEADADSFFPRCYRLGAEDDKKAFIEDFWLTAARNVLKLVVKLEEKSQSISIQAREEEAPEDTQPKKQEKKLVTVSSDFVDEALSACQEHLSSIAHKDIDKDPNSPLYLSPDDWSQFLQRYYQIVHEGAELRYLEVQVQRCEDILQQLQNVVPQLDMEGDRNIWIVKPGAKSRGRGIMCMNRLDEMLKLVDCNPMLMKDGKWIVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQRHLEASCHRHPMLPPDNMWSSQRFQAHLQEVDAPKAWSSVIVPGMKAAVIHALQTSQDNVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRRLDRSCDTGAFELIYKQPAVEVPQYVGIRLLVEGSTIKKPVPVGHRRTGVRSSLPHLLTQQGSGESKDSGSPTHRSASRKNARAESLEHTEKPEPAAVASVSGKGKKAPFHFPSLHSKAWLPSPRVHRPQGRVLRLQHDQLVGSKALSTTGKALMTLPTAKVLMSFPPHPDLKLAPSMLKPGKVGFELCCTTWRVVLSGGIGEEGHRQRAAPRPSSAPGKGLSSTEPCSKTET
Protein: LD40489p (SR family splicing factor) (Splicing factor 2, isoform A) (Splicing factor 2, isoform B) (Q9V3W7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD32469p
- U1 small nuclear ribonucleoprotein 70 kDa
- Eukaryotic initiation factor 4A-III
- Transformer-2 sex-determining protein
- RNA-binding protein 8A
- RNA-binding protein Rsf1
- Heterogeneous nuclear ribonucleoprotein A1
- RNA-binding protein 1
- Serine/arginine repetitive matrix protein 1
- Protein mago nashi
Sequence:
MGSRNECRIYVGNLPPDIRTKDIQDLFHKFGKVTFVDLKNRRGPPFAFVEFEDARDADDAVKARDGYDYDGYRLRVEFPRGGGPGSYRGGNRNDRSRDGGGRMGGRGPPAKRSQYRVMVTGLPASGSWQDLKDHMREAGDVCFADTYKDGSGVVEFLRHEDMKYAIKKLDDSRFRSHEGEVAYIRVREDSGDNDRGGGGGGSGGGGGGSGGGGSRDYRDRSRSRSFSSRPRRRGTPTYSPVRRQSYSRSRSRSNY
Protein: Beta amyloid protein-like protein (Q4ZHV6)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MTRAVLFISVFTIFLDVLHAGQASSGAEPQVAVLCEAGSTYHPQYMSAAGRWTPDLTTKPHNCLKDKMEILDYCKKVYPSHDITNIVEASHYVKVSNWCKLGTSNAAKCKVTRWVKPFRCLEGPFQSDALLVPESCLFDHIHNQSRCWQFARWNATAGRACAQRGLRLRTFAMLLPCGISLFSGVEFVCCPKHFKENVKMHKPMDVGVPVSPGGEDMLAASAAMDERDDDLLDDDDALDDDDDDDTLNLSDDDDDDDADDDMDEDEDADLSRDDDAEDDDYTDADDSAWPRPESSSSPSTTTSTTTTTTTTTASTATSDPYFSHFDPRTEHQSYKDAQQRLEETHREKITKVMKEWSELEDRYQAMMSADPAAAQTFRQRMTAKFQANVQSLEEEGVAERRRLAALHQQRVLAHLAQRRRTALACYTRSLRDTPPNAHRVQKCLQRLVRALAAERSGALAAWRRAAAAGREAAAAERTSAADRLQDADRALQRALTALRRRPHLYASIGTAIEDYVQSMQSKDDMAVSLMSMTPEAEELLLDRIEAEVQREQAAREQLSVKRDQRARQRQDIQNERAKTSNGVKESEESDDEASEPSENETSTAAPTPTSAPSSPASATPAPSAAPVSVHDITTRSGFTQDTTTTEMITTTVTDAPESETAETIEASETTSRRSTSETEGEGLRAALEHAEERAPPPPAHALKHELQHSQPGYTVRGAGPSGAGGAGGSGALYPALCVGGAALAAAACVALAVARRRDRAPHAQGFVQVEQTGVVAPTPEERHVANMQINGYENPTYKYFEVKE
Protein: Lethal(3)malignant brain tumor-like protein 4 (H-l(3)mbt-like protein 4) (L(3)mbt-like protein 4) (L3mbt-like 4) (Q8NA19)
Organism: Homo sapiens (Human)
Function: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MKQPNRKRKLNMDSKERLDQDGRLEQAEEEKKPKDSTTPLSHVPSAAAQGAWSWEWYLKEQKAVAAPVELFSKDQSFPEHENGFQIGMRLEGIDPRHPSVFCVLSVAEVCGYRLRLHFDGYLSCYDFWTNAGSPDIHPVGWCEKTKHELHIPKGYRKDKFVWMDYLKACKLQNAPKKLFRNRSPNGPMSKEFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYVQPVGWCQENGRTLIAPQGYPNPENFSWTEYLEATQTNAVPAKVFKMRLPHGFLPNMKLEVVDKRNPRLIRVATIVDVDDQRVKVHFDGWDHKYDYWVEADSPDIHPIGWCDVTGHPLEVPQRTNDLKILPGQAVCPTPGCRGIGHIRGPRYSGHHSAFGCPYSDMNLKKEATLHDRLREQTQANLESDSSHSKSKSLCSLNFNGKHEKVNSQPRLVQQAKCLKIKGKEDIDLDNLFRVLVLHPRGLEYSVEQAQQVLHQSVSMSTVSAHPFRDLPLGREQHCKLLPGVADIRASQVARWTVDEVAEFVQSLLGCEEHAKCFKKEQIDGKAFLLLTQTDIVKVMKIKLGPALKIYNSILMFRHSQELPEEDIASGQEVRG
Protein: CCR4-NOT transcription complex subunit 2 (F8VQF4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLKEVAQVTNSMFGASRKKFVEGVDSDYHDENMYYSQSSMFPHRSEKDMLASPSTSGQLSQFGASLYGQQNGSENVTGLDLSDFPALADRNRREGSGNPTPLINPLAGRAPYVGMVTKPANEQSQDFSIHNEDFPALPGSSYKD
Protein: Uncoordinated protein 58 (Q22271)
Organism: Caenorhabditis elegans
Function: Has a role in mobility, possibly in the transport of potassium in muscles.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel domain-containing protein
- RING-type domain-containing protein
Sequence:
MFFYSPNVAPQPSSTSHRRPTLTHQHHLHVGHLDTRLSVQIPEILSRSLVHDPERTRLVPEQLRFIIDENQELWTGSQPPTGFLELCASPVSSVFSNADARRMSQRKLVLRRPTISIQEDGKIIIDHVTARWEGANINSQSALLDADDGATVITDTIKDDQDDKEPKSCPQQTVKYIKILTPHVILVSVLIGYLCLGAWILMLLETRTELLARSKKLVRLTNLMSNFTAESWKMLNNAQHGVSNMDEGEWAATFREWMVRVSETVDDRRPIRRELNRPDDLSNMHNKWTFPTAILYVLTVLTTCGYGEVSVDTDVGKVFSVAFALVGIPLMFITAADIGKFLSETLLQFVSFWNRSVRKVKQWMSRIRHGRRKSLQSTGGPNDTLDILGVDGTEEKLWFPIGAYVSCICIYCSIGSAMFITWERTWSFIHAFHFGFNLIVTVGLGDIVVTDYIFLSLIVAFVIVGLSVVTMCVDLASTHLKAYFTRIHYFGRAKRFLGMSEELKEIVALLGAMRRKKGGKVTWNDVRDFLDNELRDRPFEPHELLMKLRFIDETSSGMSTIRHNSFQSDFFRESEYIRRVAALRPEQPAYL
Protein: Cys2/His2 zinc finger protein (Q62788)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTKLQEAVTFRDVAVVFSKEEMGLLDAAQRKLYHDVMLENLRNLLAVGGQSPNKMKTVDATGVRCLLLGQLLYWEITGHDANKLARAPEAVVHTQGKGSHFLEQGHSSCHREAEEPRRPSEDDSSLDSLTRDHSSTTENQEFLSGRAQGSWCKTHLRKRQNHQKHCLQTLMKNKPELLTQHSPVQRTQEDSRHSSSVPIQQSVHPGRKRYWCHECGKGFSQSSALQTHRRVHTGEKPCRDNSCRKSFSRSSGLSIHRQVHTGERPYRCKVCGKGFLRWSHLQAHERIHTGEKPYKCGECGKRFSCISNLHTHQRFHSKEKPYKCDKCGKCFSLNFNLHIHQRVHTGEKPYKCEECGKCFSLSFNLHSHQRVHTGEKPYKCEECGKCFSSASSFQRHRQIHIKEKTLHRDVCGKGSSRDSNLQTHQRVHIQEKPYRCNSCGKSFRCSMDLNIHRRVHTGEKPYKCEVCGKGFNYLSHLQAHEKIHADQKPYKCEYCGRRFSYSSNLHTHQRVHTGEKPYKCEECGKSFSLASSLQAHQRVQTGKKPFKCNACQKRFSQAWNLQAHQRVHTGEKPYKCDTCGKAFGQRSSLQIHQRIHTGEKPFKCEECGKEFSLNSGLTAHRRVHTGEKPYECTECGKGFSLASSLRTHQRIHTGEKPFQCNECQKRFSQVSHLQSHQRVHTGEKPYKCDTCGKAFSQKSGLQVHRRIHTGEKPFKCEECGKEFIWSSGLSAHRRVHTGEKTLHG
Protein: Protein MAL2 (Q969L2)
Organism: Homo sapiens (Human)
Function: Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway.
Subcellular location: Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Endomembrane system. Cytoplasm, perinuclear region. Note=Associated with lipid rafts. In polarized epithelial cells, restricted to the apical surface. In hepatocytes, as well as in polarized hepatoma Hep-G2 cells, found in the canalicular membrane, equivalent to the apical surface, beneath the canalicular actin cytoskeleton. In non-polarized Hep-G2 cells, distributed to the perinuclear region.
Interaction partners:
- Tumor protein D52
- Tumor protein D54
- Polymeric immunoglobulin receptor
Sequence:
MSAGGASVPPPPNPAVSFPPPRVTLPAGPDILRTYSGAFVCLEILFGGLVWILVASSNVPLPLLQGWVMFVSVTAFFFSLLFLGMFLSGMVAQIDANWNFLDFAYHFTVFVFYFGAFLLEAAATSLHDLHCNTTITGQPLLSDNQYNINVAASIFAFMTTACYGCSLGLALRRWRP
Protein: Mitochondrial protein C2orf69 (Q8N8R5)
Organism: Homo sapiens (Human)
Function: May play a role in the respiratory chain.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:33945503}.
Interaction partners:
Sequence:
MWGFRLLRSPPLLLLLPQLGIGNASSCSQARTMNPGGSGGARCSLSAEVRRRQCLQLSTVPGADPQRSNELLLLAAAGEGLERQDLPGDPAKEEPQPPPQHHVLYFPGDVQNYHEIMTRHPENYQWENWSLENVATILAHRFPNSYIWVIKCSRMHLHKFSCYDNFVKSNMFGAPEHNTDFGAFKHLYMLLVNAFNLSQNSLSKKSLNVWNKDSIASNCRSSPSHTTNGCQGEKVRTCEKSDESAMSFYPPSLNDASFTLIGFSKGCVVLNQLLFELKEAKKDKNIDAFIKSIRTMYWLDGGHSGGSNTWVTYPEVLKEFAQTGIIVHTHVTPYQVRDPMRSWIGKEHKKFVQILGDLGMQVTSQIHFTKEAPSIENHFRVHEVF
Protein: Possible two component system response transcriptional positive regulator PhoP (P71814)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- histidine kinase
- Sensor-type histidine kinase PrrB
- Sensor-like histidine kinase SenX3
- 6 kDa early secretory antigenic target
- Redox- and pH-responsive transcriptional regulator WhiB3
- Sensor histidine kinase TrcS
- Sensor histidine kinase component HK1
- Probable sensor histidine kinase TcrY
- Sec-independent protein translocase protein TatC
- Long-chain-fatty-acid--AMP ligase FadD26
Sequence:
MRKGVDLVTAGTPGENTTPEARVLVVDDEANIVELLSVSLKFQGFEVYTATNGAQALDRARETRPDAVILDVMMPGMDGFGVLRRLRADGIDAPALFLTARDSLQDKIAGLTLGGDDYVTKPFSLEEVVARLRVILRRAGKGNKEPRNVRLTFADIELDEETHEVWKAGQPVSLSPTEFTLLRYFVINAGTVLSKPKILDHVWRYDFGGDVNVVESYVSYLRRKIDTGEKRLLHTLRGVGYVLREPR
Protein: MEF2 transcription factor homolog (Q9U325)
Organism: Caenorhabditis elegans
Function: Transcription regulator. Binds specifically to the MEF2 element, 5'-[TC]TA[AT][AT][AT][AT]TA[AG]-3' in the regulatory elements of target genes, such as chemoreceptors str-1 and srh-234. Involved in transduction of sensory signals, together with egl-4, kin-29 and hda-4; binding to histone deacetylase hda-4 enables negative modulation of chemoreceptor gene expression in chemosensory neurons. In response to starvation, negatively modulates expression of chemoreceptor srh-234 in ADL sensory neurons, acting in concert with basic helix-loop-helix (bHLH) transcription factors. Plays a role in regulating muscle sensitivity to acetylcholine (ACh) and the magnitude of presynaptic ACh release via a retrograde signal, perhaps by indirectly decreasing Ras-related protein Rab-3 activity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Histone deacetylase 4
- Mitogen-activated protein kinase pmk-3
- Serine/threonine-protein kinase kin-29
- Mitogen-activated protein kinase pmk-2
- Mitogen-activated protein kinase pmk-1
- Serpentine Receptor, class H
- Pry-1 Interacting and CABIN1 Domain containing
Sequence:
MGRKKIQITRIQDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIVFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNNDIMEALNRKEGNQGGGNSDDESPGPSTSPVIQITMPAVVNGHSSNNSVASAASASAAAVAAAAAAVAAVEGTSSGAAAAAAALQASNAQRHHNLNLYQNLIFNPNYTRHLNQRNDPLSSTSVAPSSSSSKHLDFPPSTSFAYDTSRLHPIAAADADCDLVPSSRAAADQNIWSSALQQRPVSQPAPSISNSSTNGISNGTSSLLSPNVSSLNGHSVLDLGGPNLPYKLDPNTYVKMEPHSPPEKRPRITTEWRPQQLT
Protein: V-type proton ATPase 16 kDa proteolipid subunit c 1 (V-ATPase 16 kDa proteolipid subunit c 1) (Vacuolar proton pump 16 kDa proteolipid subunit c 1) (Q21898)
Organism: Caenorhabditis elegans
Function: Proton-conducting pore forming 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 and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad. This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization. The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates. Lysosomal acidification also leads to changes in mitochondrial morphology and function. Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity. In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance. Plays a role in the processing and secretion of the aspartic protease hrg-7 from the intestine. During embryonic development, the V-ATPase is required to repress fusion of epidermal cells probably by negatively regulating eff-1-mediated cell fusion. Involved in receptor-mediated endocytosis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit
- Probable V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 2
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B 1
- ATP synthase subunit a
- Oligomycin sensitivity conferral protein
Sequence:
MSTDTKQIIADALLKNEQAMYGPFFGSLGVTSAMAFAAAGSAYGTAKAGTGIASMAVARPDLVMKAIIPVVMAGIVAIYGLVVAVIVSGKVEPAGANYTINNAFSQFAGGLVCGLCGLGAGYAIGIAGDAGVRALSQQPRMFVGMILILIFAEVLGLYGMIVALILGAT
Protein: NADH-ubiquinone oxidoreductase subunit NUO2 (Q5AEI1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit MCI4
- NADH dehydrogenase 1 alpha subcomplex subunit
- Nuo1p
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- 4Fe-4S ferredoxin-type domain-containing protein
- Fesur1p
Sequence:
MSGGPVPVWKKYTTRPQGIWEKIRQLLVLVPNRSSGNPLVSLFRQVPPGERIKEAQNYKDPVTIPAGDIKGNPYFKRDYRRNYPQVHTFNQTKISGLLNLGSESNPRISIGEKGNKELAVFTNGQDVSLASTLKSVPASVVKGEVLGKSGEPIVAPSLNKFKWEILPEPVHGMYSEAYPCRIFTEKKVRSQSSA