wanglab/gogpt-training-data huggingface dataset:
Protein: DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme) (P41516)
Organism: Rattus norvegicus (Rat)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (By similarity). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
Interaction partners:
- Nucleolar and spindle associated protein 1
- Cyclin-dependent kinase 1
- DNA topoisomerase 1
- Assembly factor for spindle microtubules
- Baculoviral IAP repeat-containing protein 5
- Centromere protein F
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 20 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- DLG associated protein 5
Sequence:
MELSPLQPVNENMLLNKKKNEDGKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTMMRNNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGDMELKPFSGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNRLPVKGFRSYVDMYLKDKVDETGNALKVVHEQVNPRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVSKLVDVVKKKNKGGVAVKADQVKNHMWIFGNAVIENPTFDSQTKENMTLQAKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQIQLNKKCSAVKHNRIKGIPKLDDANDAGSRNSAECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEIAFYSLPEFEEWKSTNPNHKKWKVKYYKGLGTSTSKEAKEYFANMKRHRIQFKYSGPEDDAAISLAFSKKQVDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTMYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPSKDDHTLRFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRRLLDGEEPLPMLPSYKNYKGTIEELASNQYVINGEVAILNSTTIEITELPIRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVIKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESSKLNNQARFILEKIDGKIVIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPEEEENEENEESESESTSPAAESGPTFNYLLDMPLWYLTKEKKDELCKQRDEKEQELNTLKKKTPSDLWKEDLAAFVEELEVVEAKEKQDEQVGLPGKGVKAKGKKAQISEVLPSPVGKRVIPQVTMEMRAEAEKKIRRKIKSENVEGTPAEDGAEPGLRQRLEKRQKREPGTRAKKQTTLPFKPIKKAQKQNPWSDSESDMSSNESNFDVPPREKEPRIAATKAKFTADLDSDDDFSGLDEKDEDEDFFPLDDTPPKTKMPPKNTKKALKPQKSSTSVDLESDGKDSVPASPGASAADVPAETEPSKPSSKQTVGVKRTITKGQSLTSTAGTKKRAVPKETKSDSALNAHVSKKPAPAKAKNSRKRMPSSSDSSDSEFEKAISKGATSKKLKGEERDFHVDLDDTVAPRAKSGRARKPIKYLEESDDDLF
Protein: Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' (EC 3.1.4.35) (cGMP phosphodiesterase 6C) (P51160)
Organism: Homo sapiens (Human)
Function: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Cyclic nucleotide-gated channel beta-3
- Cyclic nucleotide-gated channel alpha-3
- Guanylate kinase
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- GMP reductase 1
- Adenine phosphoribosyltransferase
- GMP synthase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
Sequence:
MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESALCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPTSKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISGLPTYVAENGFICNMMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEYITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEIKSILKFQEKLNVDVIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIRLFFEINVVEKFKVPVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVDPTKKEIIMAMMMTACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIEEEAKKQEGGAEKAAEDSGGGDDKKSKTCLML
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE) (Q01064)
Organism: Homo sapiens (Human)
Function: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8855339}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Adenosine kinase
- Guanine nucleotide-binding protein G
Sequence:
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHALRTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSVFRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPKALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
Protein: Dystrobrevin binding protein 1 (A6NFV8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00037838}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037838}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037838}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}. Melanosome membrane {ECO:0000256|ARBA:ARBA00037798}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037798}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037798}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MLETLRERLLSVQQDFTSGLKTLSDKSREAKVKSKPRYEDTWAALHRRAKDCASAGELVDSEVVMLSAHWEKKKTSLVELQEQLQQLPALIADLESMTANLTHLEASFEEVENNLLHLEDLCGQCELERCKHMQSQQLENYKKNKRKELETFKAELDAEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDISDQEALDVFLNSGGEENTVLSPALGPESSTCQNEITLQVPNPSELRAKPPSSSSTCTDSATRDISEGGESPVVQSDEEEVQVDTALATSHTDREATPDGGEDSDS
Protein: Growth/differentiation factor 11 (GDF-11) (Bone morphogenetic protein 11) (BMP-11) (Q9Z217)
Organism: Rattus norvegicus (Rat)
Function: Secreted signal that acts globally to regulate anterior/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues. It is required for proper vertebral patterning and orofacial development. Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Activin receptor type-2A
- Activin receptor type-2B
- TGF-beta receptor type-1
- Activin receptor type-1B
- Follistatin
- Follistatin-related protein 3
- Activin receptor type-1C
- Receptor protein serine/threonine kinase
- Activin receptor type-1
- Angiotensin-converting enzyme
Sequence:
MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAGVGGERSSRPAPSAAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
Protein: Melanoma inhibitory activity protein 2 (MIA protein 2) (CTAGE family member 5 ER export factor) (Cutaneous T-cell lymphoma-associated antigen 5) (Meningioma-expressed antigen 6/11) (Q96PC5)
Organism: Homo sapiens (Human)
Function: Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum. Thereby, may play a role in cholesterol and triglyceride homeostasis (By similarity). Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:21807889, ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:28442536}; Single-pass membrane protein {ECO:0000269|PubMed:21807889}. Note=Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:21807889, ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:28442536}.
Interaction partners:
- Guanine nucleotide-exchange factor SEC12
- Transport and Golgi organization protein 1 homolog
- Coiled-coil domain-containing protein 68
- Protein transport protein Sec16A
- Protein transport protein Sec24C
- Protein transport protein Sec24B
- Protein transport protein Sec23A
- Protein SEC13 homolog
- Protein ERGIC-53
Sequence:
MAKFGVHRILLLAISLTKCLESTKLLADLKKCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVFISEEIQMSTKESDFLCLLGVSYTFDNEDSELNGDYGENIYPYEEDKDEKSSIYESDFQIEPGFYATYESTLFEDQVPALEAPEDIGSTSESKDWEEVVVESMEQDRIPEVHVPPSSAVSGVKEWFGLGGEQAEEKAFESVIEPVQESSFRSRKIAVEDENDLEELNNGEPQTEHQQESESEIDSVPKTQSELASESEHIPKPQSTGWFGGGFTSYLGFGDEDTGLELIAEESNPPLQDFPNSISSDKEATVPCTEILTEKKDTITNDSLSLKPSWFDFGFAILGFAYAKEDKIMLDDRKNEEDGGADEHEHPLTSELDPEKEQEIETIKIIETEDQIDKKPVSEKTDESDTIPYLKKFLYNFDNPWNFQNIPKETELPFPKQILDQNNVIENEETGEFSIDNYPTDNTKVMIFKSSYSLSDMVSNIELPTRIHEEVYFEPSSSKDSDENSKPSVDTEGPALVEIDRSVENTLLNSQMVSTDNSLSSQNYISQKEDASEFQILKYLFQIDVYDFMNSAFSPIVILTERVVAALPEGMRPDSNLYGFPWELVICAAVVGFFAVLFFLWRSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSPLGWPSSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDKMDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPLAPIRGPLFPVDARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET
Protein: ATP-dependent protease ATPase subunit HslU1 (Mitochondrial proteasome-like protease HslVU ATPase subunit 1) (Q57VB1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:18421378}. Note=Associated with kinetoplast DNA (kDNA).
Interaction partners:
- ATP-dependent protease subunit HslV
- Chaperone protein DNAJ, putative
- ATP-dependent protease ATPase subunit HslU2
Sequence:
MMRRVTSSLPSALKLGRSLGPNVRFSGGAAAVEASPAIPPNSSSGKTLVRNMKPRELMQELDNYIIGQTEAKKAVAVALRNRWRRHQVDAAIREEISPKNILMIGPTGVGKTEIARRLAKLVDAPFIKVEATKFTEVGFHGRDVESIIEDLYKASLTQTKQNIMRRHEETARQKAENRILKALAGVSDGFREHLRSGALDDIEVIVELQEKKEKPKNSGTNEGVFISLEIPSSIGGQRPQTVKKVMKIKDAIPAVLQEELDKIVDTEDVSAEALRACEEDGIVVIDEIDKIVTASGGYKGHQASAEGVQQDLLPLVEGTTVSTKGNVQIKTDKILFICSGAFHSVKPSDMLAELQGRLPIRVELKPLTKEDFHRIITEPRYNLIKQHVMMMKTEGVDLVFTDDALWEIASIAAHINSTVQNIGARRLITITEKVVEEVSFDGPDRKGETFVIDAAYVRNSVESMMKKVDIKKFIL
Protein: Cyclo(L-leucyl-L-phenylalanyl) synthase (EC 2.3.2.20) (Cyclodipeptide synthase) (CDPS) (Q8GED7)
Organism: Streptomyces noursei (Streptomyces albulus)
Function: Involved in the biosynthesis of albonoursin (cyclo[(alpha,beta-dehydro-Phe)-(alpha,beta-dehydro-Leu)]), an antibacterial peptide. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Phe-L-Leu) (cFL) as major products from L-L-phenylalanyl-tRNA(Phe) and L-leucyl-tRNA(Leu). AlbC can also incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine and L-valine, into cyclodipeptides. Indeed, ten possible cyclodipeptides composed of L-phenylalanine, L-leucine, L-tyrosine and L-methionine are all synthesized to detectable amounts by AlbC.
Interaction partners:
Sequence:
MLAGLVPAPDHGMREEILGDRSRLIRQRGEHALIGISAGNSYFSQKNTVMLLQWAGQRFERTDVVYVDTHIDEMLIADGRSAQEAERSVKRTLKDLRRRLRRSLESVGDHAERFRVRSLSELQETPEYRAVRERTDRAFEEDAEFATACEDMVRAVVMNRPGDGVGISAEHLRAGLNYVLAEAPLFADSPGVFSVPSSVLCYHIDTPITAFLSRRETGFRAAEGQAYVVVRPQELADAA
Protein: Lymphocyte antigen 6E (Ly-6E) (Retinoic acid-induced gene E protein) (RIG-E) (Stem cell antigen 2) (SCA-2) (Thymic shared antigen 1) (TSA-1) (Q16553)
Organism: Homo sapiens (Human)
Function: GPI-anchored cell surface protein that regulates T-lymphocytes proliferation, differentiation, and activation. Regulates the T-cell receptor (TCR) signaling by interacting with component CD3Z/CD247 at the plasma membrane, leading to CD3Z/CD247 phosphorylation modulation (By similarity). Restricts the entry of human coronaviruses, including SARS-CoV, MERS-CoV and SARS-CoV-2, by interfering with spike protein-mediated membrane fusion. Also plays an essential role in placenta formation by acting as the main receptor for syncytin-A (SynA). Therefore, participates in the normal fusion of syncytiotrophoblast layer I (SynT-I) and in the proper morphogenesis of both fetal and maternal vasculatures within the placenta. May also act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q64253}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q64253}.
Interaction partners:
- Prostate stem cell antigen
- Interferon-induced protein 44-like
- Interferon alpha-inducible protein 6
- 2'-5'-oligoadenylate synthase 1
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx1
- Interferon-induced protein 44
- 2'-5'-oligoadenylate synthase 3
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon alpha-inducible protein 27, mitochondrial
Sequence:
MKIFLPVLLAALLGVERASSLMCFSCLNQKSNLYCLKPTICSDQDNYCVTVSASAGIGNLVTFGHSLSKTCSPACPIPEGVNVGVASMGISCCQSFLCNFSAADGGLRASVTLLGAGLLLSLLPALLRFGP
Protein: Probable serine/threonine-protein kinase PBL16 (EC 2.7.11.1) (PBS1-like protein 16) (Q9FM85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in plant defense signaling.
Subcellular location: Cell membrane {ECO:0000305|PubMed:17644812}; Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
Interaction partners:
- Calcium-binding EF-hand family protein
- Probable protein phosphatase 2C 58
- Probable calcium-binding protein CML21
Sequence:
MGNCWCRFEPLNHRVSANAKSESPKEQSPTVEDKHIKEVQKLPSNPKEVEDLRRDSAANPLIAFTYEELKNITSNFRQDRVLGGGGFGSVYKGFIKEDLGDQEVPEPLPVAVKVHDGDNSFQGHREWLAEVIFLGQLSHPNLVKLIGYCCEDNHRVLIYEYMARGSVENNLFSRVLLPLSWAIRMKIAFGAAKGLAFLHEAKKPVIYRDFKTSNILLDMDYNAKLSDFGLAKDGPVGDKSHVSTRIMGTYGYAAPEYIMTGHLTPGSDVYSFGVVLLELLTGRKSLDKSRPTREQNLIDWALPLLKEKKKVLNIVDPKMNCEYPVKAVQKAAMLAYHCLNRNPKARPLMRDIVDSLEPLQATEEEALLVPPVQKAVITIIDEMPKNGLKKVEELKKVEEVKKVIEDAC
Protein: DnaJ protein ERDJ2A (Chaperone protein dnaJ 21) (AtDjC21) (AtJ21) (Endoplasmic reticulum dnaJ domain-containing protein 2A) (AtERdj2A) (Translocation protein SEC63 homolog ERDJ2A) (Q0WT48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:18718935}; Multi-pass membrane protein {ECO:0000305|PubMed:18718935}.
Interaction partners:
- Translocation protein SEC62
- SecY protein transport family protein
- Heat shock 70 kDa protein BIP3
- Protein STABILIZED1
- Heat shock 70 kDa protein BIP2
- Pre-mRNA-processing-splicing factor 8B
- Pre-mRNA-processing-splicing factor 8A
- Heat shock 70 kDa protein BIP1
- Small nuclear ribonucleoprotein Sm D2
- AT2G34250 protein
Sequence:
MAASEENSALFPIFILTIMAIPLVPYTMVKLSGALSKKQRTIHCQCLECDRSGKYKRSLFKKISNFSTWSNLTLVLLWVVMIFLIYYTKNMSREAQVFDPFSILGLEPGVTDSEIKKAYRRLSIQYHPDKNPDPEANKYFVEFISKAYQALTDSVSRENFEKYGHPDGRQGFQMGIALPQFLLDIDGASGGILLLWIVGVCILLPLVIAVIYLSRSSKYTGNYVMHQTLSAYYYLMKPSLAPSKVMEVFTKAAEYMEIPVRRTDDEPLQKLFMSVRSELNLDLKNMKQEQAKFWKQHPAIVKTELLIQAQLTRESGVLSPALQGDFRRVLELAPRLLEELLKMAVIPRTAQGHGWLRPAVGVVELSQCIVQAVPLSARKSSGVSSEGISPFLQLPHFSDAVVKKIARKKVKSFQDLQEMRLEDRSELLTQVAGLSATDVEDIEKVLEMMPSITVDITCETEGEEGIQEGDIVTLQAWVTLKRPNGLVGALPHAPYFPFHKEENYWVLLADSVSNNVWFSQKVSFLDEGGAITAASKAISESMEGSGAGVKETNDAVREAIEKVKGGSRLVMGKLQAPAEGTYNLTCFCLCDTWIGCDKKQALKVKVLKRTRAGTRGLVSDEGAIAEEGMEEEDEIEEEDYDDDYESEYSEDEDEKKDMDEKRGSKKANGSVKQKKESSSEESGSEEE
Protein: Auxin-responsive GH3 family protein (F4II77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDALKHKRAFKMLEKVETFDMNRVIDEFDEMTRNAHQVQKQTLKEILLKNQSAIYLQNCGLNGNATDPEEAFKSMVPLVTDVELEPYIKRMVDGDTSPILTGHPVPAISLSSGTSQGRPKFIPFTDELMENTLQLFRTAFAFRNRDFPIDDNGKALQFIFSSKQYISTGGVPVGTATTNVYRNPNFKAGMKSITSPSCSPDEVIFSPDVHQALYCHLLSGILFRDQVQYVFAVFAHGLVHAFRTFEQVWEEIVTDIKDGVLSNRITVPSVRTAMSKLLTPNPELAETIRTKCMSLSNWYGLIPALFPNAKYVYGIMTGSMEPYVPKLRHYAGDLPLVSHDYGSSEGWIAANVTPRLSPEEATFAVIPNLGYFEFLPVSETGEGEEKPVGLTQVKIGEEYEVVITNYAGLYRYRLGDVVKVIGFYNNTPQLKFICRRNLILSINIDKNTERDLQLSVESAAKRLSEEKIEVIDFSSYIDVSTDPGHYAIFWEISGETNEDVLQDCCNCLDRAFIDAGYVSSRKCKTIGALELRVVAKGTFRKIQEHFLGLGSSAGQFKMPRCVKPSNAKVLQILCENVVSSYFSTAF
Protein: Homeobox A11 (G3V6Z0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Eyes absent homolog
- Paired box 2
Sequence:
MMDFDERGPCSSNMYLPSCTYYVSGPDFSSLPSFLPQTPSSRPMTYSYSSNLPQVQPVREVTFREYAIEPATKWHPRGNLAHCYSAEELVHRDCLQAPSAAGVPGDVLAKSSANVYHHPTPAVSSNFYSTVGRNGVLPQAFDQFFETAYGTPENLASSDYPGDKNAEKGPPTAAATSAAAVAAAATGAPATSSSDGGGGGGCQEAAAEEKERRRRPESSSSPESSSGHTEDKAGGSGGQRTRKKRCPYTKYQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKINRDRLQYYSANPLL
Protein: Survival motor neuron protein (Tudor domain-containing protein) (G5EC16)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Gem-associated protein 2
- ATP-dependent RNA helicase
- Probable small nuclear ribonucleoprotein Sm D1
- Probable small nuclear ribonucleoprotein Sm D2
- Methylosome subunit pICln
- Probable small nuclear ribonucleoprotein G
- Sm domain-containing protein
- Probable small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein E
- Uncharacterized protein.
Sequence:
MAKIWSKSGDMEVDDVWDDTELIKMYDESLQEISKNETSAKITSRKFKGEDGKMYTWKVGGKCMAPYEENGEVTDYPATIDTIGGADNLEVGVTFIYYGGQAVVQMKDLWLNEEAIADAVKAENDLQKTKKTSTVNSVAHSNSKSTSSAPNTSMPFPSFAPPVPPNIIAMAPVNQKEAMNSMLMSWYMSGYHTGYYQALADQKNVQN
Protein: Octanoyltransferase, mitochondrial (EC 2.3.1.181) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) (Q06005)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Putative lipoate-protein ligase A
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Acyl carrier protein, mitochondrial
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- DNA damage checkpoint control protein MEC3
Sequence:
MSRCIRQSVCTNFNVCRRQCFSTYASALKEMTHPIKPSAQTLRHLQFTQRIPFQKGLEIQETLVRANLDIKDIQSKIERKLIQLDEEYKGTATINDNEKRILDKVMAMKPNPIILTFEFEPTYTGGKRIKKTMTPDQIAAYESFIPETQKDNPRPKFVQVERGGQVTFHGPGQIVIYIILDLKTFQSFPAKCLVSCIEQATIRTLKNTKMCDDTDKPLNLDAMTTKDTGVWVENGKKKVASVGIHVRRSITSHGVAINVNTDLSYMNSFEMCGLKNTLTTSIMEQRPDAVVNVQSVAISFVKEMTKLLGIKTLERMQIDDVNILKKNP
Protein: UL16 binding protein 1 (Q8HWA3)
Organism: Mus musculus (Mouse)
Interaction partners:
- NKG2-D type II integral membrane protein
- Natural cytotoxicity triggering receptor 1
- MHC class I-like protein MILL2
- CD226 antigen
- Histocompatibility antigen 60c
- Nectin-2
- Retinoic acid early-inducible protein 1-epsilon
- Poliovirus receptor
- mRNA export factor
- Retinoic acid early-inducible protein 1-delta
Sequence:
MELTASNKVLSCCLSLLCLLSVCLCPRIEETASLCNIYKVNRSESGQHSHEVQGLLNRQPLFVYKDKKCHAIGAHRNSMNATKICEKEVDTLKDGIDIFKGLLLHIVQETNTTGKPLTLQAEVCGQYEVDKHFTGYAIVSLNGKNIFRVDTSTGNWTQLDHEFEKFIEMCKEDKVLAAFLKKTTEGDCRTWLDELMLHWKEHLEPAGSFSTLMIILCVIAIAFLGLIFGVSCKLRHLRTKKIGLQSSPPPLLDDSLTVPTSPQSSVCGTMIQCLCPRKLKSPVFMQIDLQSSAPPLLDDSLTVPETCSVKKEDEFPTASQNSVLLTSDDIDGIP
Protein: Uncharacterized protein (Q38BQ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVMACGAWYVMRFNLFMQLLAVCLITCGTTTADTTAFCHELEPFLVQTLPQASAHLLETAIAKEAAGDNVNVTCALTPGKSVVVLLGSSNVHRFSPLRNPPPVIKLDTADGEFTHEVRGTFMFRYFRSWVNGFRAYSWTDPASVERFFFKRHIFLRFRVSDSTGNPNADIHLSASEVLTMAGLHSIRVTSFAPVAVEIRLRGGKEPKECSDATCSKYVDAFAEHSDKSAGLTRLEVLPQRFTCSPGYGANGWGSGVSGGPMDGEVYAFEEIGPYRGSNLWIPQWLSAWLGRRPMMTVSEKVVLDGMGRRKFLFHAEIPAVKPVCLRLSAVKNDNLIVELEESTVFDTFWLKIMLLFVLLVFIKPWVEEIPALQIFIAGLGSVTLLFVVTILYVLKRLQGMTIGKVGLVAMATLGGTALLAETFLSAVVALYYAFVHYDNEAEMIFYGSAMLLVFGLTCGLLSRHYCATYLTELTRWTLRLLQLAVLACAIMQNREATFASFVAALLFHPPRILRLIQWFSSSSSLVNNENEPQETFPSEALREVTYVTPLCMEGRTGRVSTMDSRERLDLYRISGNEYTHRALEDLACRVNSNPDRYASKVNDAGGVLNWAKGYQYS
Protein: Uncharacterized protein (Q387T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKSEGTPIPTRTPKSGKKKKEFTQLALAKDHRFNWMGHDGTESETLNLDLLRITNEGCLRFSDQARRDYVITMIRARLGQIKLALGLCTEEDLEDDEDEDDDEENSEAQVLWRLAVRRVELQQEAEERGDSGEPLYYGTPTEEEVAEGYRNFVKGTRVLLSHLKQTFVSYIDGREFNTVAQLVEHNNALRPTYEETAAAVQHPKFELPPVEEFDAEPLQAYVEKRNECRMKIDALRCCGGGAYAMRYMREEELDEIGTPRIYVDMEDTEATLDEELQNARQNLAKERWEYNCRAARVYRRLQKFLARRAAAAEQS
Protein: IST1 homolog (Charged multivesicular body protein 8) (H3BUI0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGSGGFTAPVGGPDGTVPMPMPMPMPMPSANTPFSYPLPKGP