wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ homolog subfamily C member 30, mitochondrial (Williams-Beuren syndrome chromosomal region 18 protein) (Q96LL9)
Organism: Homo sapiens (Human)
Function: Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration (By similarity). Associates with the ATP synthase complex and facilitates ATP synthesis (By similarity). May be a chaperone protein involved in the turnover of the subunits of mitochondrial complex I N-module. It facilitates the degradation of N-module subunits damaged by oxidative stress, and contributes to complex I functional efficiency.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30318146}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase flavoprotein 3, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
Sequence:
MAAMRWRWWQRLLPWRLLQARGFPQNSAPSLGLGARTYSQGDCSYSRTALYDLLGVPSTATQAQIKAAYYRQCFLYHPDRNSGSAEAAERFTRISQAYVVLGSATLRRKYDRGLLSDEDLRGPGVRPSRTPAPDPGSPRTPPPTSRTHDGSRASPGANRTMFNFDAFYQAHYGEQLERERRLRARREALRKRQEYRSMKGLRWEDTRDTAAIFLIFSIFIIIGFYI
Protein: Replication initiation control protein YabA (P37542)
Organism: Bacillus subtilis (strain 168)
Function: Involved in initiation control of chromosome replication.
Subcellular location: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_01159, ECO:0000269|PubMed:15927750, ECO:0000269|PubMed:16461910, ECO:0000269|PubMed:19737352, ECO:0000269|PubMed:21170359, ECO:0000269|PubMed:26615189, ECO:0000269|PubMed:29619013}. Note=Localizes in tight foci, most of which correspond to the replisome at mid-cell throughout the cell cycle (PubMed:15927750, PubMed:16461910, PubMed:19737352, PubMed:21170359, PubMed:26615189, PubMed:28166228, PubMed:29619013). When replication is blocked foci are also lost (PubMed:19737352). Correct positioning relies on interactions with both DnaA and DnaN, tested by mutagenesis (PubMed:16461910, PubMed:18506095). Positioning does not rely on DnaA, tested in a dnaA deletion strain (PubMed:19737352). Positioning does not rely on the C-terminus of SSB (ssbA) (PubMed:21170359). {ECO:0000255|HAMAP-Rule:MF_01159, ECO:0000269|PubMed:15927750, ECO:0000269|PubMed:16461910, ECO:0000269|PubMed:18506095, ECO:0000269|PubMed:19737352, ECO:0000269|PubMed:21170359, ECO:0000269|PubMed:26615189, ECO:0000269|PubMed:28166228, ECO:0000269|PubMed:29619013}.
Interaction partners:
- Beta sliding clamp
- Chromosomal replication initiator protein DnaA
- DNA polymerase III subunit delta'
- Stage 0 sporulation protein YaaT
- Probable RNA methyltransferase YabB
- Uncharacterized protein YaaR
- Cyclic di-AMP receptor A
- Ribosomal RNA small subunit methyltransferase I
- UPF0213 protein YazA
- Thymidylate kinase
Sequence:
MDKKELFDTVINLEEQIGSLYRQLGDLKQHIGEMIEENHHLQLENKHLRKRLDDTTQQIEKFKADKKESKTQKTEQTDIGEGYDNLARLYQEGFHICNVHYGSVRKEDCLFCLSFLNKK
Protein: Protein HOTHEAD (Protein ADHESION OF CALYX EDGES) (Q9S746)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable FAD-dependent enzyme. Involved in regulating post-genital organ fusion. Required to limit cellular interactions between contacting epidermal cells during floral development.
Interaction partners:
- At3g10570
- Cytochrome P450 86A2
- Cytochrome P450 86A4
- Cytochrome P450 86A7
- Cytochrome P450 86A8
- Cytochrome P450 86B1
- Cytochrome P450 like protein
- Cytochrome P450 86A1
- Peroxygenase 2
- Cytochrome P450 704B1
Sequence:
MALKLFLFALLLCLPTSLSSTASKGKEKKSKFNPYRYTFIDKASTFSSSSSSSFSSNGQDSSYDYIVIGGGTAGCPLAATLSQNFSVLVLERGGVPFTNANVSFLRNFHIGLADISASSASQAFVSTDGVYNARARVLGGGSCINAGFYSRADAAFVKRAGWDPKLVKESYPWVEREIVHQPKLTLWQKALRDSLLEVGVRPFNGFTYDHVSGTKIGGTIFDRFGRRHTAAELLAYANPQKLRVLIYATVQKIVFDTSGTRPRVTGVIFKDEKGNQHQALLSNRKGSEVILSSGAIGSPQMLMLSGIGPKKELQRLKIPVVLENEHVGKGMADNPMNTILVPSKAPIEQSLIQTVGITKMGVYVEASTGFGQSPESIHTHYGIMSNKNELFSTIPAKQRRPEATQAYITRNKYQLHEAFNGSFILEKLAYPISRGHLSLVNTNVDDNPSVTFNYFKHPVDLQRCVEAIRLVSKVVTSNRFLNYTQCDKQNVHKMLSLSVKANINLRPKQLNDTKSMAQFCKDTVVTIWHYHGGCLVGKVVSPNRKVLGVDRLRVIDGSTFDESPGTNPQATMMMMGRYMGVKILRERLGNKAGV
Protein: Spanin, outer lipoprotein subunit (o-spanin) (P39503)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex (By similarity).
Subcellular location: Host cell outer membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Periplasmic side {ECO:0000250}.
Interaction partners:
Sequence:
MIKLSAVILSIGLLVGCSTKPLEVKKETVHPNWPVQIKSYDEAKLSWQVKVIDGKAWVGMPFEDSQEFRIWLNDVKRYVHDQKTMXCYYRQELKEDKCK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q57YQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEPFSTILGTDGSGGRCKYLNKGIVGLGSYGEAYVAESVEDGSLCVAKVMDLSKMSQRDKRYAQSEIKCLANCNHPNIIRYIEDHEENDRLLIVMEFADSGNLDEQIKLRGTGDARYFQEHEALFLFLQLCLALDYIHSHKMLHRDIKSANVLLTSTGLVKLGDFGFSHQYEDTVSGVVASTFCGTPYYLAPELWNNKRYNKKADVWSLGVLLYEIMGMKKPFSASNLKGLMSKVLAGTYAPLPDSFSSEFKRVVDGVLVADPNDRPSVREIFQIPYINKGLKLFVQALKKNERISDSVKEVLVTQVSEILSSEVSPDAHRFLVSQINYDVTHRGHVNKLGGGNGKSWKPRFLQIVRGQLILTDDEEGNNPKGLNLEQVQGACPVPHSTAKRDFVFALNTVGGKGMWFQAVSHGDMEMWVHAIQRGIGVA
Protein: Protein transport protein bet1 (O13932)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Protein transport protein sec22
- Integral membrane protein sed5
- Protein transport protein gos1
- Protein transport protein bos1
- Synaptobrevin homolog ykt6
- Protein sly1
- Intracellular protein transport protein uso1
- Probable vesicular-fusion protein sec17 homolog
- Syntaxin pep12
- Synaptobrevin homolog 1
Sequence:
MGSRFGRRKERNGDMLPLYESQSPQHLDSLENENDERISKLTGKVKSLKELTMNIGTEITSSTKLMESMNDSFDSTKSLLSGTMTRLKNVSKNGGISIWMWLAFFCLVALILVLVRF
Protein: Shikimate dehydrogenase (NADP(+)) (SDH) (EC 1.1.1.25) (Q5HNV1)
Organism: Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 / CCUG 31568 / BM 3577 / RP62A)
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It can also use NAD to oxidize shikimate.
Interaction partners:
- Shikimate kinase
- 3-dehydroquinate synthase
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 3-dehydroquinate dehydratase
- GTP-binding protein, putative
- Probable nicotinate-nucleotide adenylyltransferase
- bis
- CRM domain-containing protein
- Chorismate synthase
- Ribosomal silencing factor RsfS
Sequence:
MKFAVIGNPISHSLSPLMHHANFQSLNLENTYEAINVPVNQFQDIKKIISEKSIDGFNVTIPHKERIIPYLDDINEQAKSVGAVNTVLVKDGKWIGYNTDGIGYVNGLKQIYEGIEDAYILILGAGGASKGIANELYKIVRPTLTVANRTMSRFNNWSLNINKINLSHAESHLDEFDIIINTTPAGMNGNTDSVISLNRLASHTLVSDIVYNPYKTPILIEAEQRGNPIYNGLDMFVHQGAESFKIWTNLEPDIKAMKNIVIQKLKGEL
Protein: Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-specific-processing protease 16) (Q6PAW2)
Organism: Xenopus laevis (African clawed frog)
Function: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}.
Interaction partners:
Sequence:
MVKKRGTNLPAQDFLDAEPVCKHLRKALDDGSVKRALVNVEWTMCQDCQADNKEKNNSEDESAEDPSVWLCLKCGHRGCGRNSVAQHALNHYNTPRSEPHCLVLNVDMWSAWCYLCDNEVPYNRTSRLGQLVDYLQRKAKAKNKNSNSVVSNEEVKTEIVTENEVKKIQYQDEKPDVQAKQEKASSTQKISTEPTVKGLSNLGNTCFFNAVMQNLSQTPALSELLNEVKTFRKPVTVLLPDSSSPKILEVNLEQQPGPLTLAMWQFLTEMHETKKGVVTPKELFSQVCKKAIRFKGYQQQDSQELLRYLLDGMRGEEIQRVTLAMSKSLQSTLDEEEIKKIVKDYEKRRTIPNFVDCLFGGELTSTIMCEECHTVSLVHEPFLDLSLPVLDDLIVKKNSKSTPPARERKEEEEEEENDDDRYVKERDEVSPGASKHLQKKAKKAAKKQAKNQRRQQKWQGKTVLFTDLAKQECSEDEEEVSQTKTNTRPDNETPTADGLNTMETDLSTLENGNEESADGLNTMETDLSTLENGNEEMAGGFKTMEMDLSTLENGSETIKSAVEGITEHTDLDSSVHNNVGSVETNALVGNMENNNNIEVNKTPERTAGSGGDSMEAMAAVENGNADAVNVDDTEAVNGLIDSANMDHELTNSLNRLQLSSDLEPTQVEIEILPDKEQPHTQVYEVVNEDPKTAFSTLSNRKDLPIDEFSVLSCLYQFTHKETLTGNNKLLCNVCTRKQASRLNNSNKGEKKFVYTNAKKQMLVSNPSPILTLHLKRFQQNGFNLRKINRHIKFPEVLDLAPFCTAKCKNVPEGESRLLYSLYGVIEHSGSMRSGHYTAFVKLRHPNQQLCKMLFTGVIPEVSGSEPGQGSWYHISDSHVQAVSLSRVLSSQAYLLFYERML
Protein: ABC transporter G family member 15 (ABC transporter ABCG.15) (Q55GB1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ABC transporter C family member 14
- ABC transporter C family member 2
Sequence:
MDSNENKKNGGDSLELNIINNNNDNNNNNDNNNNSTEEHIESVEQSIKEFNNVANELETEFRDYLVETHKNDVNNIKNDIEAPPSGEFEPGGGAEDEDFKLRNYFKQSKVDAIQNGGKLKKMGVSFKNLTVIGKGADQSVVSDLATPFTFLISKLNVKNWFKKSKPSTFDILHDVSGFCKDGEMLLVLGRPGSGCSSLLRTISNQTGSYVDVLGSVTYGGIDQKKWDKYKAECIYVPEEDTHYPTLTVRETLEFALKCKTPSNRLPNEKKRTFRSKIFNLLLGMFGMVHQAETMVGNEFVRGLSGGERKRITIAESMVSASSINCYDCSTRGLDAASALDYAKSIRIMSDTLHKTTIASFYQASDSIYNLFDRVLILEKGRCVYFGPVGLAKQYFIDMGFECEPRKSTPDFLTGVTNPQERKVRPGFTVPESSAEFEEAWKQSEIYAQSCQEQREYEKLIEIEQPSIDFIQEITEQKSKSTSKSSPYTTGFFVQVIALTIRNFQIIWGDKFSLISRYSSVLVQAPIYGSVFFAMSNSIDGAFTRGGAIFSSILFNALLSEQELSITFTGRRILQKHKTYAMYRPAALHFAQIITEIPIIMIQVFLFSIVTYFMFGLDSSGSKFFINCFTLIGFTLATNNLYRLAGNLTPSVYIGQNIMNVLFLTMMTFTSYIIPYHQMPVWFGWYHYCNPFSFAFRALMGNEFNGLKFDCIEDAIPKGEFYQNETFTPYRSCATTAAEPGQLYFTGERYLEKSFGWEIKPSTQGFIAYNICIVYGFWILFIICNCIVLNIIDWTSGGFTCKVYLKGKAPKMNDVENEKQQNLLVQQATNNMKESLSMPGGLFTWQHMYYSVPIGGNTMKLLLDDIQGWIKPGQMTALMGSSGAGKTTLLDVLAKRKTTGQVQGTTLLNGKPLEIDFERITGYVEQMDVLNPALTVRETLRFSAKLRGEPTISLEEKFKYVEQVLEMMEMKHLGDALIGDLETGVGISVEERKRTTIGVELVAKPHILFLDEPTSGLDAQSSYNIIKFIRKLADAGMPLVCTIHQPSSVLFEHFDRILLLAKGGKTVYFGDIGEKSKTLTSYFQRHGVRECSDSENPAEYILEACGAGRHGKSVVDWPQAWKESPEYQSICQELKELQVTGSSYASIHVDNGKPREYATSLTYQTIEVYKRLNLIWWRSPGYSYGTFIQSALVGLINGWTFYNLQDSANDMNQRIFFIFNVTMLGILLMFLVLPQFITQQDYFKRDYASKFYHWLPFALSIIVVELPFVLVSGTIFFFCSFWTAGLNSDASTNFFFWLIFMLFLFYCVGFGQAIGAVCINITVALNLLPVLIIFLFLFCGVLVIPDQIPHFWKWVYHLNPCTHFLEAMVTNVLKHVNVVCTTDDLIKFVKPSSFSTCSDYAFEFLNGSNHSVSGSVQSLGGDNCGYCLYKNGEEYYSKLGWSYDNRWRGFGIIAGYFVLNIFLVVLFVFLTRKGKR
Protein: F-box/LRR-repeat protein 3 (F-box and leucine-rich repeat protein 3A) (F-box/LRR-repeat protein 3A) (Protein after-hours) (Protein overtime) (Q8C4V4)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:26776516}. Cytoplasm. Note=Predominantly nuclear.
Interaction partners:
- Cryptochrome-2
- Cryptochrome-1
- S-phase kinase-associated protein 1
- Cullin-1
- Period circadian protein homolog 2
- Casein kinase I isoform epsilon
- Basic helix-loop-helix ARNT-like protein 1
- Circadian locomoter output cycles protein kaput
Sequence:
MKRGGRDSDQDSAEEGTAEKPKRPRTTQERSQPCDWGNLLQDIVLHVFKYLPLLDRAHASQVCRNWNQVFHMPDLWRCFEFELNQPATSYLKATHPELIKQIIKRHSNHLQYVSFKVDSSKESAEAACDILSQLVNCSLKTLGLISTARPSFMDLPKSHFISALTVVFVNSKSLSSLKIDDTPVDDPSLKVLVANNSDTLKLLKMSSCPHVSPAGILCVADQCHGLRELALNYHLLSDELLLALSSEKHVRLEHLRIDVVSENPGQTHFHTIQKSSWDAFIKHSPKVNLVMYFFLYEEEFDPFFRYEIPATHLYFGRSVSKDVLGRVGMTCPRLVELVVCANGLRPLDEELIRIAERCKNLSAIGLGECEVSCSAFVEFVKMCGGRLSQLSIMEEVLIPDQKYSLEQIHWEVSKHLGRVWFPDMMPTW
Protein: RAB6-interacting golgin (Q57VN9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSSVLTRSFSSCAGKLEETRELIKRDLETARKHRIELRKTIDDDLKRVEKERAELLGIVEEQEAKINRSVREFEEVRSRREWLKKEHDEAVKRYVKMSDTVTFIKEGDKRLQDRTDFEAVLEEENTTWADRERQLIASVSTHNTTLKQARKERRKEVETLETELAEMTKKLEQERIARREDLQQESQGLLRSRRGTPQPPSQRPTVAAVHTQAFEPLEANRKEQQFIAINKSSCLPTRQIRSCFKNNNSTGGNRFSNELETGRNTVANRRRSTNGSGSTGQGVSQHFHSAPVSRATSQSLVSGDSENIVKIRGAASQRAFSYADTKRVAGRKHELLRDSTNI
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (Q93934)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368116}.
Interaction partners:
- Purine nucleoside phosphorylase
- adenosine deaminase
- Adenine phosphoribosyltransferase
- AMP deaminase
- Adenylate kinase
- Adenylosuccinate lyase
- Probable adenylate kinase isoenzyme ZK673.2
- Probable 3',5'-cyclic-AMP phosphodiesterase pde-4
- Uridine and thymidine phosphorylase
- Adenylate kinase isoenzyme 1
Sequence:
MSPLPENTLIGMCNPLLDIQTTVEKAFLDKWGLKENDAILCDDKHNDMFTELTRDFKVEYIPGGAAQNSLRVAQWILNAPNRTVFFGAVGKDQYGDLLASKAKEAGVNVHYQINETVKTGTCAALINGTHRSLCAHLAAANTFTQDHLQKEENQKIIEQAKYFYVTGFFITVCPPAILQLASHSAEFNKTFTLNLSAPFISQFFFDKLSEIIPLVDVLFGNEDEAAAFAKANGWETTCVKEIALKAAALPKKSTKPRLVVFTQGPEPVIVVEGDKVTEFPVTRLPKEEIVDTNGAGDAFVGGFLSQFIQGKGVEASVTCGSYAAQEIIKKHGCTVPSVCKYH
Protein: Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic (PPIase CYP26-2) (EC 5.2.1.8) (Cyclophilin of 26 kDa 2) (Cyclophilin-26-2) (F4HTT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000305}.
Interaction partners:
- UPF0235 protein At5g63440
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic
- Thylakoid lumenal protein TL20.3
- Mitochondrial transcription termination factor family protein
- Putative chloroplast RNA binding protein family protein)
- Pentatricopeptide repeat-containing protein At1g01970
- Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic
- Probable membrane metalloprotease ARASP2, chloroplastic
- At2g27680/F15K20.22
Sequence:
MMQPNAKLLSPSAKFLPSPIEPPQHNRRTTVGAPPSLERNCKLSRRNLSKSSLLLLLTTQTTLTPLLDFSKAQADTIANPNLTNCENRIPTKKAFIDVSIDGEPIGRIIIGLYGDDVPAGTARFSSIVSGKAGITYRRKDFVKIMPGYVQHGGIRSYGVDAERATAAVGSLQNLIEEWERGKRGEICNVNKAGSVGIVVRDPSKPPPKTKLVARNGKLVVEEEVIAVGPNGTEFVITAVDSPELEDSVLVIGKVLEGMGVVEKMREVKTVRDNTSSPYFRVAKVIGDKRAVVAERGFNRPYSKVVVTNCGLIESQTL
Protein: Growth/differentiation factor 5 (GDF-5) (Bone morphogenetic protein 14) (BMP-14) (Cartilage-derived morphogenetic protein 1) (CDMP-1) (Lipopolysaccharide-associated protein 4) (LAP-4) (LPS-associated protein 4) (Radotermin) (P43026)
Organism: Homo sapiens (Human)
Function: Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8 (By similarity). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:11276205}. Cell membrane {ECO:0000269|PubMed:11276205}.
Interaction partners:
- Bone morphogenetic protein receptor type-1B
- Bone morphogenetic protein receptor type-1A
- Noggin
- Bone morphogenetic protein receptor type-2
- Activin receptor type-2A
- Activin receptor type-2B
- Chordin
- C-X-C chemokine receptor type 4
- Repulsive guidance molecule A
- Neuroblastoma suppressor of tumorigenicity 1
Sequence:
MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 7.1.1.2) (A2QJ32)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364066}; Matrix side {ECO:0000256|RuleBase:RU364066}.
Interaction partners:
Sequence:
MISRAAAPSSSIASLSSRSLRAQAPAARSFATVQDNAPPVKHYGGLKDQDRIFTNLYGHHGADLKSAMKYGDWHRTKDIVLKGHDWLISELKASGLRGRGGAGFPSGLKYSFMNFKDWDKDPRPRYLVVNADEGEPGTCKDREIMRKDPQKLIEGCLVVGRAMNANAAYIYIRGEFYQEATVLQRAINEAYEAGLIGKNACGTGYDFDVYIHRGMGAYVCGEETSLIESIEGKAGKPRLKPPFPAAVGLFGCPSTVTNVETVAVTPTIMRRGASWFSSFGRERNAGTKLFCISGHVNNPCTVEEEMSISLRELIDRHCGGVRGGWDNLLAVIPGGSSTPVLPKTICDDQLMDFDALKDSQSGLGTAAVIVMDKSTDIVRAISRLSTFYKHESCGQCTPCREGSKWTMQMMQRMEKGQAREREIDMLQELTKQVEGHTICALGEAFAWPIQGLIRHFRPELEARIREYSKEVGGNGPYAGGWHPEARAEGKLISPGM
Protein: Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.260) (18S rRNA (pseudouridine(1189)-N1)-methyltransferase) (18S rRNA Psi1189 methyltransferase) (Essential for mitotic growth protein 1) (Nucleolar essential protein 1) (Q06287)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1189 (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp-modification at the N3-position of U1191. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 (RPS19A/RPS19B) during the formation of pre-ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11694595, ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:20972225}.
Interaction partners:
- Nucleolar protein 58
- KRR1 small subunit processome component
- Essential nuclear protein 1
- Ribosomal RNA-processing protein 9
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 20
- U3 small nucleolar RNA-associated protein 13
- U3 small nucleolar RNA-associated protein 18
- U3 small nucleolar RNA-associated protein MPP10
- rRNA processing protein RCL1
Sequence:
MVEDSRVRDALKGGDQKALPASLVPQAPPVLTSKDKITKRMIVVLAMASLETHKISSNGPGGDKYVLLNCDDHQGLLKKMGRDISEARPDITHQCLLTLLDSPINKAGKLQVYIQTSRGILIEVNPTVRIPRTFKRFSGLMVQLLHKLSIRSVNSEEKLLKVIKNPITDHLPTKCRKVTLSFDAPVIRVQDYIEKLDDDESICVFVGAMARGKDNFADEYVDEKVGLSNYPLSASVACSKFCHGAEDAWNIL
Protein: Saxitoxin and tetrodotoxin-binding protein 1 (Q90WJ7)
Organism: Takifugu pardalis (Panther puffer) (Tetraodon pardalis)
Function: Binds both saxitoxin and tetradotoxin. May play a role in toxin accumulation and/or excretion.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGAVPGVVLLLMLAVLGIRAAPAPEECHKLTKPVTKADVQSVSGDWVLVWSVANTTERWICENLTSSYVEFKLHSDIIEYTERNLFLGNSCISFYSNLSASTEKQQQFSLNNLQMEEKGVVRPFNDNGTVKFFETCVDCLSMEYSGDIGRFLLIYRRDGVHQNVEVLKAAQDESQKLAECLGFSIDEPFIYDGVSDFCHKKSPEECHKLTKPVTKADVQSVSGDWVLVWSIDENSTISDDWKKLKTSYVEQRVDSGVIRFTERNMLKNNSCMTFKTNMTAGPESQNTFIYTSGKMEENGVVTVLDENGTVKFFETCADCLSMEYSGFFGHFLLIYRRDGVHQNVEVLKAAQDESQKLAECLGFSIDEPFIYDGVSDFCHKKSSPEVKPEQD
Protein: Ectonucleoside triphosphate diphosphohydrolase 4 (NTPDase 4) (EC 3.6.1.15) (EC 3.6.1.6) (Golgi UDPase) (Lysosomal apyrase-like protein of 70 kDa) (Uridine-diphosphatase) (UDPase) (EC 3.6.1.42) (Q9Y227)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner, with a preference for pyrimidines. Preferentially hydrolyzes UTP and TTP. AMP, ADP, ATP and UMP are not substrates. Preferentially activated by Ca(2+) over Mg(2+).
Subcellular location: [Isoform 1]: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:10393803}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:10393803}; Multi-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:9556635}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nucleoside diphosphate phosphatase ENTPD5
- Ectonucleoside triphosphate diphosphohydrolase 6
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ectonucleoside triphosphate diphosphohydrolase 8
- Ectonucleoside triphosphate diphosphohydrolase 3
- AMP deaminase 3
- Adenylosuccinate synthetase isozyme 1
- Bifunctional purine biosynthesis protein ATIC
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Inosine triphosphate pyrophosphatase
Sequence:
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGRLTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDIRQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTAGMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHIEDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKNLLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAALWMEEGLPAQNAPGTL
Protein: Probable ubiquitin carboxyl-terminal hydrolase 8 (EC 3.4.19.12) (Deubiquitinating enzyme 8) (Ubiquitin thioesterase 8) (Ubiquitin-specific-processing protease 8) (Q09738)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- SAGA complex subunit Spt7
- Histone acetyltransferase gcn5
- SAGA complex subunit Sgf29
- SAGA complex subunit Sus1
- SAGA complex subunit Sgf73
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex subunit Spt8
- SAGA complex subunit Sgf11
- SAGA complex subunit Ngg1
Sequence:
MPGDVEGCQHLKLKPADVENYQKICTQIFSCHFVPRRCSTCKRINKRSIRCLSCHSVGCLWGHHGEEHAMEHTHMIGVDVKNGHTYCFGCQDYVYQTELETLRFKIKNIKAWQSDHKRLPEKYNQMVCLEAYRKYPPVCATAGLRGIQNLGATCFMSVILQSILHNPLVRNLFFSGFHTSTDCKRPTCMTCAIDDMFSSIYNSKNKSTFYGPTAVLNLMWKLSKSLCGYSQQDGHEFFVYLLDQMHTESGGGTSMPCTCPIHRIFSGSLKNVVTCLDCKKERVAVDPLMDISLDINEPTLQGCLERFVSKEKVQYSCHSCGSKNAIKQLVFDKLPPTICMQLKRFEQNNFAMSTKIDKQVSYPAFLRMRYNFNQDDVDYQLYSVVCHKGTLDTGHYIAYTYYQNQWFLLDDTTIVEVKESEVLNSQAYLLFYHERQILYSDEMTVKTEN
Protein: RWD domain-containing protein 2B (P57060)
Organism: Homo sapiens (Human)
Interaction partners:
- Growth arrest and DNA damage-inducible protein GADD45 gamma
Sequence:
MKIELSMQPWNPGYSSEGATAQETYTCPKMIEMEQAEAQLAELDLLASMFPGENELIVNDQLAVAELKDCIEKKTMEGRSSKVYFTINMNLDVSDEKMAMFSLACILPFKYPAVLPEITVRSVLLSRSQQTQLNTDLTAFLQKHCHGDVCILNATEWVREHASGYVSRDTSSSPTTGSTVQSVDLIFTRLWIYSHHIYNKCKRKNILEWAKELSLSGFSMPGKPGVVCVEGPQSACEEFWSRLRKLNWKRILIRHREDIPFDGTNDETERQRKFSIFEEKVFSVNGARGNHMDFGQLYQFLNTKGCGDVFQMFFGVEGQ