wanglab/gogpt-training-data huggingface dataset:
Protein: Monocarboxylate transporter 11 (MCT 11) (Solute carrier family 16 member 11) (Q8NCK7)
Organism: Homo sapiens (Human)
Function: Proton-linked monocarboxylate transporter. It catalyzes the transport of pyruvate across the plasma membrane. Probably involved in hepatic lipid metabolism: overexpression results in an increase of triacylglycerol(TAG) levels, small increases in intracellular diacylglycerols and decreases in lysophosphatidylcholine, cholesterol ester and sphingomyelin lipids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24390345}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:28666119}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPAPQRKHRRGGFSHRCFPTPQTAMTPQPAGPPDGGWGWVVAAAAFAINGLSYGLLRSLGLAFPDLAEHFDRSAQDTAWISALALAVQQAASPVGSALSTRWGARPVVMVGGVLASLGFVFSAFASDLLHLYLGLGLLAGFGWALVFAPALGTLSRYFSRRRVLAVGLALTGNGASSLLLAPALQLLLDTFGWRGALLLLGAITLHLTPCGALLLPLVLPGDPPAPPRSPLAALGLSLFTRRAFSIFALGTALVGGGYFVPYVHLAPHALDRGLGGYGAALVVAVAAMGDAGARLVCGWLADQGWVPLPRLLAVFGALTGLGLWVVGLVPVVGGEESWGGPLLAAAVAYGLSAGSYAPLVFGVLPGLVGVGGVVQATGLVMMLMSLGGLLGPPLSGFLRDETGDFTASFLLSGSLILSGSFIYIGLPRALPSCGPASPPATPPPETGELLPAPQAVLLSPGGPGSTLDTTC
Protein: Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (Q3U2A8)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Elongation factor 1-gamma
- Lysine--tRNA ligase
- Aspartate--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, mitochondrial
- Ribosome production factor 2 homolog
- Alanine--tRNA ligase, cytoplasmic
Sequence:
MPHLPLASFRPPLWGLRPSWGLSRPQALCTQPEPHGSPVSRRNREAKQKRLREKQAALEAGLAEKSKIPAVPTKAWSHKEVVLYEIPTGPGEKKDVSGPLPPAYSPQYVEAAWYQWWVREGFFKPEYQARLPQATGETFSMCIPPPNVTGSLHIGHALTVAIQDALVRWHRMRGDRVLWIPGSDHAGIATQAMVEKQLWKEQRVRRHELSREDFLRAVWQWKHEKGGEIYEQLCALGASLDWDRECFTMDAGSSAAVTEAFVRLYNSGLLYRNRQLVNWSCTLRSAISDIEVESRPLPGRTVLQLPGCPTPVSFGLLASVAFPVDGEPDTEIVVGTTRPETLPGDVAVAVHPDDPRYTHLHGRQLRHPLTGQLLPLITDTTVQPHVGTGAVKVTPAHSPIDAEIGTRHGLTPLSVIAEDGTMTSLCGDWLQGLHRFVAREKIMCTLREQGLFRGLQEHPMVLPICSRSGDVVEYLLKSQWFVRCQEMGDLAAKAVESGALELWPSFHQKSWQHWFAHIGDWCVSRQLWWGHQIPAYRVIGENAEDDRKECWVVGRSEAEARAVAAKRTGRPEAELTLERDPDVLDTWFSSALFPFSALGWPRETPDLAHFYPLTLLETGSDLLMFWVGRMVMLGTQLTGQLPFSKVLLHSMVRDRQGRKMSKSLGNVLDPRDIISGQELQVLQAKLRDGNLDPGELAVAAAAQKKDFPYGIPECGTDALRFALCSHGILGGDLHLSVSEVLNYRHFCNKLWNALRFVLRALGDNFVPQPAEEVTPSSPMDAWILSRLAFAASECERGFLSRELSLVTHTLYHFWLHNLCDVYLEAVKPVLSSVPRPPGPPQVLFSCADVGLRLLAPLMPFLAEELWQRLPPRPGGPLAPSICVAPYPSTRSLEFWRQPELERCFSRVQEVVQALRALRATYQLTKARPQVLLQCSDPGEQGLVQPFLEPLGILSHCGAVGFLSPGAAAPSGWALTPLGDTMKIYMELQGLVDPQSQLPRLTARRQKLQKQLDDLLNRTMSEGLAERQQRISSLHLELSKLDQAASYLQQLMDEAPSAREL
Protein: Protein AKNAD1 (Q5T1N1)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein eS7
Sequence:
MDEADFSEHTTYKQEDLPYDGDLSQIKIGNDYSFTSKKDGLEVLNQIIFIADDPQEKAMHSETCGNTAVTIPLGKITENAANKKDEKEKQCTAALHIPANEGDASKSSISDILLHHLSKEPFLRGQGIDCETLPEISNADSFEEEAIIKSIISCYNKNSWPKEQTPELTDQLNPKRDGENSNKPGSATTTEENTSDLEGPVAAGDSSHQENVNVLTKTKGPGDKQKSYQGQSPQKQQTEKANSGNTFKYGQGQVHYQLPDFSKIAPKVKIPKNKIINKPLAIAKQASFSSKSRDKPTLVQDSLETTPESNCVEKQHQEQKGKITEPSQQIQMEPIVHIHQELLTGIESEASLSKLSPTSQKGTSSSSSYIFQKISQGKQMCQKLKEQTDQLKTKVQEFSKRIKQDSPYHLQDKKLVLEKLQGHLELLEQNFLATKDKHLTLQQQVHKHESTIVGDFDPERKVEGEIFKLEMLLEDVKEKMDESKYTSAPSLPVSSPVTLDDLASTFSSLSNEIPKEHPGHPSGPRGSGGSEVTGTPQGGPQEAPNEELCELAPQTYLNGHYGDAAAQNKPDQVAMRLSSNSGEDPNGTPRRQDCAEMTAPSPSCAFCRRLLEWKQNVEKKGHGRINCGRFSIVLHEKAPHSDSTPNSDTGHSFCSDSGTEMQSNKCQDCGTKIPTSRRACRKEPTKEFHYRYNTPGQNYSNHSKRGAFVQPHSLDESKNSSPSFLKPKRICSQRVNSKSFKGEHEPTPGKKKLQAFMTYSSDPATPSPHFYSCRISGSKSLCDFDSTEEIKSEILNSALDHALRTATILKETTDQMIKTIAEDLAKAQRWRNRLKY
Protein: Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen homolog) (Pteroylpoly-gamma-glutamate carboxypeptidase) (O35409)
Organism: Mus musculus (Mouse)
Function: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}.
Interaction partners:
- N-acetylaspartylglutamate synthase A
- Aspartoacylase
- N-acetylaspartate synthetase
- Beta-citrylglutamate synthase B
- Prostate stem cell antigen
- Folate receptor alpha
- Mesothelin
- Folate receptor beta
- Sperm-egg fusion protein Juno
- Epidermal growth factor receptor
Sequence:
MWNALQDRDSAEVLGHRQRWLRVGTLVLALTGTFLIGFLFGWFIKPSNEATGNVSHSGMKKEFLHELKAENIKKFLYNFTRTPHLAGTQNNFELAKQIHDQWKEFGLDLVELSHYDVLLSYPNKTHPNYISIINEDGNEIFKTSLSEQPPPGYENISDVVPPYSAFSPQGTPEGDLVYVNYARTEDFFKLEREMKISCSGKIVIARYGKVFRGNMVKNAQLAGAKGMILYSDPADYFVPAVKSYPDGWNLPGGGVQRGNVLNLNGAGDPLTPGYPANEHAYRHELTNAVGLPSIPVHPIGYDDAQKLLEHMGGPAPPDSSWKGGLKVPYNVGPGFAGNFSTQKVKMHIHSYTKVTRIYNVIGTLKGALEPDRYVILGGHRDAWVFGGIDPQSGAAVVHEIVRSFGTLKKKGRRPRRTILFASWDAEEFGLLGSTEWAEEHSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYDSWKEKSPSPEFIGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWKTNKVSSYPLYHSVYETYELVVKFYDPTFKYHLTVAQVRGAMVFELANSIVLPFDCQSYAVALKKYADTIYNISMKHPQEMKAYMISFDSLFSAVNNFTDVASKFNQRLQELDKSNPILLRIMNDQLMYLERAFIDPLGLPGRPFYRHIIYAPSSHNKYAGESFPGIYDALFDISSKVNASKAWNEVKRQISIATFTVQAAAETLREVA
Protein: Drebrin like (cDNA FLJ59450, highly similar to Drebrin-like protein) (B4DDD6)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004145}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQSRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPSTPPCLVQAEEEAVYEEPPEQETFYEQPPLVQQQGAGSEHIDHHIQGQGLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
Protein: Spindle pole body component alp6 (Altered polarity protein 6) (Q9USQ2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11080156}. Note=Localizes to the SPB and also to the equatorial MTOC.
Interaction partners:
- Spindle pole body component alp4
- Mitotic-spindle organizing protein 1
- Tubulin gamma chain
- Spindle pole body component alp16
- Gamma-tubulin complex subunit mod21
- Gamma-tubulin complex component gfh1
- DASH complex subunit dad2
- DASH complex subunit dam1
- DASH complex subunit dad3
- DASH complex subunit spc19
Sequence:
MSEIHVKTALSRLADKYLQNSKNPSVPYTIETIVSFFQEIIHSISPDTFQLDIDDILYKIYSKIPPEENNDALFSKLSNLVSRLKSQTVIHNKSQILYFLYLLSPISQSSRDVSSHLLDESISNPINIPSTEVESSNFGQTRYDQVPENPQITDWDEGLENESSISIAHDSSRLNRSTETSSVQHTLITEADLLSSISYVLQGISTEYVQFKNELALLSKRIPVQYLLQMRALSETGLLYQELKVFSNYDPSVSQSIDGDNVSKAFINDQSLALQSLKSVISKELTNFLALIASLDSQIRADASLEKPMVTIRRCIAWTQVAKLKLRILSSVVNDNMNQENKKRLIQVVSKYNVHGDPLIQELSDKILTEITGPLYEMIENWIYKGELVDPYQEFFVKEKNGSESHDHQGQGDVVWKGKYFLDKELIPSFLSEELVDKIFLIGKSLNFARYGCGDFDWAQEHYQKLVKKLSYRDPHSLETVVDKAYTESINHLVYLMEEVFHLTDHLKAIKKYLLLGQGDFVDLLMESLGNSLDQPANTLFRHNLTASLESAIRSSNASYEPEYVLKRLDARLLELSHGETGWDVFTLEYKVDSPINVIITPYCSRQYLKIFNFLWRLKRIEFALAHSWRRVNLGERNVFRNLDYTKFEWHFVSCHLAEMIHFVCQLQYYILFEVIEISWQELQLAMEKPNATLDTYIEAHEKYVTSITHKGLLGGGKSRNEDSFLHQLHDILKVILNFHDAIELLYNFSCSLSNRIRINVPISTDALAAQYTPIKNELSNFTEEFQVRLQKLLHGLASHKDPEMRFLSVRLNYNEFYVSHRRRHDKDVTSQ
Protein: Alkylated DNA repair protein ALKBH8 homolog (EC 1.14.11.-) (Alpha-ketoglutarate-dependent dioxygenase ALKBH8 homolog) (AtALKBH8) (Q8RWY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine.
Interaction partners:
- tRNA
- DNA oxidative demethylase ALKBH2
- Multifunctional methyltransferase subunit TRM112 homolog B
- Multifunctional methyltransferase subunit TRM112 homolog A
- DNA N
- tRNA
- RNA binding / RNA-directed DNA polymerase
- YTH domain-containing protein ECT3
- YTH domain-containing protein ECT4
- Serine carboxypeptidase-like 12
Sequence:
MVQPRFVRPTQSSPSSISGEPNSSNLYVANCGPAVGLTHNAIAAVFAEFGEVNGVYAADDSGVRVIVSFADPFSAKAALEALSGRPCPDLKGRSLHIRYSVLQLPSETQVNDCVPVSLIDSELNIPGLFLLPDFVTVAEEQQLLAAVDARHWIGLAKRRVQHYGYEFCYGTRNVDTKKRLGELPSFVSPILERIYLFPNFDNGSASLNLDQLTVNEYPSGVGLSPHIDTHSAFEDCIFSLSLAGPCIMEFRRYSVSTWKASTTDAEKSGDSSCIKKALYLPPRSMLLLSGEARYAWNHYIPHHKIDKVKDKVIRRSSRRVSFTLRKVRNHPCSCKYPQYCDSQQQM
Protein: Decidual/trophoblast prolactin-related protein (Prolactin family 8, subfamily a, member 2) (O35258)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLPLSQPHFWALLLLVVSNLLLWEKAASIPECQTGENGCSDPLVITFKNALQRAEVINILADKMHEEFYHNPFSAGQFETLVSRMYRRDEEVLRARNHCHSNVTNPPAHGPEHENLKTKRYLKTMINFMGAWITPVYYLVEVLSDMQNVPESIYSKAQEIELKFREIHDDLTWVLKKVYPKVTFWEKSIIWEYLPGLRSTDTSKKFLAMFNLSHCLRVDIFFIKYHLSALMCRITGQDC
Protein: 5-hydroxytryptamine receptor 1E (5-HT-1E) (5-HT1E) (S31) (Serotonin receptor 1E) (P28566)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14744596, ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964, ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}; Multi-pass membrane protein {ECO:0000269|PubMed:14744596, ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964, ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 3A
- 5-hydroxytryptamine receptor 1B
- 5-hydroxytryptamine receptor 1D
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein subunit beta-4
Sequence:
MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVADFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCREHT
Protein: Mast cell-expressed membrane protein 1 (Q8IX19)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000269|PubMed:15953541}; Single-pass type II membrane protein {ECO:0000269|PubMed:15953541}.
Interaction partners:
Sequence:
MEVEEIYKHQEVKMQAPAFRDKKQGVSAKNQGAHDPDYENITLAFKNQDHAKGGHSRPTSQVPAQCRPPSDSTQVPCWLYRAILSLYILLALAFVLCIILSAFIMVKNAEMSKELLGFKRELWNVSNSVQACEERQKRGWDSVQQSITMVRSKIDRLETTLAGIKNIDTKVQKILEVLQKMPQSSPQ
Protein: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (BPG-dependent PGAM) (PGAM) (Phosphoglyceromutase) (dPGM) (EC 5.4.2.11) (Q9CIM0)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Interaction partners:
Sequence:
MPKLVFARHGESEWNLANLFTGWADVDLSENGTKQAIEAGKLIKEAGIEFDIAYTSVLKRAIKTTNLALEYSDQLWVPVVKSWRLNERHYGGLTGLNKADAAAKHGDEQVHIWRRSYDVLPPAMDHDDKYTAHGDRRYAGLEDSLIPDAENLKVTLERALPFWEDQIAPALKEGKNVFVGAHGNSIRALVKQIKKLSDDEIMDVEIPNFPPLVFEFDDNLNVQNEYYLAPKKA
Protein: Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (Q9JJL8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:15081407}.
Interaction partners:
- L-seryl-tRNA
- Probable arginine--tRNA ligase, mitochondrial
- Probable cysteine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
- Probable leucine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, mitochondrial
- Cysteine--tRNA ligase, cytoplasmic
Sequence:
MAASMARLWWPFLARQGLRSRGRCVCSQNPRRSFATEKRVRNLLYEHAREGYSELPYLDMESVCACPEKAARSLELRKGELRPADLPAIISTWQELRQLREQIRSLEAEKEAVAEAVRALLANQDSDQVQKDPQYQGLRARGREIRKQLTPLYPQETQLEEQLYQQALRLPNQTHPDTPVGDESQARVVRVVGEKPAFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTLSKLVSRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPSRFEDLNLAGTAEVGLAGYFMDHSVAFRDLPVRMVCASTCYRAETDTGKEPWGLYRVHHFTKVEMFGVTGPGLEQSSQLLDEFLSLQVEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRYGEVTSASNCTDFQSRRLYIMFETETGELQFAHTVNATACAVPRVLIALLESNQQKDGSVLVPAALQPYLGTDRITAPTHVPLQYIGPNQPQKPRLPGQSATR
Protein: Large delta antigen (L-HDAg) (p27) (P29996)
Organism: Hepatitis delta virus genotype I (isolate D380) (HDV)
Function: Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. Needs co-infection with hepatitis B virus to provide surface proteins, otherwise there is no packaging or budding. Packages the HDV ribonucleoprotein in hepatitis B virus empty particles. Interacts with both HDV genomic RNA and cytoplasmic tail of HBsAg. May inhibit viral RNA replication.
Subcellular location: Virion {ECO:0000269|PubMed:1731113}. Host nucleus, host nucleolus {ECO:0000269|PubMed:1731113}. Note=isoprenylated in the cytoplasm, and translocates in the nucleus possibly after phosphorylation. Translocates after to nuclear speckle, then to the ER membrane where interaction with Hepatitis B virus antigene takes place.
Interaction partners:
Sequence:
MSRPEGRKNRGGREEVLEQWVSGRKKLEELERDLRKVKKKIKKLEDEHPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPSRGGFTDKERQDHRRRKALENKRKQLSAGGKNLSKEEEEELRRLTEEDERRERRIAGPQVGGVNPLEGGTRGAPGGGFVPSMQGVPESPFTRTGEGLDIRGSQGFPWDILFPADPPSSPQSCRPQ
Protein: Mitochondrial carrier protein, putative (Q38DI5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDATLHDKSTRQNTAPTCLSKAETKPSIHAAAGLLGASISTAMFYPLDALRTQMHVCKGGDVNQLSSLRQVVRQKGLRRLYAGFAVSVTSYGIGWGAYMAVFKSVQQNLSAYVSSNQIGGGSGSAKSGSVTAGCNVLSGCAAAITTGTVVTPLCVIRTRQQLFDGSNGAKPQNCWQGFKAIVENEGCGALMRGMIPQILIMGNTIIQMAIYEELRHYIVEQKIQPTSFDVALISSVSKAVASALFNPIEVVRTRLQDKRNCTSPEYRSMTVGLRTIWRTEGIRGLYRGVWVNLCRVVPTTSVSFILYEKFLAILSHHNARRAACLPLVAD
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (C8VIX5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Glutamate synthase
- NAD-specific glutamate dehydrogenase
- NADP-specific glutamate dehydrogenase
- Aspartate aminotransferase
- Citrate synthase, mitochondrial
- 2-methylcitrate synthase, mitochondrial
Sequence:
MSSVRFTSALARRSLNSPLLPCGAPPISSALRSFSSASYSAFSSSSSSFPSPSSARALASTARISRPAATRSLYRVQTRTMATEVQKIKVKNPVVELDGDEMTRIIWKEIREKLILPFLDIDLKYYDLGLEYRDQTDDKVTTESAEAIKKYGVGVKCATITPDEARVEEFKLKKMWLSPNGTIRNILGGTVFREPIVIPRIPRLVPGWTKPIIIGRHAFGDQYRATDRVIPGPGKLELVYTPEGGQPEAIKVFDFPGGGVTQTQYNTDESIRGFAHASFKLALTKGLPLYMSTKNTILKKYDGRFKDIFQEIFESDYKKEFDAKGIWYEHRLIDDMVAQMIKSEGGFIMALKNYDGDVQSDIVAQGFGSLGLMTSTLITPDGQAFESEAAHGTVTRHYREHQKGRETSTNPIASIFAWTRGLIQRGKLDETPDVVKFAEELERACIDVVNEEGIMTKDLALSCGRKERDAWVTTREYMAAVERRLRANLKARL
Protein: Apoptosis regulator Bcl-2 homolog (vBcl-2) (Protein M11) (P89884)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Function: Plays a role in the protection against apoptosis mediated by cytotoxic cells during the immune response to acute and persistent viral infection. Contributes therefore to latency establishment. Plays also a role in the inhibition of host starvation-induced autophagy which ultimately contributes to the viral chronic infection.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:15604429, ECO:0000269|PubMed:18248095, ECO:0000269|PubMed:18797192}.
Interaction partners:
Sequence:
MSHKKSGTYWATLITAFLKTVSKVEELDCVDSAVLVDVSKIITLTQEFRRHYDSVYRADYGPALKNWKRDLSKLFTSLFVDVINSGRIVGFFDVGRYVCEEVLCPGSWTEDHELLNDCMTHFFIENNLMNHFPLEDIFLAQRKFQTTGFTFLLHALAKVLPRIYSGNVIYV
Protein: Chascon, isoform B (Chascon, isoform E) (Q7KUW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRYAAETTQMDKDGPTDLERPGDWDSLSDRMRKLRRSQQQQQKEVALLADRKDALTKRPLDFDREEETRKGETMKWLESHFGSESTASNDSRDDEADAEVEPTKKSYFNVTIKSQSHAQSHLATQQHSHPQHISHGHHPQTLPRSAERERERERERERERERERERERDRDRHPLAMTASASQERKAPANSAGGRSKYFQGISNWSERKDPGPPVNHFSSQAFRDDLQETIRRNGLKKKVSGPGSSQGSALAQETVVQPKDSYVSREDILQQKRQSLSSQFLARSMRGSRDALDDLEAIPGPGPGPSMISPRAEEPSHKRVAYGHRGNNGTHINGHALNGVAPTLVNGRGKSYEPPAPPPAAVPPLEFGGGGSQLGQNPRPTVPQRRRAIEKKLGEHSHTHSHSHSHSSHTSHSAHLPVKSQAPMPSQLNQLEPPPDYSPPPRSRSRSSSPQVDYLMTREMPASTMTLSRKQQQRTRFAPTSSYPPATGGTGNLRPPGATSVSTSNLSAMSGGVSTSKSSRMGQVIGNSLRKLVSKIRSASAERKFRMKSAASKSREQSPSPGQDPRGVGPPVTTYQQYNVIDGHIGSHDSEDSNSDNQRRRERERERERERERERERDPLKQESQSRQNFKRAESADPQLQHLEQAISPRQRYYLGEDPYSSTLYGKENHYERRPRQRNMERTDERMERLERLEREDDYYESRAPPPVTAAHTLGRYQKHGQRFSGSTPNLHQQQQDYRSAQTLPRKLHEQRTQRFGNAMEKQPAPGRGSYLSASGQQQQSRGIPHNQNQQNQQNPNPSPSINGNPNPMQAQQGPAKPARTYAKVLNRSKSFNVHGMNGSNDPSPIYIEKLTRNNYQQRQEPSFGYGLGQGPNANYKSNPHLFSGKDNSLKSGLKSPSIVNLISRSQKDLTKIAGNDEDDVGYPEQDKKQLYLRGLHQQAPDLYRVIHGDEDYGSRKYPLQAKYSLDSRSPPSVELNKDTASIVRRSSEVDHQQSHHHNQQHHQHHIQSHQQQNLRRGSGATIIELRHRK
Protein: Phospholamban (PLB) (P26678)
Organism: Homo sapiens (Human)
Function: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. Controls intracellular Ca(2+) levels in elongated spermatids. May play a role in germ cell differentiation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17241641}; Single-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12804600, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:22427649}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:A4IFH6}; Single-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P61014}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HAX1 at the endoplasmic reticulum (PubMed:17241641). Colocalizes with DMPK at the sarcoplasmic reticulum (PubMed:15598648). {ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:17241641}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Sarcolipin
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL
Protein: Kinase suppressor of ras 1 (D3ZHL1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Lymphocyte specific 1, isoform CRA_a
- RAF proto-oncogene serine/threonine-protein kinase
- Dual specificity mitogen-activated protein kinase kinase 1
- Serine/threonine-protein kinase PLK3
- non-specific serine/threonine protein kinase
- Dual specificity mitogen-activated protein kinase kinase 2
- MAP/microtubule affinity-regulating kinase 3
- non-specific serine/threonine protein kinase
- CD209a molecule
- Mitogen-activated protein kinase 3
Sequence:
MDRAALRAAAMGEKKEGGGGGASAAADGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCSVSNDLTQQEIRTLEAKLVRYICKQRQSKLSVTPSDRTAELNSYPRFSDWLYIFNVRPEVVQEIPQELTLDALLEMDEAKAKEMLRRWGASAEECSRLQQALTCLRKVTGLGGEHKEDSGWSSAEARESSSGPSVDMLSSLGRAGASTQGPRSISVSALPASDSPVPGLSEGLSDTCIPLHTSGRLTPRALHSFITPPTTPQLRRHAKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDEVAPMRFELPHGSPQLVRRDIGLPVTHRFSTKSWLSQVCNVCQKSMMFGVKCKHCRLKCHNKCTKEAPACRISFLPLARLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNLDSSSNPSSTTSSTPSSPAPFLTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPDISACPQAAPLSSTADSTRLDDQPKTDVLGVPEAEAEEPEAGKSEAEDDEDEIDDLPSSRRHWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVKRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADANSSKVMPRFERFGLGTLESSNPKM
Protein: Chaperone protein DNAJ, putative (Q385J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFFVTSIVRMTVHAPRGIPFQITTGDAVKSVQKKYHKPFFGVSMEYLQLGPPSAEFLPFYFCEGSIKGTFRGVVSYRDAEGGAKNNAGISGNSGMRQVVTAPQPLQSSFGPHQTQIYAGYKYNLHYVQGVLCSETNPLQLRNMSSVNVEGATINLFEQSTRTLRVFVEQEVRRQATETACAMISSYHPSASNIVVEFIELNIHIDDVIPVFMPCYVVKACYDQQEYTLYVNGASGQVTGPFLINSLYAGRTAAVATALVTLCLAPNKGAGFIMGSLFAVPMYYIAFYAARYFPLLRRDYSRKRRQKLREKHESDDRSGFRPDMSSKRIDEEYSRSSYWDTHAYEQKWSRKQGTVRDPRGYYGALGLNGGESVNEIRSAYRKIVLTEHPDTGGSTERMTKVNEAYRVLRDPKKREEYDRSGCYT
Protein: MaoC family protein (P96927)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MALREFSSVKVGDQLPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGIGGGYVTSWVGDPGAVTEYNVRFTAVVPVPNDGKGAELVFNGRVKSVDPESKSVTIALTATTGGKKIFGRAIASAKLA