wanglab/gogpt-training-data huggingface dataset:
Protein: Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog (LPS-induced TNF-alpha factor homolog) (Small integral membrane protein of lysosome/late endosome) (Q8QGW7)
Organism: Gallus gallus (Chicken)
Function: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. May also contribute to the regulation of gene expression in the nucleus. Binds DNA (in vitro) and may play a synergistic role in the nucleus in regulating the expression of numerous cytokines.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane {ECO:0000250|UniProtKB:Q99732}. Late endosome membrane {ECO:0000250|UniProtKB:Q99732}. Endosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Cell membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99732}. Note=Associated with membranes of lysosomes, early and late endosomes. Can translocate from the cytoplasm into the nucleus (By similarity). Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q99732, ECO:0000250|UniProtKB:Q9JLJ0}.
Interaction partners:
- Interleukin-6
- Interleukin
- Interleukin-1
- Interleukin-10
- Ig-like domain-containing protein.
- Ig-like domain-containing protein.
- Uncharacterized protein.
- Interleukin-4
- Interleukin-5
- Uncharacterized protein.
Sequence:
MSAPSGFPAPSAPPSYEETVGINVNYPHPYPVPQPGLRPDGKGMNPPQYSGQPMPTSTPVTVQTVYVQQPVVLFYDRPVQMSCPSCNQMIVTRLCYESGALTWLSCGGLFLLGCIAGCCLIPFCVDALKDVEHFCPNCNAHVGSYKRL
Protein: Protein PB1-F2 (P0C5U5)
Organism: Influenza A virus (strain A/Duck/Hong Kong/2986.1/2000 H5N1 genotype C)
Function: Plays an important role in promoting lung pathology in both primary viral infection and secondary bacterial infection. Promotes alteration of mitochondrial morphology, dissipation of mitochondrial membrane potential, and cell death. Alternatively, inhibits the production of interferon in the infected cell at the level of host mitochondrial antiviral signaling MAVS. Its level of expression differs greatly depending on which cell type is infected, in a manner that is independent of the levels of expression of other viral proteins. Monocytic cells are more affected than epithelial cells. Seems to disable virus-infected monocytes or other host innate immune cells. During early stage of infection, predisposes the mitochondria to permeability transition through interaction with host SLC25A6/ANT3 and VDAC1. These proteins participate in the formation of the permeability transition pore complex (PTPC) responsible of the release of mitochondrial products that triggers apoptosis.
Subcellular location: Host mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_04064}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04064}. Host cytoplasm, host cytosol {ECO:0000255|HAMAP-Rule:MF_04064}. Note=Inner mitochondrial membrane in most cells types. Otherwise is detected in the nucleus and cytosol. {ECO:0000255|HAMAP-Rule:MF_04064}.
Interaction partners:
Sequence:
MEQEQDTPWTQSTEHINIQNRGNGQRTQRLEHPNSIRLMDHCLRIMSRVGMHRQIVYWKQWLSLKSPTQGSLKTRVLKRWKLFSKQEWIN
Protein: Vacuolar arginine/histidine antiporter stm1 (Seven transmembrane protein 1) (Q10482)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:33189720}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein C2E12.03c
- Ribosome-associated protein oga1
Sequence:
MSVIAPSFDMANILTELSSFLGALSLGCWVVLLIPQLLENYKNQSGESISDLFLIIWLIGDFFNVLGSIYGNVSSTVLVLSFYYIVSDSTLLMQIYYYRWKAARRIASREHEPLLQSRSLEEGLHAPIGKQQIWWDRLSTRQQFGVMGCVVIVSTIVGNLIISSASSDKSDDDLNAWPFTAGCISSVLYFCARIPQIIKNHKAKSTEGLSIIFFVLASVGNTSYAFSILVFPASDYLNYTYANLPWILGAFSTIFLDIYIFYQFIKYRNHY
Protein: E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)] (P62877)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11027288}. Nucleus {ECO:0000269|PubMed:11027288}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- S-phase kinase-associated protein 1
- Cullin-7
- Cullin-associated NEDD8-dissociated protein 1
- Cullin-4A
- Glomulin
- Ubiquitin-conjugating enzyme E2 D1
- F-box/WD repeat-containing protein 8
- S-phase kinase-associated protein 2
- Ubiquitin-like protein NEDD8
Sequence:
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Protein: Suppressor of forked domain-containing protein (Q381G3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- C3H1-type domain-containing protein
- Cleavage stimulation factor 50 kDa subunit
- Cleavage and polyadenylation specificity factor-like protein, putative
- Uncharacterized protein
- Cleavage and polyadenylation specificity factor subunit, putative
- RNA-binding protein, putative
- RNA-binding protein, putative
- polynucleotide adenylyltransferase
- Poly
Sequence:
MEDEQSSLRDMMDRLRFATGKVAAAPVQEVTSTRIDEKCLLVIRQVLCRHPALVAIHKTRDELKRQLMDQLQHTLQVENTVADDVGRMLVWMNETSETLEMERLSAVYSDVEQAFGEARQRMLDDLGIEALPEFSQYSVGDLSPWNVLFPLVTGPLLTLDESKYKRAEVQLPNPTPSMITDLIEVNKNVYSVSSWISLLNSLDEYPINAVRHVWHAATFFFPTSGPLVTYYLRKEINEVAKGRYLWDERHEDDAKETYRSYCRVLNCFFRHLPLCFSVELYRLFVDFLEVYIKPDDSGMENVFTTALQRDVGHCPASTDIWKKFLRWKGDKILDMYQRREWVRKLYIRMLRTPLQELQEVKEDYDYFVKTEYRGRPPPEGRVEERFVRARAAVAELNKLMGSVGGFSSQSSSTRNLLPKALYLPRPVRLHVDGAFDVRDEKEEHMHRSEVEAWLVWSTIIERESSTSAYAGIELFGYERVRFFLLMRTSIFPHEPLCWCNYADFCLEKQPLLSERERRVMVRDALERVSYLLPGNFYMRVAYCDYMLNNLGDPECAHRKMKELLMQQRNMVVDYVKGESLAGTDAVVSALEKVTLLSVNWMRWGSINREVTNTQFIRLVARFTMHRVDFLSLIMGVVRRAVRESKDFTPRRCQRAFNTFCHHWIRLELIRNGALVQALVILERWKDHLKMFVSSAKDKGWDLADCGVDEYFTSSCTDICHSDASVVSQVLGILEDLRLALAAVYSSPASGDFVSVSSQAMDTLLTQIESIRNTFFVVDEEANSLASYFKLPLDLVSTRIHGATVPLQTYDNCLFTSEWAGLEESSAFHGPTTPGGGTEKKFVNFPLQGVVEAMPDDTSWMPCRMNDRTSRLSGEKADGKQGAHTNLDMRSKKVSRPPNRRGLVTRSVLLKDLTLALRGVGGSSTVTGVPNVKKIEDMVKENLPTTYETDPLFKDKAVDTEWLLRLFENIPALC
Protein: Aspartokinase (EC 2.7.2.4) (Aspartate kinase) (ASK) (P9WPX3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.
Interaction partners:
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Diaminopimelate epimerase
- Diaminopimelate decarboxylase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Putative asparagine synthetase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Homoserine kinase
- Argininosuccinate synthase
Sequence:
MALVVQKYGGSSVADAERIRRVAERIVATKKQGNDVVVVVSAMGDTTDDLLDLAQQVCPAPPPRELDMLLTAGERISNALVAMAIESLGAHARSFTGSQAGVITTGTHGNAKIIDVTPGRLQTALEEGRVVLVAGFQGVSQDTKDVTTLGRGGSDTTAVAMAAALGADVCEIYTDVDGIFSADPRIVRNARKLDTVTFEEMLEMAACGAKVLMLRCVEYARRHNIPVHVRSSYSDRPGTVVVGSIKDVPMEDPILTGVAHDRSEAKVTIVGLPDIPGYAAKVFRAVADADVNIDMVLQNVSKVEDGKTDITFTCSRDVGPAAVEKLDSLRNEIGFSQLLYDDHIGKVSLIGAGMRSHPGVTATFCEALAAVGVNIELISTSEIRISVLCRDTELDKAVVALHEAFGLGGDEEATVYAGTGR
Protein: Probable hydroxyacylglutathione hydrolase glo2 (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Q9UT36)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Lactoylglutathione lyase
- Glutathione-independent glyoxalase hsp3101
- Glutathione-independent glyoxalase hsp3102
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- Putative glutathione-independent glyoxalase hsp3105
- Probable glutathione-independent glyoxalase hsp3103
- Probable glutathione-independent glyoxalase hsp3104
- 2-hydroxyacid dehydrogenase homolog 2
- Probable hydroxyacylglutathione hydrolase SPCC13B11.03c
- Glutathione-independent glyoxalase DJ-1
Sequence:
MSFHITPIWMWKGTGNNYAYLLTCDKTKITAIVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKNASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVSSPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLAALPDDTVTYPGHEYTKSNAKFSSTIFSTPELTKLVDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKNAA
Protein: Transcription elongation factor A protein 3 (Transcription elongation factor S-II protein 3) (Transcription elongation factor TFIIS.h) (O75764)
Organism: Homo sapiens (Human)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000255|PROSITE-ProRule:PRU00651}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB9
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB2
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MGQEEELLRIAKKLEKMVARKNTEGALDLLKKLHSCQMSIQLLQTTRIGVAVNGVRKHCSDKEVVSLAKVLIKNWKRLLDSPGPPKGEKGEEREKAKKKEKGLECSDWKPEAGLSPPRKKREDPKTRRDSVDSKSSASSSPKRPSVERSNSSKSKAESPKTPSSPLTPTFASSMCLLAPCYLTGDSVRDKCVEMLSAALKADDDYKDYGVNCDKMASEIEDHIYQELKSTDMKYRNRVRSRISNLKDPRNPGLRRNVLSGAISAGLIAKMTAEEMASDELRELRNAMTQEAIREHQMAKTGGTTTDLFQCSKCKKKNCTYNQVQTRSADEPMTTFVLCNECGNRWKFC
Protein: Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (CDP-DAG synthase) (Mitochondrial import protein MMP37) (Mitochondrial matrix protein of 37 kDa) (Mitochondrial translocator assembly and maintenance protein 41) (P53230)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16790493, ECO:0000269|PubMed:16943180, ECO:0000269|PubMed:23623749}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16790493, ECO:0000269|PubMed:16943180, ECO:0000269|PubMed:23623749}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16790493, ECO:0000269|PubMed:16943180, ECO:0000269|PubMed:23623749}.
Interaction partners:
- Phosphatidylglycerophosphatase GEP4, mitochondrial
- Protein UPS1, mitochondrial
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase
- Mitochondrial distribution and morphology protein 35
- Protein UPS2, mitochondrial
- Cardiolipin-specific deacylase 1, mitochondrial
- Tafazzin
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MLRVSENGLRFLLKCHSTNVSMFNRLLSTQIKEGRSSIDDAGIIPDGTINERPNHYIEGITKGSDLDLLEKGIRKTDEMTSNFTNYMYKFHRLPPNYGSNQLITIDKELQKELDGVMSSFKAPCRFVFGYGSGVFEQAGYSKSHSKPQIDIILGVTYPSHFHSINMRQNPQHYSSLKYFGSEFVSKFQQIGAGVYFNPFANINGHDVKYGVVSMETLLKDIATWNTFYLAGRLQKPVKILKNDLRVQYWNQLNLKAAATLAKHYTLEKNNNKFDEFQFYKEITALSYAGDIRYKLGGENPDKVNNIVTKNFERFQEYYKPIYKEVVLNDSFYLPKGFTLKNTQRLLLSRISKSSALQTIKGVFTAGITKSIKYAWAKKLKSMRRS
Protein: Protein EXORDIUM-like 3 (Q9FHM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in a brassinosteroid-dependent regulation of growth and development.
Subcellular location: Secreted. Secreted, extracellular space. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Putative F-box/kelch-repeat protein At1g13200
- Phosphoinositide phosphatase SAC4
- Rop guanine nucleotide exchange factor 5
- Pentatricopeptide repeat
- Probable diphthine methyl ester synthase
- At4g27620
- MIF4G domain-containing protein
- At4g12840
- F-box protein At1g70590
- At3g27230
Sequence:
MHSLPVNLVLTVLTVFLTSPAQVIGYRPYPPKTNGSDQIFDASKKFEGSSNLVRLRYHMGPVLTNNITVHPIWYGTWQKSQKKIIREFINSISAVGSKHPSVSGWWKTVQLYTDQTGSNITGTVRLGEEKNDRFYSHGKSLTRLSIQSVIKSAVTSRSRPLPVNPKSGLYLLLTADDVYVQDFCGQVCGFHYFTFPSIVGFTLPYAWVGNSAKLCPGVCAYPFAVPAFIPGLKPVKSPNGDVGVDGMISVIAHEIAELATNPLVNAWYAGPDPVAPVEIADLCEGIYGTGGGGSYTGQMLNDHSGATYNVNGIRRRYLIQWLWSHVVSYCTGPNALD
Protein: Transcriptional regulator (A0A1D8PU74)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcriptional adapter 2
- Histone acetyltransferase
- SAGA histone acetyltransferase complex subunit
- Histone acetyltransferase
- Transcriptional coactivator HFI1/ADA1
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- SGF29 C-terminal domain-containing protein
- Deubiquitination module subunit
- Transcription initiation factor TFIID subunit 6
Sequence:
MASDNKYKYRIEISQMMFVSGEANDPPIETTSIIEDIVRGQVIEILRQSTKTANSRGSRSIIPEDVIFLIRHDKAKVNRLRTYLSWKDVRKNAKDQEGGGTESLIENTNDVGVGAGGPSQSQSNDSSKMLSRYKKSKIRLPWELQFMFSEQHLETQEENELIDDEEKAASIARLKKLKMADDRTKNMTREEYVHWSECRQASFTFRKGKRFREWAQMSQLCDTRPNDDVIDILGFLTFEIVCSLTEEAMNIKNSEDKLHHIQRLKQIVDNKEKPVKRKYLFDKPDEFTTPIMPYHIEEAWRRLQSTDFKHKAARAFGGGVLKTRTRLI
Protein: Receptor-transporting protein 1 (Q8C8C1)
Organism: Mus musculus (Mouse)
Function: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15550249}; Single-pass type III membrane protein {ECO:0000269|PubMed:15550249}. Note=Effective cell surface expression depends upon interaction with olfactory receptors.
Interaction partners:
- Receptor expression-enhancing protein 1
- Olfactory receptor
- Olfactory receptor
- Chaperone Ric-8B
- Anoctamin-2
- Olfactory receptor 5B21
- Olfactory receptor
- Olfactory receptor
Sequence:
MRIFRPWRLRCPALHLPSFPTFSIKCSLPPLPTDEDMCKSVTTGEWKKVFYEKMEEVKPADSWDFIIDPNLKHNVLAPGWKQYLELHASGRFHCSWCWHTWQSPHVVILFHMYLDKAQRAGSVRMRVFKQLCYECGTARLDESSMLEENIESLVDNLITSLREQCYGERGGHYRIHVASRQDNRRHRGEFCEACQEGIVHWKPSEKLLEEEATTYTFSRAPSPTKPQAETGSGCNFCSIPWCLFWATVLMLIIYLQFSFRTSV
Protein: Translationally-controlled tumor protein (J3KPG2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC
Protein: Endochitinase At2g43590 (EC 3.2.1.14) (O24658)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Lectin-like protein At3g16530
- RING-type E3 ubiquitin transferase
- Transmembrane protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- At1g25420/F2J7_16
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
Sequence:
MAFTKISLVLLLCLLGFFSETVKSQNCGCAPNLCCSQFGYCGTDDAYCGVGCRSGPCRGSGTPTGGSVGSIVTQGFFNNIINQAGNGCAGKRFYTRDSFVNAANTFPNFANSVTRREIATMFAHFTHETGHFCYIEEINGATRNYCQSSNTQYPCAPGKGYFGRGPIQLSWNYNYGACGQSLGLDLLRQPELVGSNPTVAFRTGLWFWMNSVRPVLNQGFGATIRAINGMECNGGNSGAVNARIGYYRDYCGQLGVDPGPNLSC
Protein: Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (Q91VA0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism. Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate. Also catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate (By similarity). Activates lipoate with GTP at a 1000-fold higher rate than with ATP and activates both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11470804}. Mitochondrion {ECO:0000269|PubMed:12709059}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Mannose-binding protein A
- Peroxisomal acyl-coenzyme A oxidase 2
Sequence:
MQWLKSFQICKVLQGFSLSPTQLHRRLFSRVGAPRWNDHDSPEEFNFASDVLDYWAQMEEEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFGQL
Protein: Putative lipid-binding protein AIR1 (Auxin-induced in root cultures protein 1) (Q9S7I2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- DExH-box ATP-dependent RNA helicase DExH9
- F21B7.34
Sequence:
MAPRTPLALFVSLNLLFFTYTSATTGTCPKNSIEIGTCVTVLNLVDLTLGNPPVKPCCSLIQGLADLEAAVCLCTAVKASILGIVNINLPINLSVLLNVCSRNAPKSFQCA
Protein: Neuronal synaptobrevin (n-syb) (Q9W0C1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles. Also involved in a neuron-specific sort-and-degrade mechanism that promotes endolysosomal degradation and is required for neuronal maintenance.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:22270918, ECO:0000305|PubMed:9482790}; Single-pass type IV membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:22270918}; Single-pass type IV membrane protein {ECO:0000255}. Note=Localizes to synaptic vesicles and to a subset of early endosomal compartments, predominantly at synapses. {ECO:0000269|PubMed:22270918}.
Interaction partners:
Sequence:
MADAAPAGDAPPNAGAPAGEGGDGEIVGGPHNPQQIAAQKRLQQTQAQVDEVVDIMRTNVEKVLERDSKLSELDDRADALQQGASQFEQQAGKLKRKFWLQNLKMMIIMGVIGLVVVGIIANKLGLIGGEQPPQYQYPPQYMQPPPPPPQQPAGGQSSLVDAAGAGDGAGAGGSAGAGDHGGV
Protein: Thyroid hormone nuclear receptor beta variant 1 (A0A024R2I8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Protein: ATP-dependent DNA helicase Q-like 4B (EC 5.6.2.4) (DNA 3'-5' helicase RecQ4B) (RecQ-like protein 4B) (AtRecQ4B) (AtRecQl4B) (Q9FT70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3'-5' DNA helicase that may play a role in the repair of DNA (By similarity). Required to promote but not to suppress crossovers.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA topoisomerase 3-alpha
- DEAD-box ATP-dependent RNA helicase FANCM
- Crossover junction endonuclease MUS81
- DNA mismatch repair protein MLH1
- AT5G19950 protein
- DNA mismatch repair protein MSH5
- Exonuclease 1
- Exonuclease 1
- ATPase family AAA domain-containing protein FIGL1
- ATP-dependent DNA helicase Q-like 3
Sequence:
MVVTRGDKFAGSSLACKSMIGANKMSGSHLHEVNNSRSHFPQTNWLKVAKAFECIPSLNKFMGSNFLYSLESQKLGRDREMAARSIENIAPVTVQTLARPQIEKAWCTLINLSINNTYLRPGITPAIDNDSTSRTSSTKGSTFKVTSNADGSFCAHNHPEHSQRSVRGTAKSIDSFSSSSVGDNKIIIDKVPRVNYEVRDSVTVTNGMEMPPIKNSAQLARPVEPREVSLGEIDYDDIMEIIDVDQIAMEHCPSTCTKQPSVSKFVDIFTSRREEEQGLPPEICSNCSHGIKLGLCPEASTHVEQMKDTLLAISNEILDNTYDLGPDHVEQLHQKRLLLKKQIQQLEILIHNKERKKSQCLVSIPSHNTQYETPQTTNLEVVYGQTDSPTHVKEQGRCVTDNWNMPRDYLVSKERYDISSGSEEREQSVSEVIDVTDTESSNDKKWTSSDFPWTKNLEVYNKLVFGNHSFRPNQREIINATMSGCDVFVLMPTGGGKSLTYQLPALLCAGITLVISPLVSLIQDQIMNLLQTNISAASLSAGMEWAEQLEILQELSSEKSKYKLLYVTPEKVAKSESLLRHLEILNSRSLLARFVIDEAHCVSQWGHDFRPDYQGLGVLKQKFPNIPMLALTATATTSVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTNKCLEDIDKFIRENHFDECGIIYCLSRMDCEKVTEALRVFGHKAAFYHGSMDPGKRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYTDYIRVKHMISQGGLGQGQMKMGYNCKASSGRMLETNTENLLRMVSYCENEVDCRRFLQLVHLGEKFDSTNCKNTCDNCSSSKILIDKDVTVIARQLVALVKLTGERFSSAHIVEIYRGSLNQSVKRNRQDTLHLHGAGKHLTKSEASRILHYLVTEDILAEGVKKSELYGSVSSLLKVNRSKAASLLSGGQSITMRFPSTIKVSKQSKSTANPAKVPLKQTTLPMAKAAPQDSNLSGILLTALKNLRTDIVKESPDLVMAYHIFGNATLKEISKRLPRTKEELLDINGLGKAKVSKYGDRLLETIDSTINDHYKTRPGSGKRRRDENVNPNVAEDDDPDWSASQSHKKVVKNKK