wanglab/gogpt-training-data huggingface dataset:
Protein: AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200) (E9Q7E2)
Organism: Mus musculus (Mouse)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00858}.
Interaction partners:
- Bromodomain-containing protein 7
- PHD finger protein 10
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Protein polybromo-1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF complex subunit SMARCC2
- Bromodomain-containing protein 9
Sequence:
MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSSVFGEEWREKTDRDFVKFWKDIVDDNEVRDLISDRNKAHEDTPGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEESNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFRTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVTSTLEVLYMLTEMGDVACTKIAKVEKSIDVLVCLVSMDAQMFGPDALAAVKLIEHPSSSHQVLSEIRPQAIEQVQTQTHIASGPASRAVVAQHAAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSTSSGQAHIHVIGVKRRALPLPIQMYYQQQPISTPVVRVDAVADLSPTPSPAGIPHGPQAAGNHFQRTPVTNQSSNLTATQMSFPVQGIHTVAQTVSRIPPNPSVHTHQQQNSPVTVIQNKAPIPCEVVKATVIQNSVPQTAVPVSISVGGAPAQNSVGQNHSAGPQPVTVVNSQTLLHHPSVMPQPSPLHTVVPGQVPSGTPVTVIQQTVPQSRMFGRVQSIPACTSTVSQGQQLITTSPQPMHTSSQQTAAGSQPQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQVVTIAGVPSPQPSRVGFQNIAPKPLPSQQVSPSVVQQPIQQPQQPAQQSVVIVSQPAQQGQAYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPPTNNQVPTAMSSSSTLQSQGPPPTVSQMLSVKRQQQQQHSPAAPAQQVQVQVQQPQQVQVQVQPQQPSAGVGQPAPNESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVANNQAAGFGVQGQTPAQQLLVGQQNVQLVQSAMPPAGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFATATVSQGNAAQLIAPAGLSMSGAQASAGLQVQTLPAGQSACTTAPLPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGTTNTSNGDTSESELQVGSLLNGRKYSDSSLPPSNSGKLQSETSQCSLISNGPSLELGENGAPGKQNSEPVDMQDVKGDLKKALVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPVEPQGTSGATQQDTAKGDQLERVSNGPVLTLGGSPSTSSMQEAPSVATPPLSGTDLPNGPLASSLNSDVPQQRPSVVVSPHSTAPVIQGHQVIAVPHSGPRVTPSALSSDARSTNGTAECKTVKRPAEDNDRDTVPGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAAQQKQQHPPTYMQSVAPQNTPMPPSPAVQVQGQPSSSQPSPVSASSQHADPVRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQVANQKSSTKQPTVGGTGSAPRAQKAIASHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEML
Protein: Very-long-chain enoyl-CoA reductase (EC 1.3.1.93) (Enoyl reductase TSC13) (Temperature-sensitive CSG2 suppressor protein 13) (Trans-2-enoyl-CoA reductase) (Q99190)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. VLCFAs serve for instance as precursors for ceramide and sphingolipids. Required for normal biogenesis of piecemeal microautophagy of the nucleus (PMN) bleps and vesicles during nutrient stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15958487}; Multi-pass membrane protein {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15958487}. Note=Accumulates at nucleus-vacuole (NV) junctions. Sequestred to NV junctions by NVJ1. Accumulates in nuclear PMN bleps and vesicles during stationary phase and nitrogen starvation. {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:15958487}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Fatty acid elongase 3
- Fatty acid elongase 2
- Nucleus-vacuole junction protein 1
- Fatty acid elongase 1
- Acyl-CoA desaturase 1
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- AP-1-like transcription factor YAP4
- Vacuolar protein 8
Sequence:
MPITIKSRSKGLRDTEIDLSKKPTLDDVLKKISANNHNISKYRIRLTYKKESKQVPVISESFFQEEADDSMEFFIKDLGPQISWRLVFFCEYLGPVLVHSLFYYLSTIPTVVDRWHSASSDYNPFLNRVAYFLILGHYGKRLFETLFVHQFSLATMPIFNLFKNCFHYWVLSGLISFGYFGYGFPFGNAKLFKYYSYLKLDDLSTLIGLFVLSELWNFYCHIKLRLWGDYQKKHGNAKIRVPLNQGIFNLFVAPNYTFEVWSWIWFTFVFKFNLFAVLFLTVSTAQMYAWAQKKNKKYHTRRAFLIPFVF
Protein: Myelin proteolipid protein (PLP) (Lipophilin) (P60201)
Organism: Homo sapiens (Human)
Function: This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24103481}; Multi-pass membrane protein {ECO:0000269|PubMed:24103481}. Myelin membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat. {ECO:0000250}.
Interaction partners:
- Proteolipid protein 2
- Myelin basic protein
- Myelin-oligodendrocyte glycoprotein
- Myelin-associated glycoprotein
- Transcription factor SOX-10
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Myelin-associated oligodendrocyte basic protein
- Myelin transcription factor 1
- Oligodendrocyte transcription factor 1
- Receptor-type tyrosine-protein phosphatase-like N
Sequence:
MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF
Protein: GldM (A5FIT0)
Organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
Interaction partners:
- GldL
- GldN
- GldK
- SprE
- SprT
- SprA
- GldJ
- GldO
- GldB
- GldD
Sequence:
MAGGKLTPRQKMINLMYLVFIAMLAMNVSKEVISAFGLMNEKFEAANTSSVTTNESLLTSLDQKAAEAKGEFAKAAETAHKVQAASKEFYDYIGTLKTQAVKGFEVDKETGKMPYEAMDRGDNIDDWFTGDGYTKKGNEIIAKIEKYKSDIKAALGTDKKYAGIISEVEKKFDVSDVKNKEGIKEKYLAYHFKGFPAIASAAKLSAWQNDVKKTEADVYNSALGKAAVAAASYSNYQAIVVLDKNAYFQGEKVTGKVVLGRYDENTKPTSFQGPGQIVNGQAVISLTAGGVGEQDINGQFTFLEDGKNIPLKFSGKYVVVPRPNSATISADKMNVVYRGVVNPISVSFAGVDANKIVASAPGLSSAGKPGKYNMSPGQGTEATISVTGTLPNGDKVTDKKTFRIKGIPGPTGTIRGEMGVVKGPKSNLEIATIGAKLLDFDFEVGLDVVGFNMKIAGQPTVVVTGNKMNAQCKSVLARAGKGDQVTISEIKTKLVGAGSYLLPRTAPVIYEIQ
Protein: ATP synthase subunit e, mitochondrial (Q08C42)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU367005}.
Interaction partners:
Sequence:
MVPPVHVSPLIKTARWSALLVGIIYGKRRYDNLKPIAEEERRIEEEEKKVREEQERIAKQLAEANEDTILK
Protein: Ras family GTPase (A0A1D8PCX9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Oxidant-induced cell-cycle arrest protein 5
- Serine/threonine protein kinase
- Mitotic regulator
- Tyrosine-protein phosphatase CDC14
- Serine/threonine-protein kinase
- Bfa1p
- Cell cycle protein kinase DBF2
- Uncharacterized protein
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine protein kinase
Sequence:
MEEDNQQDQNNQVALKIGLIGDSQIGKTSLMVKYVEGSFDEDYIQTLGVNFMDKKIQIRNTTITFSIWDLGGQKEFINMLPLVSNDAVAILFMFDLTRKSTLNSIKEWYRQVRGFNKTAIPFLVGTKYDQFIDLSFQDQIEITQQAKKFGSAMKAPVIFCSTSHSINVQKIFKIILSKAFDLKLNLDEIVNVGEPILIYK
Protein: DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) (Q8TEB1)
Organism: Homo sapiens (Human)
Function: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- Cullin-4B
- E3 ubiquitin-protein ligase RBX1
- DET1- and DDB1-associated protein 1
- DDB1- and CUL4-associated factor 8
- DDB1- and CUL4-associated factor 1
- DDB1- and CUL4-associated factor 12
- DDB1- and CUL4-associated factor 4
- POU domain, class 2, transcription factor 3
Sequence:
MGSRNSSSAGSGSGDPSEGLPRRGAGLRRSEEEEEEDEDVDLAQVLAYLLRRGQVRLVQGGGAANLQFIQALLDSEEENDRAWDGRLGDRYNPPVDATPDTRELEFNEIKTQVELATGQLGLRRAAQKHSFPRMLHQRERGLCHRGSFSLGEQSRVISHFLPNDLGFTDSYSQKAFCGIYSKDGQIFMSACQDQTIRLYDCRYGRFRKFKSIKARDVGWSVLDVAFTPDGNHFLYSSWSDYIHICNIYGEGDTHTALDLRPDERRFAVFSIAVSSDGREVLGGANDGCLYVFDREQNRRTLQIESHEDDVNAVAFADISSQILFSGGDDAICKVWDRRTMREDDPKPVGALAGHQDGITFIDSKGDARYLISNSKDQTIKLWDIRRFSSREGMEASRQAATQQNWDYRWQQVPKKAWRKLKLPGDSSLMTYRGHGVLHTLIRCRFSPIHSTGQQFIYSGCSTGKVVVYDLLSGHIVKKLTNHKACVRDVSWHPFEEKIVSSSWDGNLRLWQYRQAEYFQDDMPESEECASAPAPVPQSSTPFSSPQ
Protein: Uncharacterized membrane protein ArfC (P9WJG5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for wild-type expression of ArfA and ammonia secretion, not however part of an ammonia transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A1KH33}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peptidoglycan-binding protein ArfA
- Uncharacterized membrane protein ArfB
- Uncharacterized protein Rv3412
Sequence:
MEHVHWWLAGLAFTLGMVLTSTLMVRPVEHQVLVKKSVRGSSAKSKPPTARKPAVKSGTKREESPTAKTKVATESAAEQIPVAGEPAAEPIPVAGEPAARIPVVPYAPYGPGSARAGADGSGPQGWLVKGRSDTRLYYTPEDPTYDPTVAQVWFQDEESAARAFFTPWRKSTRRT
Protein: Expressed protein (Transmembrane protein) (Q9ZQQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGRSALIHLLRSQSRRLSSSTFTSGYHHRSIAGSWSSSVNPKVRFQVPSLSQRSWASFGAKTREDDDEHKISIGPQEKKEEKDGGVVYYGPISSTIKKVKLLSLSTCCLSVSLGPVITFMTSPGLNVIMKGAVASTVIFLSASTTAALHWFVSPYVHKLRWQPGSDTFEVEMMTWLGTFSAKTLKFSDIRYPDTQRPYVSFKADGNFYFVDADHCPNKALLARLTPPKDAHDSAFKNL
Protein: Fibroblast growth factor 2 (FGF-2) (Basic fibroblast growth factor) (bFGF) (Heparin-binding growth factor 2) (HBGF-2) (P48800)
Organism: Gallus gallus (Chicken)
Function: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (By similarity). Functions as a potent mitogen in vitro (By similarity). Can induce angiogenesis (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol (By similarity). Nuclear import from the cytosol requires the classical nuclear import machinery (By similarity). {ECO:0000250|UniProtKB:P09038}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Uncharacterized protein.
- Vascular endothelial growth factor receptor 2
- Collagen alpha-1
- Platelet-derived growth factor receptor alpha
- Epidermal growth factor receptor
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor
- Vascular endothelial growth factor receptor 1
Sequence:
MAAGAAGSITTLPALPDDGGGGAFPPGHFKDPKRLYCKNGGFFLRINPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRFLAMKEDGRLLALKCATEECFFFERLESNNYNTYRSRKYSDWYVALKRTGQYKPGPKTGPGQKAILFLPMSAKS
Protein: Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)] (P48445)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Acetyl-CoA carboxylase
- Biotin synthase, mitochondrial
- Acetyl-CoA carboxylase, mitochondrial
- Pyruvate carboxylase 1
- Pantoate--beta-alanine ligase
- Dethiobiotin synthetase
- Urea amidolyase
Sequence:
MNVLVYNGPGTTPGSVKHAVESLRDFLEPYYAVSTVNVKVLQTEPWMSKTSAVVFPGGADLPYVQACQPIISRLKHFVSKQGGVFIGFCAGGYFGTSRVEFAQGDPTMEVSGSRDLRFFPGTSRGPAYNGFQYNSEAGARAVKLNLPDGSQFSTYFNGGAVFVDADKFDNVEILATYAEHPDVPSSDSGKGQSENPAAVVLCTVGRGKVLLTGPHPEFNVRFMRKSTDKHFLETVVENLKAQEIMRLKFMRTVLTKTGLNCNNDFNYVRAPNLTPLFMASAPNKRNYLQEMENNLAHHGMHANNVELCSELNAETDSFQFYRGYRASYDAASSSLLHKEPDEVPKTVIFPGVDEDIPPFQYTPNFDMKEYFKYLNVQNTIGSLLLYGEVVTSTSTILNNNKSLLSSIPESTLLHVGTIQVSGRGRGGNTWINPKGVCASTAVVTMPLQSPVTNRNISVVFVQYLSMLAYCKAILSYAPGFSDIPVRIKWPNDLYALSPTYYKRKNLKLVNTGFEHTKLPLGDIEPAYLKISGLLVNTHFINNKYCLLLGCGINLTSDGPTTSLQTWIDILNEERQQLHLDLLPAIKAEKLQALYMNNLEVILKQFINYGAAEILPSYYELWLHSNQIVTLPDHGNTQAMITGITEDYGLLIAKELVSGSSTQFTGNVYNLQPDGNTFDIFKSLIAKKVQS
Protein: Interferon regulatory factor 5 (D3ZPU1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TNF receptor-associated factor 6
- C-C motif chemokine 4
- Myeloid differentiation primary response protein MyD88
- Signal transducer and activator of transcription 1
- Interleukin-1 beta
Sequence:
MNQSAPGIPTPPRRVRLKPWLVAQVNSCQYPGLQWVNGEKKLFYIPWRHATRHGPSQDGDNTIFKAWAKETGKYTEGVDEADPAKWKANLRCALNKSRDFQLYYDGPRDMPPQPYKIYEVCSNGPAPTESQPTDDYVLGEEEEEEDEELQRMLPGLSITEPVLPGPPIAPYSLPKEDTKWPPALQPPVGLGPPPPDPNLLAPPSGDSAGFRQLLPEVLEPGPLASNQPPTEQLLPDLLISPHMLPLTDLEIKFQYRGRPPRALTISNPQGCRLFYSQLEATQEQVELFGPVTLEQVRFPSPEDIPSDKQRFYTNQLLDVLDRGLILQLQGQDLYAIRLCQCKVFWSGPCALAHGSCPNPIQREVKTKLFSLEQFLNELILFQKGQTNTPPPFEIFFCFGEEWPDLKPREKKLITVQVVPVAARLLLEMFSGELSWSADSIRLQISNPDLKDHMVEQFKELHHIWQSQQRLQPMVQAPPVAGLDAGQGPWPMHPVGMQ
Protein: Signal recognition particle 54 kDa protein (Q385M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Signal recognition particle subunit SRP72
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L35, putative
- SRP19 protein
- Signal recognition particle subunit SRP68
- Signal recognition particle receptor alpha subunit, putative
- 60S ribosomal protein L5, putative
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S15a, putative
Sequence:
MVLAELGQKIGAAISKMSSKSFVGEDDVKEFLNEVARALLQADVNVKTVKELQQNVRAEVAITAEAAGLNKRKMLQTAVFNGIKKMLDPGVKPFIPAKGKTSIVMFVGLQGSGKTTSCTKYAAYFQRKGLKTGLVCADTFRAGAYDQLRQNATKAKVRFYGSLTEADPVIIAKEGVLELKKEKYDLIIVDTSGRHKQESALFEEMKQVQQAVKPNDIVFVMSATDGQGIEEQARQFKEKVPIGSVIVTKLDGQAKGGGALAAVAMTKSPIVFIGTGEHFDDFELFQPESFVSRMLGMGDMRALVDSMKDANIDTDSELYKRFQDGQFTLRDMYEHLQNVLKMGSVSKIMDMIPGMSGFTGNAGDAGDVTLKTFIHMMDSMTAAELDDSRVKKTMTPTRIHRIARGSGHTILEVHNLITSYTKFEDVVKKMGKVNFKAMTQDSSTAFSGKMGQQQVLQLAKALNPTMLRQIGGLTGLQDIMKQLQSIK
Protein: Cell division control protein 53 (Cullin-A) (E3 ubiquitin ligase complex SCF subunit CDC53) (Q12018)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cell division control protein 4
- Ubiquitin-conjugating enzyme E2-34 kDa
- RING-box protein HRT1
- SCF E3 ubiquitin ligase complex F-box protein GRR1
- F-box protein MET30 subunit MET30)
- Defective in cullin neddylation protein 1
- Protein phosphatase PP2A regulatory subunit B
- Protein SIC1
- NEDD8-like protein RUB1
Sequence:
MSETLPRSDDLEATWNFIEPGINQILGNEKNQASTSKRVYKILSPTMYMEVYTAIYNYCVNKSRSSGHFSTDSRTGQSTILVGSEIYEKLKNYLKNYILNFKQSNSETFLQFYVKRWKRFTIGAIFLNHAFDYMNRYWVQKERSDGKRHIFDVNTLCLMTWKEVMFDPSKDVLINELLDQVTLGREGQIIQRSNISTAIKSLVALGIDPQDLKKLNLNVYIQVFEKPFLKKTQEYYTQYTNDYLEKHSVTEYIFEAHEIIKREEKAMTIYWDDHTKKPLSMALNKVLITDHIEKLENEFVVLLDARDIEKITSLYALIRRDFTLIPRMASVFENYVKKTGENEISSLLAMHKHNIMKNENANPKKLALMTAHSLSPKDYIKKLLEVHDIFSKIFNESFPDDIPLAKALDNACGAFININEFALPAGSPKSATSKTSEMLAKYSDILLKKATKPEVASDMSDEDIITIFKYLTDKDAFETHYRRLFAKRLIHGTSTSAEDEENIIQRLQAANSMEYTGKITKMFQDIRLSKILEDDFAVALKNEPDYSKAKYPDLQPFVLAENMWPFSYQEVEFKLPKELVPSHEKLKESYSQKHNGRILKWLWPLCRGELKADIGKPGRMPFNFTVTLFQMAILLLYNDADVLTLENIQEGTSLTIQHIAAAMVPFIKFKLIQQVPPGLDALVKPETQFKLSRPYKALKTNINFASGVKNDILQSLSGGGHDNHGNKLGNKRLTEDERIEKELNTERQIFLEACIVRIMKAKRNLPHTTLVNECIAQSHQRFNAKVSMVKRAIDSLIQKGYLQRGDDGESYAYLA
Protein: Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-beta) (Diphosphoinositide kinase 2-beta) (Phosphatidylinositol 5-phosphate 4-kinase type II beta) (PI(5)P 4-kinase type II beta) (PIP4KII-beta) (PtdIns(5)P-4-kinase isoform 2-beta) (Q80XI4)
Organism: Mus musculus (Mouse)
Function: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Preferentially utilizes GTP, rather than ATP, for PI(5)P phosphorylation and its activity reflects changes in direct proportion to the physiological GTP concentration. Its GTP-sensing activity is critical for metabolic adaptation. In collaboration with PIP4K2A, has a role in mediating autophagy in times of nutrient stress. Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism. PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Associated with the plasma membrane and the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Inositol polyphosphate 5-phosphatase OCRL
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
Sequence:
MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEEEECENDGVGGSLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESAPKKEVYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT
Protein: NAD-dependent protein deacylase (EC 2.3.1.286) (Regulatory protein SIR2 homolog) (P9WGG3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Reactivates acetylated acetyl-CoA synthetase (ACS) through an NAD-dependent deacetylation. Is able to ADP-ribosylate itself.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
Interaction partners:
- Possible transcriptional regulatory protein NadR
- Glutamine-dependent NAD
- Probable nicotinate-nucleotide adenylyltransferase
- NAD-capped RNA hydrolase NudC
- Purine nucleoside phosphorylase
- Nicotinamidase/pyrazinamidase
- NAD kinase
- HTH-type transcriptional regulator Rv1152
- Probable soluble pyridine nucleotide transhydrogenase
- Probable nucleoside hydrolase IunH
Sequence:
MRVAVLSGAGISAESGVPTFRDDKNGLWARFDPYELSSTQGWLRNPERVWGWYLWRHYLVANVEPNDGHRAIAAWQDHAEVSVITQNVDDLHERAGSGAVHHLHGSLFEFRCARCGVPYTDALPEMPEPAIEVEPPVCDCGGLIRPDIVWFGEPLPEEPWRSAVEATGSADVMVVVGTSAIVYPAAGLPDLALARGTAVIEVNPEPTPLSGSATISIRESASQALPGLLERLPALLK
Protein: Heat shock transcription factor 4 (A0A096MJV3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQEAPAALPTEPGPSPVPAFLGKLWALVGDPGTDHLIRWSPSGTSFLVSDQSRFAKEVLPQYFKHSNMASFVRQLNMYGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGCEQLLERVRRKVPALRGDDTRWRPEDLGRLLGEVQALRGVQESTEARLQELRQQNEILWREVVTLRQSHSQQHRVIGKLIQCLFGPLQTGPSSTGAKRKLSLMLDEGSACSASAKFNACPVSGALLQDPYFIQSHPHRCPWLWCRPSWKGKGASALRGPGAYNSLNQGAPGRYLTGELWAWIAVTGAQRVCCPPCCFGLPLKLWSPWMRWVLACMDENGP
Protein: Alanine--glyoxylate aminotransferase (AGT) (EC 2.6.1.44) (Serine--pyruvate aminotransferase) (SPT) (EC 2.6.1.51) (P31030)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Peroxisomal aminotransferase that catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification (By similarity). Also catalyzes the transamination between L-serine and pyruvate and contributes to gluconeogenesis from the L-serine metabolism.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P21549}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein
- Serine hydroxymethyltransferase, cytosolic
- Phosphoserine phosphatase
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Aminomethyltransferase, mitochondrial
- alanine transaminase
- (S)-2-hydroxy-acid oxidase
- Glycine cleavage system P protein
Sequence:
MASRQLLVAPPEALRKPLCTPHRLLLGPGPSNLPPRVLAAGGLQMIGHMHEEMYQVMDEIKQGIQYAFQTRNALTLAVSGSGHCALETALFNLLEPGDAFLVGANGIWGQRAAEVGERIGARVHPMIKDPGSHYTLQEVEECLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGAPIYMDQQGIDVLYSGSQKALNAPPGTSLISFSDKAKSKIYARKTKPFSFYMDVQLLANIWGCDGKPRMYHHTTPVIGIFALRESLALLVEQGLEKSWQRHREVAQHLYRRLQELGLQLFVKDPALRLPTVTTVIVPASYRWRDIVSYVMHHFGIEITGGLGPSADKVLRIGLLGCNATRENVDRLATALREALQHCAQSQL
Protein: BCL2-interacting killer (A0A8I6GEH5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASAPVSARTWEFASVPPLGILGSVPFLPRSEDMSEARLMARDIIKTLLHDQVPQPAVVSGAPSMKEPVGVEDVSPVRDLDFMRCLESRNQVALRLACIGDEMDRCLRSPRLVQLPGIAMHRLAATYSQTGVRGIFRSLIGSLTNLRENIWSWRVFTPGAWVSPDQDPGQLFPMVLLVFLLLGGAWHLQLQ