wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein Rv2913c (P9WJH9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator Rv2912c
- Uncharacterized protein Rv2915c
Sequence:
MLAWRQLNDLEETVTYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVAAGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESVRHGVTTVLLGNCSLSTVYANSEDAADLFSRVEAVPREFVLGALRDNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDLRTAVLGLDRATDDTVRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIDKLDGDRFRSRALPSTFATWRERRKLISVLRHRGRILQSAPDVDNPVSALLFFLASSRIFNRRKGVRMSMLVSADAKSMPLAVHVFGLGTRVLNKLLGSQVRFQHLPVPFELYSDGIDLPVFEEFGAGTAALHLRDQLQRNELLADRSYRRSFRREFDRIKLGPSLWHRDFHDAVIVECPDKSLIGKSFGAIADERGLHPLDAFLDVLVDNGERNVRWTTIVANHRPNQLNKLAAEPSVHMGFSDAGAHLRNMAFYNFGLRLLKRARDADRAGQPFLSIERAVYRLTGELAEWFGIGAGTLRQGDRADFAVIDPTHLDESVDGYHEEAVPYYGGLRRMVNRNDATVVATGVGGTVVFRGGQFGGQFRDGYGQNVKSGRYLRAGELGAALSRSA
Protein: Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D1) (Stimulator of Fe transport) (SFT) (UBC4/5 homolog) (UbcH5) (Ubiquitin carrier protein D1) (Ubiquitin-conjugating enzyme E2(17)KB 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase D1) (P51668)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18845142}.
Interaction partners:
- E3 ubiquitin-protein ligase CHIP
- E3 ubiquitin-protein ligase RBX1
- E3 ubiquitin-protein ligase RNF4
- Ubiquitin-like modifier-activating enzyme 1
- E3 ubiquitin-protein ligase Mdm2
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Anaphase-promoting complex subunit 11
- Ubiquitin thioesterase OTUB1
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM
Protein: Alpha/beta hydrolase domain-containing protein 17A (Abhydrolase domain-containing protein 17A) (EC 3.1.2.22) (Q96GS6)
Organism: Homo sapiens (Human)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS. Has depalmitoylating activity towards DLG4/PSD95. May have depalmitoylating activity towards MAP6 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:26701913}; Cytoplasmic side {ECO:0000269|PubMed:26701913}. Endosome membrane {ECO:0000269|PubMed:26701913}; Lipid-anchor {ECO:0000269|PubMed:26701913}; Cytoplasmic side {ECO:0000269|PubMed:26701913}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5XIJ5}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q5XIJ5}.
Interaction partners:
- Acyl-protein thioesterase 1
Sequence:
MNGLSLSELCCLFCCPPCPGRIAAKLAFLPPEATYSLVPEPEPGPGGAGAAPLGTLRASSGAPGRWKLHLTERADFQYSQRELDTIEVFPTKSARGNRVSCMYVRCVPGARYTVLFSHGNAVDLGQMSSFYIGLGSRLHCNIFSYDYSGYGASSGRPSERNLYADIDAAWQALRTRYGISPDSIILYGQSIGTVPTVDLASRYECAAVVLHSPLTSGMRVAFPDTKKTYCFDAFPNIEKVSKITSPVLIIHGTEDEVIDFSHGLALYERCPKAVEPLWVEGAGHNDIELYSQYLERLRRFISQELPSQRA
Protein: Shikimate O-hydroxycinnamoyltransferase (EC 2.3.1.133) (Hydroxycinnamoyl transferase) (AtHCT) (Hydroxycinnamoyl-Coenzyme A shikimate/quinate hydroxycinnamoyltransferase) (Q9FI78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyltransferase involved in the biosynthesis of lignin. Accepts caffeoyl-CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on both shikimate and quinate acceptors.
Interaction partners:
- Cytochrome P450 98A3
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Cinnamoyl-CoA reductase 1
- Trans-cinnamate 4-monooxygenase
- Caffeoyl-CoA O-methyltransferase 1
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Cinnamoyl-CoA reductase 2
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Chalcone synthase
- Caffeoylshikimate esterase
Sequence:
MKINIRDSTMVRPATETPITNLWNSNVDLVIPRFHTPSVYFYRPTGASNFFDPQVMKEALSKALVPFYPMAGRLKRDDDGRIEIDCNGAGVLFVVADTPSVIDDFGDFAPTLNLRQLIPEVDHSAGIHSFPLLVLQVTFFKCGGASLGVGMQHHAADGFSGLHFINTWSDMARGLDLTIPPFIDRTLLRARDPPQPAFHHVEYQPAPSMKIPLDPSKSGPENTTVSIFKLTRDQLVALKAKSKEDGNTVSYSSYEMLAGHVWRSVGKARGLPNDQETKLYIATDGRSRLRPQLPPGYFGNVIFTATPLAVAGDLLSKPTWYAAGQIHDFLVRMDDNYLRSALDYLEMQPDLSALVRGAHTYKCPNLGITSWVRLPIYDADFGWGRPIFMGPGGIPYEGLSFVLPSPTNDGSLSVAIALQSEHMKLFEKFLFEI
Protein: Small ribosomal subunit protein uS15 (40S ribosomal protein S13) (Q03334)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62277}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62277}.
Interaction partners:
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL29
Sequence:
MGRMHAPGKGISQSALPYRRTVPSWLKLNADDVKEQIKKLGKKGLTPSKIGIILRDSHGVAQVRFVNGNKILRIMKSVGLKPDIPEDLYHMIKKAVAIRKHLERNRKDKDGKFRLILVESRIHRLARYYKTKSVLPPNWKYESSTASALVA
Protein: Enterotoxin type B (SEB) (P01552)
Organism: Staphylococcus aureus
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome (By similarity).
Subcellular location: Secreted.
Interaction partners:
Sequence:
MYKRLFISHVILIFALILVISTPNVLAESQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNYDNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEHNGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSPYETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLTTKKK
Protein: Protein arginine N-methyltransferase 1-B (xPRMT1b) (EC 2.1.1.319) (Arginine methyltransferase 1b) (Histone-arginine N-methyltransferase PRMT1-B) (Q6VRB0)
Organism: Xenopus laevis (African clawed frog)
Function: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). Methylates ilf3 to regulate its DNA-binding activity. Required for neural induction, playing a key role in the control of epidermal versus neural cell fate choice.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm {ECO:0000250|UniProtKB:Q99873}.
Interaction partners:
Sequence:
MAEAKTCNMEVSCALPEGSVKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGAKKVIGIECSSISDYAIKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIYARDKWLNPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVSNACLIKEVDIYTVKVDDLTFTSPFCLQVKRNDYIHAMVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTISMKPNAKNNRDLDFTVDIDFKGQLCELSCSTDYRMR
Protein: Nucleolar protein 6 (A0A0A0MRW6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364032}.
Interaction partners:
Sequence:
MGPAPAGEQLRGATGEPEVMEPALEGTGKEGKKASSRKRTLAEPPAKGLLQPVKLSRAELYKEPTNEELNRLRETEILFHSSLLRLQVEELLKEVRLSEKKKDRIDAFLREVNQRVVRVPSVPETELTDQAWLPAGVRVPLHQVPYAVKGCFRFLPPAQVTVVGSYLLGTCIRPDINVDVALTMPREILQDKDGLNQRYFRKRALYLAHLAHHLAQDPLFGSVCFSYTNGCHLKPSLLLRPRGKDERLVTVRLHPCPPPDFFRPCRLLPTKNNVRSAWYRGQSPAGDGSPEPPTPRYNTWVLQDTVLESHLQLLSTILSSAQGLKDGVALLKVWLRQRELDKGQGGFTGFLVSMLVVFLVSTRKIHTTMSGYQVLRSVLQFLATTDLTVNGISLCLSSDPSLPALADFHQAFSVVFLDSSGHLNLCADVTASTYHQVQHEARLSMMLLDSRADDGFHLLLMTPKPMIRAFDHVLHLRPLSRLQAACHRLKLWPELQDNGGDYVSAALGPLTTLLEQGLGARLNLLAHSRPPVPEWDISQDPPKHKDSGTLTLGLLLRPEGLTSVLELGPEADQPEAAKFRQFWGSRSELRRFQDGAIREAVVWEAASMSQKRLIPHQVVTHLLALHADIPETCVHYVGGPLDALIQGLKETSSTGEEALVAAVRCYDDLSRLLWGLEGLPLTVSAVQGAHPVLRYTEVFPPTPVRPAFSFYETLRERSSLLPRLDKPCPAYVEPMTVVCHLEGSGQWPQDAEAVQRVRAAFQLRLAELLTQQHGLQCRATATHTDVLKDGFVFRIRVAYQREPQILKEVQSPEGMISLRDTAASLRLERDTRQLPLLTSALHGLQQQHPAFSGVARLAKRWVRAQLLGEGFADESLDLVAAALFLHPEPFTPPSSPQVGFLRFLFLVSTFDWKNNPLFVNLNNELTVEEQVEIRSGFLAARAQLPVMVIVTPQDRKNSVWTQDGPSAQILQQLVVLAAEALPMLEKQLMDPRGPGDIRMGPSENVALL
Protein: Gibberellin-regulated protein 14 (GAST1 protein homolog 14) (Q9LFR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- DELLA protein GAI
Sequence:
MALSLLSVFIFFHVFTNVVFAASNEESNALVSLPTPTLPSPSPATKPPSPALKPPTPSYKPPTLPTTPIKPPTTKPPVKPPTIPVTPVKPPVSTPPIKLPPVQPPTYKPPTPTVKPPSVQPPTYKPPTPTVKPPTTSPVKPPTTPPVQSPPVQPPTYKPPTSPVKPPTTTPPVKPPTTTPPVQPPTYNPPTTPVKPPTAPPVKPPTPPPVRTRIDCVPLCGTRCGQHSRKNVCMRACVTCCYRCKCVPPGTYGNKEKCGSCYANMKTRGGKSKCP
Protein: Tachykinin-related peptide 2 (TKRP-2) (P86558)
Organism: Acrosternum hilare (Green stink bug) (Nezara hilaris)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APAAGFFGMR
Protein: C-C motif chemokine 28 (Mucosae-associated epithelial chemokine) (MEC) (Protein CCK1) (Small-inducible cytokine A28) (Q9NRJ3)
Organism: Homo sapiens (Human)
Function: Chemotactic activity for resting CD4, CD8 T-cells and eosinophils. Binds to CCR3 and CCR10 and induces calcium mobilization in a dose-dependent manner.
Subcellular location: Secreted.
Interaction partners:
- C-C motif chemokine 13
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- C-C motif chemokine 5
- Platelet factor 4
- C-X-C motif chemokine 13
- Platelet basic protein
- C-X-C motif chemokine 9
- C-X-C motif chemokine 2
- C-X-C motif chemokine 10
Sequence:
MQQRGLAIVALAVCAALHASEAILPIASSCCTEVSHHISRRLLERVNMCRIQRADGDCDLAAVILHVKRRRICVSPHNHTVKQWMKVQAAKKNGKGNVCHRKKHHGKRNSNRAHQGKHETYGHKTPY
Protein: Polyamine oxidase (A0A8I6A890)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAARGPRVLVVGGGIAGLGAVQRLCHHRAAPHLRVLEATACAGGRIRSERCFGFLKEHQDTFFEPPLPAKKAEAIRKLGFGTNNKIFLEFEEPFWEPDCQFIQVVWEDTSPLQDSPLSLQDTWFKKLIGFLVLPSFESSHVLCAFIAGLQSEFMETLSDEEVLLSLTQVLRRVTGNPQLPAAKSVLRSRWHSAPYTRGSYSYVAVGSTGDDLDLMAQPLPADGTGTQLQVLFAGEATHRTFYSTTHGALLSGWREADRLIGLWDSQAEQSRPRL
Protein: Syntaxin-17 (Q9Z158)
Organism: Rattus norvegicus (Rat)
Function: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21545355}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000269|PubMed:10930465}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:21545355}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10930465}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:10930465}. Mitochondrion membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into membranes. Localized into endoplasmic reticulum membranes, it also localizes to the completed autophagosome membrane upon cell starvation (By similarity). {ECO:0000250|UniProtKB:P56962}.
Interaction partners:
- Synaptosomal-associated protein 29
- Vesicle-associated membrane protein 8
- Beclin 1-associated autophagy-related key regulator
- Vesicle-associated membrane protein 7
- VPS39 subunit of HOPS complex
- Synaptobrevin homolog YKT6
- Vacuolar protein sorting-associated protein 41 homolog
- Syntaxin-8
- Vacuolar protein sorting-associated protein 16 homolog
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MSEDEEKVKLRRLEPAIQKFTKIVIPTDLERLKKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREMEKLCLKVHKDDLILLKRMIDPMKEAAAAATAEFLQLHLESVEELKKQVKNEEALLQPSLTRSTTIDGVHTGEAEAASQSLTQIYALPEIPRDQNAAESWETLEADLIELSHLVTDMSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYKLAALPVAGAVIGGVVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRRKQKMMEKLTSSCPDLPSQSDKKCS
Protein: Muscleblind-like protein 1 (Triplet-expansion RNA-binding protein) (Q9JKP5)
Organism: Mus musculus (Mouse)
Function: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasm {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9NR56}. Note=Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress. Localized in the cytoplasm of multinucleated myotubes. {ECO:0000250|UniProtKB:Q9NR56}.
Interaction partners:
- CUGBP Elav-like family member 1
- KH domain-containing RNA-binding protein QKI
- Chloride channel protein 1
- CCHC-type zinc finger nucleic acid binding protein
- Myotonin-protein kinase
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoprotein H2
- Serine/arginine-rich splicing factor 1
- Transcriptional activator protein Pur-alpha
- CUGBP Elav-like family member 2
Sequence:
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATSASAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVDTHNICRTSD
Protein: Heat shock protein 70 (B3VHV2)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSGKGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKYDDPTVQSDMKHWPFRVVNEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGKKVQNAVITVPAYFNDSQRQATKDAGTITGLNVMRIINEPTAAAIAYGLDKKGTRAGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNRFVEEFKGKHKRDNAGNKRAVRRLRTACERARRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVTPLSLGIETAGGVMTALIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLPGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKDDIDRMVQEAEKYKAEDEANRDRVGAKNSLESYTYNMKQTVEDEKLKGKISDQDKQKVLDKCQEVISWLDRNQMAEKEEYEHKQKELEKLCNPIVTKLYQGAGGAGAGGSGGPTIEEVD
Protein: DNA-directed RNA polymerase II subunit GRINL1A (DNA-directed RNA polymerase II subunit M) (Glutamate receptor-like protein 1A) (Q6P6I6)
Organism: Mus musculus (Mouse)
Function: Isoform 1 appears to be stable component of the Pol II(G) complex form of RNA polymerase II. Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. Isoform 1 may play a role in Mediator-dependent regulation of transcription activation. Isoform 1 acts in vitro as negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- Myocardial zonula adherens protein
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MFSLPRGFEPPAPEDLGRQSSAELRERLRRQERLLRNEKFICKLPDKGKKISDTVAKLKAAISEREEVRGRSELFHPVSVDCKLRQKATTRADTDVDKAQSSDLMLDTSSLDPDCSSIDIKSSKSTSETQGPTHLTHRGNEETLEAGYTVNSSPAAHIRARAPSSEVKEHLPQHSVSSQEEEISSSIDSLFITKLQKITIADQSEPSEENTSTENFPELQSETPKKPHYMKVLEMRARNPVPPPHKFKTNVLPTQQSDSPSHCQRGQSPASSEEQRRRARQHLDDITAARLLPLHHLPAQLLSIEESLALQREQKQNYEEMQAKLAAQKLAERLNIKMQSYNPEGESSGRYREVRDEADAQSSDEC
Protein: IA2 (Q9BKN7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004358}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004358}.
Interaction partners:
Sequence:
STGGAAGGGSNEPAPSGRITSLSKENEGRPPSSRSSTSSWSEEPALTNMDISTGNMVRSNMEDHLRNKGRLQREWEALCRYEAEPSAREAASQPQCAGLNRPGAPLPYDHSRVVLNHLANAEGLDYVNASTITDHDPRAPAYVAAQGPLPSTLAHFWQMIWEQGAVVIVALCRLQENGEVACARYWPEEGAEVYHIYEVHLVSEHIWCDDYLVRSFYLKNLRTSETRTVTQFHFLSWPHMGVPAQAKALLDFRRKVNKSYRGRRLPIVVHGSAGAGRTGVYILLDLVLERMNKGAREIDIAATLEHLRDQRASVVATRQQFEFVLMAVAXXVHAILKALPANTSGEKRELDKDPVVGGGSSSTTTKEPLKEDKAQEAAEEEAPTSSSKAAAAAKKEKEKDKDKEEKQAKDQAKVAEPRTPAKSAKQAKK
Protein: Possible conserved membrane or secreted protein (O33272)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable conserved integral membrane protein
- Possible thioredoxin protein
- Pyruvate carboxylase
- Carboxylic ester hydrolase LipN
- Aldo-keto reductase Rv2971
Sequence:
MADKSKRPPRFDLKSADGSFGRLVQIGGTTIVVVFAVVLVFYIVTSRDDKKDGVAGPGDAVRVTSSKLVTQPGTSNPKAVVSFYEDFLCPACGIFERGFGPTVSKLVDIGAVAADYTMVAILDSASNQHYSSRAAAAAYCVADESIEAFRRFHAALFSKDIQPAELGKDFPDNARLIELAREAGVVGKVPDCINSGKYIEKVDGLAAAVNVHATPTVRVNGTEYEWSTPAALVAKIKEIVGDVPGIDSAAATATS
Protein: B3 domain-containing transcription factor NGA2 (Protein NGATHA 2) (Q9M268)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates lateral organ growth. Functionally redundant with NGA1, NGA3 and NGA4.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor IND
Sequence:
MNQEDKEKPIEEASSSMEREHMFDKVVTPSDVGKLNRLVIPKQHAERYFPLDNSTTNDSNKGLLLNFEDRSGNSWRFRYSYWNSSQSYVMTKGWSRFVKDKKLDAGDIVSFQRDSCNKDKLYIDWRRRPKIPDHHHQQFAGAMFPRFYTFPHPQMPTNYETHNLYHRFHQRDLGIGYYVRSMERSHPTAVIESVPVMMQRRAQVASMASRGEKRLRLFGVDMECGGGGGSVNSTEEESSSSGGSIPRGRVSMVGAGSLLQLRLVSSDDESLVAMEAASLEDHHFFTKKGKPSLSFDLDR
Protein: ADP-ribosylation factor, putative (Q585W3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GMP phosphodiesterase delta subunit domain-containing protein
- Cilia- and flagella-associated protein 36
Sequence:
MLKGIRSRAKRDNEPRVLIVGLDNAGKTTVLNALGEDEVPVEGKVSHAAPEGPTQGFNIKTLTRGNKRAKLCDLGGQRALRDYWQDYYSNTDCIMYVVDSSDHRRLEESHAAFVDVLKGIEGAPVLVFANKQDLATAKDAQAIAECLHLHDFRDRKWHIQGCSAKTGAGLEEGVAWILSTCAP
Protein: Anthocyanidin synthase (Gibberellin 3-hydroxylase 1) (Q2QCX4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MVTSVLPRVESLASSGIQSIPKEYIRPQEELTSIGNVFEEEKKEEGPQVPTIDLTEIESEDKEVRERCQQELKKAAMEWGVMHLVNHGISEELMDRVRKVGQKFFELPVEEKEKYANDQSSGNVQGYGSKLANNASGQLEWEDYFFHLIFPEDKRDLSIWPKIPSEYTEVTSEYARQLRGLASKILSALSICLGLEEGRLEKEVGGVEELLLQLKINYYPKCPQPELALGVEAHTDISALTFILHNMVPGLQLFYQGKWVTAKCVPNSIIMHIGDTIEILSNGKFKSILHRGLVNKEKVRISWAVFCEPPKDKIILKPLPETVSETEPPLFPPRTFAQHIEHKLFRKTQDNLSN
Protein: Bacteriophage SPP1 complete nucleotide sequence (Orf44) (Q38072)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Interaction partners:
Sequence:
MREKTEVEEAYEAYFEEYDSAYEDTGIDPEILVLPLMMFGKVGNKWHEPGVPVRKRIKTGETTYKTGPKKGQVKPVYEWVADLKKKKVVVGHKEITRGKNKGQMKPIYETILSDYESTGFYPSANAIYMNTFGGSRRLTPAAEGKLLEWKNLAASGPSRTIGSRVRKGRKSS
Protein: Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1) (Q9W4H6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRTLSRVSELPIIVKQLQKNAAQAGVSKTNNYATEATVQVNRPFKLHRLDEGPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAELTGVQGGCARGKGGSMHMYAPNFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDALPGIWVDGMDVLAVRSATEFAINYVNTHGPLVMETNTYRYSGHSMSDPGTSYRTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVSHLWTDVYSNNLEPKLRGTIAYDIDHIQERKGVNH
Protein: Protein ELFN1 (Extracellular leucine-rich repeat and fibronectin type-III domain-containing protein 1) (Protein phosphatase 1 regulatory subunit 28) (Q8C8T7)
Organism: Mus musculus (Mouse)
Function: Postsynaptic protein that regulates circuit dynamics in the central nervous system by modulating the temporal dynamics of interneuron recruitment. Specifically present in excitatory synapses onto oriens-lacunosum molecular (OLM) interneurons and acts as a regulator of presynaptic release probability to direct the formation of highly facilitating pyramidal-OLM synapses. Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:23042292}. Note=Localizes to excitatory synapses onto somatostatin (Sst)-containing oriens-lacunosum moleculare (O-LM) interneurons.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1F
Sequence:
MAGHGWGTAWVLVAAATLLHAGGLAQGDCWLIEGDKGFVWLAICSQNQPPYEAIPQQINNTIVDLRLNENRIRSVQYASLSRFGNLTYLNLTKNEIGYIEDGAFSGQFNLQVLQLGYNRLRNLTEGMLRGLSKLEYLYLQANLIEVVMASAFWECPNIVNIDLSMNRIQQLGSGTFAGLTKLSVCEIYSNPFYCSCELLGFLRWLAAFTNATQTHDRVQCESPPVYAGYFLLGQGRHGHQRSILSKLQSVCTEGSYTAEVLGPPRPVPGRSQPGHSPPPPPPEPSDMPCADDECFSGDGTTPLVILTTLVPQTEARPSMKVKQLTQNSATIMVQLPSPFNRMYTLEQYNNSKSFTVSKLTQPQEEIRLTNLYTLTNYTYCVVSTSSGTHHNHTCLTICLPKPPSPPGPVPSPSTATHYIMTILGCLFGMVLVLGAVYYCLRKRRRQEEKHKKAVAAAAGSLKKTIIELKYGPEIEAPGLAPLTQGPLLGPEAVTRIPYLPAATSDVEQYKLVESSETPKATKGNYIEVRTGEPQERRGCELSRPGEPQSSVAEISTIAKEVDRVNQIINNCIDALKSESTSFQGAKSGAVSAAEPQLVLLSEPLASKHSFLSPVYKDAFGHGGLQRHHSVEAAPGPPRASTSSSGSARSPRTFRAEATGTHKAPATETKYIEKSSPVPETILTVTPAATVLRAEADKSRQYGEHRHSYPGSHPAEPPAPPPPPPTHEGLGGRKASILEPLTRPRPRDLVYSQLSPQYHNLSYSSSPEYTCRASPSIWERLRLSRRRHKDDAEFMAAGHALRKKVQFAKDEDLHDILDYWKGVSAQHKS