wanglab/gogpt-training-data huggingface dataset:
Protein: Maleylacetate reductase 2 (EC 1.3.1.32) (Chloromaleylacetate reductase) (Maleylacetate reductase II) (P94135)
Organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134))
Function: Plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. This enzyme converts maleylacetate and 2-chloromaleylacetate with similar efficiencies. NADH is preferred to NADPH as the cosubstrate.
Interaction partners:
Sequence:
MTGDLNEFVAHFWPVRVVFGAGSTERIPAEVKRLGARRALVLCTPDQRDLAQRVLGDLGDLGAGFHDGAVMHVPEASVTRAAQAARDADADLLVAVGGGSTIGLAKALALHHGMRFVALPTTYAGSEMTPIWGLTADGAKRTGRDPRVLPSTVLYDPHHLTSLPPEVTGPSGMNAIAHAVESMYAPDRNPITMLLAEESIRAMAQGLPVAVDSPGDLDARTRTLYAAWLAGTVLGMVSMGLHHKLCHVLGGRFNLPHAPMHAVLLPHVAAFNEVAAPAELGRVAAALGAPGPGGAGAALHALLRFTCTERSLAAIGMPAQGIYDAAEHALADAYANPRQASREDIARLLRAAFTGEMPA
Protein: Growth/differentiation factor 8 (GDF-8) (Myostatin) (D1LWV1)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU369049}.
Interaction partners:
Sequence:
MQKLAVYVYIYLFMQIAVDPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDETGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKHPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
Protein: RNA helicase (EC 3.6.4.13) (Q6FKD7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- ribonuclease Z
Sequence:
MFPNMLRHRFHYRYIFGALNRRTISSYGLFENNQWLIRKPQLKYLNAKERKNLDTFKLNIDPEKRKCIYTTDKEFKKNLENALAHVYSTQIENSAPDQVEFRKVAWLRLKDMLYNQLLDKNLPAKINGYDPGLMETISPTQPQHIIPHLVKMNKIDQLIWKKITGKTEGVTKYEQFQYLLSSYYDCILNQEIIPSMLNTGTDDSVHSVDFSNPAEWFPEARKIRRHIIMHVGPTNSGKTFRSLQKLKAADRGYYAGPLRLLAREVYEKFKHENVRCNLLTGEEVIKDLDEMGNEANLTSGTIEMIPLNQNFDVVVLDEIQMMADLDRGWAWTNALLGAKAKEVHCCGEASTIPLIKKIVEMTGDKLTINEYERMGKLVVEEEALTKGYHSLKKGDCVVAFSKKAILDLKLEIEKKTELKAAVIYGSLPPETRVKQANLFNSGEFDILIASDAIGMGLNLSIDRVVFTTSKKFDGRDMVDMTSSAIKQIGGRAGRFKQNIHDNGELPVGYITAVKPNVLKAVREAINAPIEYLTSATTWPTDEICTHVMTRFMPGTTCKTLLETIAADIEQSSNKLFQICDLKARMSAIEIIDSMEDITFSDKLRLSNAPLKDFPLVKAAFKKFCDTIARGHTRGLLSYRFPFDILNLKYIYTEKHGLEEYEALYNIIMLFFWLSNRYPNYFIDQESASELKNFCEMIIFEKIDHLKRNPYIRKKFISPYLKRRR
Protein: dolichyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.18) (Q57W34)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Phosphatidic acid phosphatase, putative
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Pretranslocation protein, alpha subunit, putative
Sequence:
MTKGGKVAVTKGSAQSDGAGEGGMSKAKSSTTFVATGGGSLPAWALKAVSTIVSAVILIYSVHRAYDIRLTSVRLYGELIHEFDPWFNYRATQYLSDNGWRAFFQWYDYMSWYPLGRPVGTTIFPGMQLTGVAIHRVLEMLGRGMSINNICVYIPAWFGSIATVLAALIAYESSNSLSVMAFTAYFFSIVPAHLMRSMAGEFDNECVAMAAMLLTFYMWVRSLRSSSSWPIGALAGVAYGYMVSTWGGYIFVLNMVAFHASVCVLLDWARGIYSVSLLRAYSLFFVIGTALAICVPPVEWTPFRSLEQLTALFVFVFMWALHYSEYLRERARAPIHSSKALQIRARIFMGTLSLLLIVASLLAPFGFFKPTAYRVRALFVKHTRTGNPLVDSVAEHRPTTAGAYLRYFHVCYPLWGCGGLSMLVFMKKDRWRAIVFLASLSTVTMYFSARMSRLLLLAGPAATACAGMFIGGLFDLALSQFGDLHSPKDASGDSDPAGGSKRAKGKVVNEPSKRAIFSHRWFQRLVQSLPVPLRRGIAVVVLVCLFANPMRHSFEKSCEKMAHALSSPRIIAVTDLPNGERVLADDYYVSYLWLRNNTPEDARILSWWDYGYQITGIGNRTTLADGNTWSHKHIATIGKMLTSPVKESHALIRHLADYVLIWAGEDRGDLLKSPHMARIGNSVYRDMCSEDDPRCRQFGFEGGDLNKPTPMMQRSLLYNLHRFGTDGGKTQLDKNMFQLAYVSKYGLVKIYKVVNVSEESKAWVADPKNRVCDPPGSWICAGQYPPAKEIQDMLAKRFHYE
Protein: Disks large 1 tumor suppressor protein (Dlg) (P31007)
Organism: Drosophila melanogaster (Fruit fly)
Function: During embryonic development, some isoforms are essential for proper neuronal differentiation and organization. Required for cell polarity; maintenance of apicobasal polarity. Plays a critical role at septate junctions in cellular growth control during larval development. The presence of a guanylate kinase domain suggests involvement in cellular adhesion as well as signal transduction to control cellular proliferation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Cell membrane {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}; Peripheral membrane protein {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}; Cytoplasmic side {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Basolateral cell membrane {ECO:0000269|PubMed:24768049}; Peripheral membrane protein {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}; Cytoplasmic side {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Cell junction, septate junction {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Note=Cytoskeleton- and membrane-associated. Located at the cytoplasmic face of the membrane in the cellular blastoderm and becomes associated with septate junctions which begin to form between epithelial cells at the time of dorsal closure. In adult flies, located at the apical-lateral membrane boundary of epithelial cells. {ECO:0000269|PubMed:10884224}.
Interaction partners:
- LD33695p
- Glutamate [NMDA] receptor subunit 1
- Protein lap4
- NMDA receptor 2, isoform C
- Peripheral plasma membrane protein CASK
- Kekkon 5, isoform A
- Potassium voltage-gated channel protein Shaker
- LD44824p
- Lethal
- Kinesin heavy chain 73, isoform E
Sequence:
MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL
Protein: Protein aurora borealis (Q9VVR2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the activation of Aurora-A (aur) at the onset of mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16890155}. Nucleus {ECO:0000269|PubMed:16890155}. Note=Shuttles between the cytoplasm and the nucleus. In interphase cells, it is nuclear. Upon entry into mitosis, it is excluded from the nucleus and translocates into the cytoplasm in a Cdk1-dependent manner.
Interaction partners:
- Serine/threonine-protein kinase polo
- Aurora kinase
- Cyclin-dependent kinase 1
- G2/mitotic-specific cyclin-B
- Inner centromere protein, isoform A
- Guanylate kinase-associated protein mars
- Bub1-related kinase
Sequence:
MYNDEVRTPQALKNRYITNVNGLKCRARRNSHSNSSNSSAASATPTNGGKENGKYSPQMSGNVCTPPPKRLHKVRNPFEGAMADRLHLPLIASPSLFRSRTPQLSSTQFEWNIDEVSQLKPADVEPHETQFHDSPDPEQESKAQLAISAFFKESLIVPSPVDCPLRKQRIILNCSEDNTPISNKSRRMRDCEVQTELTLPPILPKALEDALRPYFQPHLAGRLSGRSKSSGGPDIFNSSMRRKLFDLHNVIVLGEQDTAEPSRSMVGSSPQGKQTMFAGRLSDSASGESSFGCLSPIRNLCGLPPGTPDNGTCSGKRKLLMHELELPSPIAPSEHLSRRLVHSKVEISVTEQHDTLSERTALKFTPDRSSSPMGGGLEHSDCSINQRVRRLRVNSTRQVVIETGDQPLFEETEGEEEEAESEDDEEADAMQLSTVSFNCSSSNSDTPRGHKRHRSAQRKNLSQSFSANLEEEADQTQGGAGSIQPAEPPSVAMPQQGARIPLYRADSGFNETSSTTFAFSQDLPLDVSMACCSTPSTRS
Protein: E3 ubiquitin-protein ligase RNF180 (EC 2.3.2.27) (RING finger protein 180) (RING-type E3 ubiquitin transferase RNF180) (Q3U827)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18363970}; Single-pass membrane protein {ECO:0000269|PubMed:18363970}. Nucleus envelope {ECO:0000269|PubMed:18363970}.
Interaction partners:
Sequence:
MKRSEESTSTQSPEEQTGTLHCWRCRKCIASSGCFMTPLETQVVEQDRHESVDAQNTCHLWHMNVDALPEWISCLLQKAQWTVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLCKSRTDHQAAQGGRLMRPALKHLPHPGVPSGCDKETLLTGGGSKTRNHWLLSMARNSNGLGRLTEALCLEVRATYFEMKNEKLLFKASDPKCQPFVPQPDTGRCPSRASHRKSHSLDLNISEKLILLPTLYEIHRKPTAYPRLNETGPIDLSGLALPCSNSSCSFQSPPSFDPNMLLHRLSVAPHETQAQRGRECQCGLEASSVYSDHANANSLPFLMDLPSAGRSVLEASDQEEHLSQLDFLRSASFPLGTINHRLNNRERSKLRTLRRQQRRERWLQKQGKYSGVGLLDHMTVSNEMSTDEETEFPEEKDSYMCAVCLDVYFNPYMCYPCHHIFCEPCLRTLAKDNPASTPCPLCRTIISRVFLQTELNNATKTFFTKEYLKIKQSFQKSSSAKWPLPSCRKGFHLFGGFHRRAAPVTRRQFPHGAHRMDYLHFEDDSRGWWFDMDMVIIYIYSVNWVIGFVVFCFLCYFFFPF
Protein: NADH-quinone oxidoreductase subunit E (EC 7.1.1.-) (NADH dehydrogenase I subunit E) (NDH-1 subunit E) (NUO5) (P0AFD1)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Interaction partners:
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit H
Sequence:
MHENQQPQTEAFELSAAEREAIEHEMHHYEDPRAASIEALKIVQKQRGWVPDGAIHAIADVLGIPASDVEGVATFYSQIFRQPVGRHVIRYCDSVVCHINGYQGIQAALEKKLNIKPGQTTFDGRFTLLPTCCLGNCDKGPNMMIDEDTHAHLTPEAIPELLERYK
Protein: Oligophrenin-1 (O60890)
Organism: Homo sapiens (Human)
Function: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at presynaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation (By similarity).
Subcellular location: Postsynapse {ECO:0000250|UniProtKB:P0CAX5}. Presynapse {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, axon {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99J31}. Cytoplasm {ECO:0000250|UniProtKB:Q99J31}.
Interaction partners:
- Rho guanine nucleotide exchange factor 6
- E3 ubiquitin-protein ligase Praja-1
- Ribosomal protein S6 kinase alpha-6
- Cell division control protein 42 homolog
- Ephrin-B1
- Protein YIPF6
- Transforming protein RhoA
- Homer protein homolog 1
Sequence:
MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGNALISAMRNYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVHNASDLLIKPLENFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLQEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQGPLDLTLKYCVRRKTESIDKRFCFDIETNERPGTITLQALSEANRRLWMEAMDGKEPIYHSPITKQQEMELNEVGFKFVRKCINIIETKGIKTEGLYRTVGSNIQVQKLLNAFFDPKCPGDVDFHNSDWDIKTITSSLKFYLRNLSEPVMTYRLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIRHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEESAAPPVPPPRVTARRHKPITISKRLLRERTVFYTSSLDESEDEIQHQTPNGTITSSIEPPKPPQHPKLPIQRSGETDPGRKSPSRPILDGKLEPCPEVDVGKLVSRLQDGGTKITPKATNGPMPGSGPTKTPSFHIKRPAPRPLAHHKEGDADSFSKVRPPGEKPTIIRPPVRPPDPPCRAATPQKPEPKPDIVAGNAGEITSSVVASRTRFFETASRKTGSSQGRLPGDES
Protein: MYB-like DNA-binding domain protein (Myb-like transcription factor 5) (O49021)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKPCCDKQGTNKGAWSKQEDQKLIDYIRIHGEGCWRSLPKAAGLHRCGKSCRLRWINYLRPDIKRGNFAQDEEDLIIKLHALLGNRWSLIAGRLPGRTDNEVKNYWNSHIKRKLMKMGIDPNNHKLNQYPHHVGPLNPTTTNSMDVACKLRVCSTDNDDGISDAASYLEDATPPTGISNLDLDLTIAFPSSPIKNIIEESQQKTASIVTNDEEEQYTVPTLLLFR
Protein: Growth-blocking peptide, long form (GBP) [Cleaved into: Growth-blocking peptide, short form] (Q27913)
Organism: Mythimna separata (Oriental armyworm) (Pseudaletia separata)
Function: Biogenic peptide that prevents the onset of metamorphosis from larva to pupa. Has repressive activity against juvenile hormone esterase. Induces cell proliferation at low concentrations and inhibits it at high concentrations. Mediates the spreading of plasmatocytes to foreign surfaces. May have a role in the regulation of dopamine concentrations.
Interaction partners:
Sequence:
MKLTISILFCVILTLQYNGADGKLKDLFGKIHDSVHGTADKVKEDLNSLFHPNDKNQQGNNDASSNIHFADSEENTDAAKKPDEVTPATTTTTTAAPAVPNAPSDNPTTLAPSTTTKDGRENFSGGCVAGYMRTPDGRCKPTFYQ
Protein: AT04835p (Heat shock protein 60D, isoform A) (Heat shock protein 60D, isoform B) (Q9VJX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Heat shock 70 kDa protein cognate 5
- 10 kDa heat shock protein, mitochondrial
- T-complex protein 1 subunit theta
- GrpE protein homolog, mitochondrial
- T-complex protein 1 subunit alpha
- Heat shock protein 83
Sequence:
MLSRLGRSGRAGVRTFANDIRFGAEARCLLMQGVNVLANAVATTLGPKGRNVLIEQLLISPRITKDGITVANNVQLGNRRQDMGVQLLRQATNNTNNKVGDGTTTATILARGIACQGMHVLRQSKVNVQLLREGILEGSRAVCDALGEMSQSVDTIGQVEAVAKVALNGDERLAELIGDIILELGDSGVILLKESHSPFDEAKIQEGITIASGYYSPFFAKQSHTLELENCLLLLTLAKIDQVEQILPALELARLKERPLLIIAKNFGSDLLKILVLNNLQGRVQVCAVKAPSFGDEQCEEMEDIAFATGGHLLEDASSLADLSEEDLGEVMEAVVDAKETHLLQPINVNEEQVQCRIQDIRELIDEAFTDVELDRLKTRLGRLQGHLATIFVGGTSELEVSERKDRFNDALHAVRVAISDGVVPGGGTAYLRCIPVLDELPPTDIMELQVGREIVKDALRLPCYTIARNAGVDPNEVLRRVLKGSGNYGYDAAAGEFGDLVVRGIVDPTKVLQSAMTSAAGIASLLATTEVLITKQPTKPKIPKNQVTKDLAKLVGM
Protein: Dynamin-3 (EC 3.6.5.5) (Dynamin, testicular) (T-dynamin) (Q08877)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9725914}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9725914}. Note=Microtubule-associated. Isoform-specific localization. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm. Golgi apparatus {ECO:0000269|PubMed:9725914}.
Interaction partners:
- Hematopoietic lineage cell-specific protein
- Dynamin-1
- Dynamin-2
- Src substrate cortactin
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1B
- Clathrin heavy chain 1
- Activity-regulated cytoskeleton-associated protein
- Caveolin-1
- Endophilin-A1
Sequence:
MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRHEIEAETDRVTGMNKGISSVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKSTIGNQGTNLPPSRQIVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKDYRSLELACDSQEDVDSWKASLLRAGVYPDKSFTENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESVEQAQRRDEMLRMYQALKEALAIIGDINTVTVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTLSAPLPRPASSRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSYGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD
Protein: Myoglobin (Nitrite reductase MB) (EC 1.7.-.-) (Pseudoperoxidase MB) (EC 1.11.1.-) (P02144)
Organism: Homo sapiens (Human)
Function: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Subcellular location: Cytoplasm, sarcoplasm {ECO:0000269|PubMed:30918256}.
Interaction partners:
- Cytochrome c
- Albumin
- Cytochrome b5
- Cytochrome b5 type B
- Insulin
- Thyroglobulin
- Haptoglobin
- Cytochrome b
- Neuroglobin
- Ribonuclease pancreatic
Sequence:
MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKHPGDFGADAQGAMNKALELFRKDMASNYKELGFQG
Protein: Immunoglobulin kappa variable 1-5 (Ig kappa chain V-I region CAR) (Ig kappa chain V-I region EU) (Ig kappa chain V-I region HK102) (Ig kappa chain V-I region Kue) (P01602)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWLPGAKCDIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPSRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYS
Protein: Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) (Q8BML9)
Organism: Mus musculus (Mouse)
Function: Glutamine--tRNA ligase. Plays a critical role in brain development.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P47897}. Cytoplasm {ECO:0000250|UniProtKB:P47897}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Leucine--tRNA ligase, cytoplasmic
- Ubiquitin-like protein FUBI
- Aspartate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
Sequence:
MATPDSLALFTGLGLSENKARETLKNEALSTQLREAATQAHQILGSTIDKATGVLLYDLVSRLRDTRRRSFLVSYIANKKIHTGLQLSAALEYVRSHPQDPIDTKDFEQECGVGVVVTPEQIEEAVESTINKHQLQLLAERYRFNMGLLMGEARAALRWADGKMIKNEVDMQVLHLLGPKMEADLVKKPKVAKARLEETDRKTAKDVVEKGEVAGQTLSLMEQLRGEALKFHKPGENYKTPGYVITPYTMDLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVTWLGYTPYKVTYASDYFDQLYAWAVELIHGGLAYVCHQRVEELKGHNPLPSPWRDRPKEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALKVYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDAAPRAMAVLEPLQVVITNFPAPKPLDIRVPNFPADETKGFHQVPFASTVFIERSDFKEESEPGYKRLASGQPVGLRHTGYVIELQNIVRGSSGCVERLEVTCRRADAGEKPKAFIHWVSQPLVCEIRLYECLFQHKNPEDPVEVPGGFLSDLNPASLQVVEGALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGQIVFNRTVTLKEDPGKI
Protein: Mth938 domain-containing protein (Adipogenesis associated Mth938 domain-containing protein) (Q9H7C9)
Organism: Homo sapiens (Human)
Function: May play a role in preadipocyte differentiation and adipogenesis.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Diffuse distribution with some highly concentrated spots around the nucleus. {ECO:0000250}.
Interaction partners:
Sequence:
MTSPEIASLSWGQMKVKGSNTTYKDCKVWPGGSRTWDWRETGTEHSPGVQPADVKEVVEKGVQTLVIGRGMSEALKVPSSTVEYLKKHGIDVRVLQTEQAVKEYNALVAQGVRVGGVFHSTC
Protein: Protein arginine methyltransferase NDUFAF7 homolog, mitochondrial (EC 2.1.1.320) (NADH dehydrogenase [ubiquinone] complex I, assembly factor 7 homolog) (Protein midA homolog) (P36052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MMKRLHPLRIQVHLKSDYPLFTFEQLLSTNGIRRGQTARISLKDYIEWQNFPNIMKRENFFTQRKPVTTTAKEEPFSFDNILDCEPQFSKCLAKWLLVNYKLNDYPYYDLNIVNIYTDLPQAIQICKNLMSYLKSTLSDNMFQKIKYFMVPLYKCDKIPSKLLDGIPGSVSLVQDYPVSPYFLQKKFHIEDPIQILMLNDVIKYTTHDLVRYSSDDKGWQQCFVDINKNGQKSKSFDSAIDYSCELALEQMFNDRSHVSPGKELYIPTKLIEILMTIKNNIPEHRLFIVDTPQRSSPTIISLLKSLISPRPTGSSQIVQPYSDSIFSDKRSGRICFMTDFLQLQNIYNGINSSSSSCEVEDVADFVEKWISPSERSTLSSQNGNRPQLEDIKNSSLAVLHST
Protein: Malic enzyme (Q9VG31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pyruvate carboxylase
- L-lactate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Uncharacterized protein, isoform A
- Pyruvate dehydrogenase E1 component subunit alpha
- Malate dehydrogenase
- Probable citrate synthase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase
- Malate dehydrogenase
Sequence:
MGNSSSICADRNVITNFDENGTPVYPTANNSQSPSSYSRGKERELGCYTKRNSNSNNNNSHERESQSCCSSRVCKNHTTTTTTTLEYELSNFAKLTTRITTQSAAEVDTSPHTDTETHRDRDSNPGNIALATDLELPKGLPLSLSSRHHWNQLQSSLHALHHQQQQQQQQLRSYSSTSETNLEDKMSKPDSKLDKYAQRDRLGLWGTGDNEVVGSLSGFTRLLDKRYSKGLAFTHEERQQLGIHGMLPYVVREPSEQVEHCRALLARLDQDLDKYMYLISLSERNERLFYNVLSSDIAYMMPLVYTPTVGLACQRYSLIHQNAKGMFISIKDKGHIYDVLKNWPETDVRAIVVTDGERILGLGDLGANGMGIPVGKLSLYTALAGIKPSQCLPITLDVGTNTESILEDPLYIGLRERRATGDLYDEFIDEFMHACVRRFGQNCLIQFEDFANANAFRLLSKYRDSFCTFNDDIQGTASVAVAGLLASLKIKKTQLKDNTLLFLGAGEAALGIANLCLMAMKVEGLTEEEAKARIWMVDSRGVITRDRPKGGLTEHKLHFAQLHEPIDTLAEAVRKVRPNVLIGAAAQGGAFNQEILELMADINETPIIFALSNPTSKAECTAEEAYTYTKGRCIFASGSPFAPVTYNNKKFYPGQGNNSYIFPGVALGVLCAGMLNIPEQVFLVAAERLAELVSKDDLAKGSLYPPLSSIVSCSMAIAERIVEYAYKNGLATVRPEPVNKLAFIKAQMYDLDYPRSVPATYKM