wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional uridylyltransferase/uridylyl-removing enzyme (UTase/UR) (Bifunctional [protein-PII] modification enzyme) (Bifunctional nitrogen sensor protein) [Includes: [Protein-PII] uridylyltransferase (PII uridylyltransferase) (UTase) (EC 2.7.7.59); [Protein-PII]-UMP uridylyl-removing enzyme (UR) (EC 3.1.4.-)] (P9WN29)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Modifies, by uridylylation and deuridylylation, the PII regulatory protein (GlnB), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII protein and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII protein, and plays an important role in the regulation of nitrogen assimilation and metabolism (Probable).
Interaction partners:
- Nitrogen regulatory protein P-II
- Ammonium transporter
- Glutamine synthetase
- Glutamine synthetase
- Probable glutamine synthetase GlnA3
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Probable glutamine synthetase GlnA4
- Glutamate synthase large chain
- Probable 3-hydroxyisobutyrate dehydrogenase
- Possible conserved secreted protein
Sequence:
MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD
Protein: Activated leukocyte cell adhesion molecule b (F1QE54)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}.
Interaction partners:
- Elastin microfibril interfacer 3a.
- Retinal homeobox protein Rx3
Sequence:
MQRTAFLTCLLTVSLMNQVCGLETVTGKYGDTVEIPCNSGLVSDVGVTFVKWKSDKDGSILVKHTGQNASSPTDGNYKNRVSIKKDFGLIITQVSLADQKTFTCMVVAADDILEYPVQLVIYKTPLQPQIANLTTAMEIGKLTTLAQCHTEGANPAANITWFKNKTPLIADGTAIKITNDVAVDKATGLSATTSKLEYTAVKDDINSKFTCQVQHIKSANMDSSPLVFTVNYPSETISFHVLPDGPVKEGDNVTLKCTADGNPPPSRYNFYIKGEKKTVEKSNIFILSNVTRQNTGEYKCSLVDNEILTASKNITVEYLDVILSTTGEVFKKLGDSFETTLDIKASGKTETFCKKGGEKMVGPPKFASLKYTDSGVYECVVTMLGLKKTQTFDLNVHGQPLIKSLTKKRGDGTNKILSCEAEGSPKPTVQWITNGTDVKFQESEHVNGKITYYITVSPKANVTVSCTISNDLGSDTRSIDVSSLVEDVTMDKQDQSEDYSDQTALAVGIVVGLMLAALLIGLAYWLYMKKFRQGSWKTGEKEDGSAEESKKLEENQSQKAEV
Protein: Endoglucanase 1 (EC 3.2.1.4) (Cellulase 2) (AtCEL2) (Endo-1,4-beta glucanase 1) (Q9SRX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable xyloglucan endotransglucosylase/hydrolase protein 5
- B3 domain-containing protein At3g17010
- 2-oxoglutarate
Sequence:
MALYLSSSRLITFLSFILLLSNGFSSSSSRPSIHHRHHLDNHNYKDALSKSILFFEGQRSGKLPPNQRMTWRSNSGLSDGSALNVDLVGGYYDAGDNMKFGFPMAFTTTMLSWSLIEFGGLMKSELPNAKDAIRWATDFLLKATSHPDTIYVQVGDPNMDHACWERPEDMDTPRSVFKVDKNNPGSDIAGEIAAALAAASIVFRKCDPSYSNHLLQRAITVFTFADKYRGPYSAGLAPEVCPFYCSYSGYQDELLWGAAWLQKATNNPTYLNYIKANGQILGADEFDNMFSWDNKHVGARILLSKEFLIQKVKSLEEYKEHADSFICSVLPGASSSQYTPGGLLFKMGESNMQYVTSTSFLLLTYAKYLTSARTVAYCGGSVVTPARLRSIAKKQVDYLLGGNPLKMSYMVGYGLKYPRRIHHRGSSLPSVAVHPTRIQCHDGFSLFTSQSPNPNDLVGAVVGGPDQNDQFPDERSDYGRSEPATYINAPLVGALAYLARS
Protein: Tail completion protein p143 (Tail protein p143) (Q6QGE0)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Stabilizes the tail sheath structure and acts as a connector between the end of tail and the portal vertex of the capsid.
Subcellular location: Virion. Note=Component of the tail. Located on the side of the baseplate, at the level of the cone formed by the BHP-pb3 trimer. {ECO:0000269|PubMed:24198424, ECO:0000305|PubMed:36961893}.
Interaction partners:
Sequence:
MSLSDLARQIIKEQLDTASRSENNKNTVVYSVETGLKDPTRDGTVAQVSFKFSKPVSQDLLNIRTASILKAVSSSLDLSGDLGALENLIQATAGKKSSVGKKRSTGRVQVNFGDPSDVEDGYSGAVTGASGRFVSNSNMKIILEIVAKEYLIKDMKKAGAPLKFRTGRFANSLKIKDVMLRDSETSKGSPELNVTYNYMTRPYSVFNPAVSTYRRLSLRPYPGARNPQKLIGEAIAKAARDLIHSRYKIKVNQGT
Protein: LD29915p (Q8MSB6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTYHFRSSLTQFSVPQLEAPSGESAKRSKVRKEGNKSNMNTNSPSKNVTVKSSQLYRYIAPRNRSMLVMKDPRSMRTLRRMPKPGSNEMGTTSDCAASLSQQIKAVSSPTLSEPCLEEQPQKGTESTDVANTGSSAGSGGLGVLQKFKRTLNNFNNKNQLHISPLSPAAVGNNAPKTKTSPTTTTASIAPMITTTTASDPGSEAGDTSSGKYRFGPLIWRSSKERRKTKYNRRDKCNSGDSGIQIELEQDEQYSRATMAVSRQDEPRAFALTNGSCGVALSKMRAIRRTNSAKASSILGPFIVKTKIAKHLNIGESDKAERKAPESLPTRSLSQPNGLESYGMGRPDLEDSDSDSVASNEEAISFYPTTYAEVLYNFTAGGPQELGLERGMLIEILRKEVGPWWFGRIKKEETNLVEDILGPELGWFPKEFVRIIHCPETDNFFIAHRAAADEAAAEEATARAEEGSVPVPVAAFAEDTDVTVTTDQSNVTLIVIESPPTPSAPSVDFVAQPDHSTIIRRSAVRELLDTEVNYVKLLAAICDGYLPAMSKRIDIFSPNSIRLIFSNITAIYKFQRKFLEALRRGIEQNQVAKVFLKMHKGFLCYSTYCNAYPRALIELETYDRVKDARTILENCRESQNLAELPLSAHLLAPVQRICRYPLHLNEIIKSALEKGAKEGNDTDGAKSAGKTTDYEQLDVTELDIPDSQDTVNLALEAMRGITEAVNEGKRHSETIARHQASFQNFKGPPLHLHSARFFLQVDATRQKQNLWNSSYTLFLFDNQLVYCKRDIIKRSHFIYKGRIFLDRCRVVNVRDGKMFGHTIKNSLRIYSESRDKWYDFSFRSANRKHRFLSTLALERQFGGKALYVSEMTGFEYNYEERPGDYSDQSDYDAQDFELATGVTSGESSLPESPAKSTSRLCETLPKNLSPGTEYPALKTLK
Protein: Vacuolar-sorting protein BRO1 (BRO domain-containing protein 1) (AtBRO1) (F4HXZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen (Probable). Associates with FREE1 and ELC to perform function in the ESCRT-I complex. Binds ubiquitin in vitro. Plays a role in the biogenesis of vacuole and multivesicular bodies (MVBs). Required for the endosomal location of AMSH3. Mediates high-affinity phosphate transporter trafficking to maintain phosphate homeostasis. Regulates vacuolar degradation of PHT1-1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016}. Late endosome {ECO:0000269|PubMed:26324913}. Endosome, multivesicular body {ECO:0000269|PubMed:26342016, ECO:0000269|PubMed:26902184}.
Interaction partners:
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Protein ELC-like
- Protein ELC
- Protein SUPPRESSOR OF K
- Vacuolar protein sorting-associated protein 36
- At2g14110 superfamily protein)
- AMSH-like ubiquitin thioesterase 3
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Vacuolar protein sorting-associated protein 28 homolog 2
Sequence:
MASSSLSNLMLAIHEKKTSSVDLYRPLRNYVTFTYSEREAQLIDDDLETLKQLRSDIERVSDPSPAARRDLLISYYKVLCLVETRFPISPDKDHVNAVSFVWYDAFKQKHKATQQNIHLEKAAVLFNLGASYSQIGLGHDRTTVDGRRQASHAFMAAAGAFAHLRDNESIKATIGPSTTVDVSVECVGMLERLMVAQAQECVFENTIAKGSTPGVSAKIARQVGIFYEEALSALIISPLKDHFDKGWISHVQLKAALFYGEACFRYGKELHEKEEIAEEIARLRSGASRLAEAKKSSRGAPAQLIEAMNTLESSINGNLDRAVKENDRVYLMRVPSPSSLSPLPAFSMVKPMNMTDILDASKEKMFSILVPDSSAKALSRYTEMVDDVIRTQAERLQQASELTRVRLKEMDLPDSILAVDGNSALPVDLKEDVEAVQISGGPAGLEAELQQLRDLKRVNQELLVHTEELLQKEATEDSQFRSQFGTRWTRPQSSTLTKNLQDRLNRFAANLKQAGESDVKIERSVRDNSALMSILDRRPIESAVPTLARPIMSLDATEDAIVGTLKQSLRQLENLGAQRAGLEDMLKEMKRKDDILPKLMTITGSYEDMFRKEISKYDHICEDISQNIEVQEQLLMQIQAQNEEFSTIFNLEDYKASKEKCYKQIQAAIMKYREIKENINEGLKFYVTLQDAITNVKQQCSDFVMTRSIQCRDMIEDVQRQMSGLSFQDHRSSGPYPSVHQPTASSPPPPPETQNPSHPHPHAPYYRPPEQMSRPGYSIPPYGPPPPYHTPHGQAPQPYPPQAQQQPHPSWQQGSYYDPQGQQPRPPYPGQSPYQPPHQGGGYYRQ
Protein: Protein Wnt-2b (Protein Wnt-13) (Q93097)
Organism: Homo sapiens (Human)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a redundant role in embryonic lung development.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
Interaction partners:
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-4
- Frizzled-8
- Low-density lipoprotein receptor-related protein 5
- Wnt inhibitory factor 1
- Frizzled-1
- Dickkopf-related protein 2
- Dickkopf-related protein 1
- Frizzled-7
- Dickkopf-related protein 4
Sequence:
MLRPGGAEEAAQLPLRRASAPVPVPSPAAPDGSRASARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRVMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVMATQDGANFTAARQGYRRATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT
Protein: Dicarboxylate carrier 4, isoform A (Dicarboxylate carrier 4, isoform C) (IP09652p) (Q9VVS1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPVFDDHFLGDCHDEPEGLLPRWWFGGFASMCVAFAVAPIDIVKTHMQIQRQKRSILGTVKRIHSLKGYLGFYDGFSAAILRQMTSTNIHFIVYDTGKKMEYVDRDSYLGKIILGCVAGACGSAFGIPTDLINVRMQTDMKEPPYKRRNYKHVFDGLIRIPKEEGWKALYKGGSVAVFKSSLSTCSQIAFYDIIKTEVRKNISVNDGLPLHFLTSLGTSIISSAITHPLDVVRTIMMNSRPGEFRTVFQASVHMMRFGVMGPYRGFVPTIVRKAPATTLLFVLYEQLRLHFGICSLGGEKYN
Protein: V-type proton ATPase subunit (Q57VV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar proton pump subunit B
- ATP synthase, putative
- Uncharacterized protein
- V-type proton ATPase subunit F
- 
- V-type ATPase, C subunit, putative
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- H
- V-type proton ATPase subunit a
Sequence:
MGRGILNFNVYDGSLEAIVHGYKDGFLRPEEYASLVQCDSLGDMKSQLQVTDYGNFLQHDGQAQLSARVIVERAQEHYAKQLRELRSWAAPPLSHFLDFITYEHMIANVLKLIIAKRSGRDGMQLLTRCHPLGWFPELASLTAAADVREMFEVVLIDSPVGRFFNANGGLESDLDELSVEYIQGMLMKNYYEQFYDLCCELGGATAEVMCPLLELEADLTVLRSTVNTMGVPDIHATDRRRLFPSFGSLVDIHDDIAEAESVEQLRERVRRFGLMHELLDDSRYNSTSSSSAKGGNNNRGNNAVSGAASGQTGASAAGASSLERRFVEVTVALYRDALSRQFQYGVFYAWAKLKELEVSNLHWIADCIAQGMMHRVDEYVSIF
Protein: Phospholipase D alpha 3 (AtPLDalpha3) (PLD alpha 3) (EC 3.1.4.4) (P58766)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Active with phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and phosphatidylserine (PS) as substrates. No activity toward phosphatidylinositol (PI) or PIP2. Positively mediates plant responses to hyperosmotic stresses and promotes root growth, flowering, and stress avoidance. Not involved in the abscisic acid regulation of stomatal movement and transpirational water loss.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q38882}. Membrane {ECO:0000250|UniProtKB:Q38882}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q38882}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Non-specific phospholipase C5
- Non-specific phospholipase C4
- Non-specific phospholipase C1
- Phosphatidylserine decarboxylase proenzyme 2
- Non-specific phospholipase C2
- Phosphatidylserine decarboxylase proenzyme 3
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Non-specific phospholipase C6
Sequence:
MTEQLLLHGTLEVKIYRIDKLHQRSRFNLCGKGNKEPTGKKTQSQIKRLTDSCTSLFGGHLYATIDLDRSRVARTMMRRHPKWLQSFHVYTAHSISKIIFTVKEDEPVSASLIGRAYLPVTEVITGQPIDRWLDILDENRRPIQGGSKLHVRVKFTHVTQDVNWNKGIILPSFNGVPNAYFNQREGCKVTLYQDAHVLNEYPDVTLTGGQVIYKHHRCWEEIFDAIWEAKHLIYIAGWSVNTDVTLVRDPKRTRPGGDLKLGELLKKKAEENVTVLMLVWDDRTSHEVFKRDGLMMTHDQETYDYFKNTKVRCVLCPRNPDNGDSIVQGFEVATMFTHHQKTIVVDSEVDGSLTKRRIVSFLGGIDLCDGRYDTVEHPLFGTLNSVHANDFHQPNFDGASIKKGGPREPWHDIHCKLDGPAAWDVLYNFEQRWMKQGSGRRYLISMAQLAEITVPPLPIVQPDNEEGWTVQVFRSIDDGAVEGFPEDPREAASIGLISGKDNVIERSIQDAYVNAIRRAKNFIYIENQYFLGSSFGWNSRDINLNEINALQLIPKEISLKIVSKIEAGERFSVYIVIPLWPEGKPGSASVQAILDWQRRTMEMMYTDIIIALRKKGLDANPRDYLTFFCLGNREKGKVGEYLPPEKPEANSDYARAQESRRFMIYVHSKMMIVDDEYIIIGSANINQRSMDGGRDTEIAMGAYQPSHLLSTNNMRPVGQIFSFRISLWLEHLRVTTNAFQCPESEECIRMVNATADELWGLYSAQEYPRNDDLPGHLLSYPISIGSNGEVTNLAGTEFFPDTNAKVVGEKSNYLPPILTS
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (eIF-3 p48) (Q641X8)
Organism: Rattus norvegicus (Rat)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004}. Nucleus, PML body {ECO:0000255|HAMAP-Rule:MF_03004}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Protein: THAUMATIN-LIKE PROTEIN 1 (F4JQ53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MIITVLHSHVSFYFIILSFLFFHALHLVGSDGATITIVNRCSFTVWPGILSNSGSGDIGTTGFELVPGGSRSFQAPASWSGRFWARTGCNFNSDTGQGTCLTGDCGSNQVECNGAGAKPPATLAEFTIGSGPADPARKQDFYDVSLVDGYNVPMLVEASGGSEGTCLTTGCVTDLNQKCPTELRFGSGSACKSACEAFGSPEYCCSGAYASPTECKPSMYSEIFKSACPRSYSYAFDDATSTFTCTDADYTITFCPSLPSQKSAANGWRDGGGSVQTSPSPLSTWLSDVFTSDSSNVQSSQYLLIFTIFLLLHF
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I) (P63213)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 7
- Pituitary adenylate cyclase-activating polypeptide type I receptor
Sequence:
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFREKKFFCAIL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6GA79)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEPGRGGVETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQVRPEYCNGGDLADYLHTMRTLSEDTVRLFLQQIAGAMQLLHSKGIIHRDLKPQNILLSNPGGRRANPSNIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPAIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASTPIKKSPPVPVPSYPSSGSGSSSSSSSASHLASPPSLGEMPQLQKTLTSPADAAGFLQGSRDSGGSSKDSCDTDDFVMVPAQFPGDLVPEAASAKPPPDSLLCSGRPGPFSSNRYGASVPIPVPTQVHNYQRIEQNLQSPTQQQTARSSAIRRSGSTSPLGFGRASPSPPSHTDGAMLARKLSLGGGRPYTPSPQVGTIPERPSWSRVPSPQGADVRAGRSPRPGSSVPEHSPRTTGLGCRLHSAPNLSDFHVVRPKLPKPPTDPLGATFSPPQTSAPQPCPGLQSCRPLRGSPKLPDFLQRSPLPPILGSPTKAGPSFDFPKAPSSQSLLTLLARQGVVMTPPRNRTLPDLSEAGPFQGQQLGSGLRPAEDTRGPFGRSFSTSRLTDLLLKAAFGTQASDSGSTDSLQEKPMEIAPSAGFGGTLHPGARAGGASSPAPVVFTVGSPPSGTTPPQSTRTRMFSVGSSSSLGSTGSSSARHLVPGACAEAPELSAPGYCCSLADPLAANLEGAVTFEAPDLPEETLMEQEHTETLHSLRFTLAFAQQVLEIAALKGSASEAAGGPEYQLQESVVADQISQLSREWGFAEQLVLYLKVAELLSSGLQTAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDGIHGVTAERLILSHAVQMVQSAALDEMFQHRESCVPRYHKALLLLEGLQHTLTDQADIENIAKCKLCIERRLSALLSGVYA
Protein: Protein fem-1 homolog B (FEM1b) (FEM1-beta) (Fem-1-like death receptor-binding protein alpha) (Fem-1-like in apoptotic pathway protein alpha) (F1A-alpha) (Q9UK73)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1B) complex specifically recognizes proteins ending with -Gly-Leu-Asp-Arg, such as CDK5R1, leading to their ubiquitination and degradation. Also acts as a regulator of the reductive stress response by mediating ubiquitination of reduced FNIP1: in response to reductive stress, the CRL2(FEM1B) complex specifically recognizes a conserved Cys degron in FNIP1 when this degron is reduced, leading to FNIP1 degradation and subsequent activation of mitochondria to recalibrate reactive oxygen species (ROS) (By similarity). Promotes ubiquitination of GLI1, suppressing GLI1 transcriptional activator activity. Promotes ubiquitination and degradation of ANKRD37 (By similarity). Promotes ubiquitination and degradation of SLBP. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet (By similarity). May also act as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19330022, ECO:0000269|PubMed:24076122}. Nucleus {ECO:0000269|PubMed:19330022}. Note=In the nucleus, the protein level increased slightly after camptothecin (CPT) treatment (PubMed:19330022). Associated with chromatin (PubMed:19330022). {ECO:0000269|PubMed:19330022}.
Interaction partners:
- Cullin-2
- E3 ubiquitin-protein ligase RBX1
- Elongin-B
- Kelch domain-containing protein 10
- Amyloid protein-binding protein 2
- Protein zyg-11 homolog B
- Kelch domain-containing protein 3
- Kelch domain-containing protein 2
- Elongin-C
- Protein fem-1 homolog C
Sequence:
MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEFEQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNETVKAPDIECVLRCSVLEIEQSMNRVKNISDADVHNAMDNYECNLYTFLYLVCISTKTQCSEEDQCKINKQIYNLIHLDPRTREGFTLLHLAVNSNTPVDDFHTNDVCSFPNALVTKLLLDCGAEVNAVDNEGNSALHIIVQYNRPISDFLTLHSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVSEILLKTQMKMSLKCLAARAVRANDINYQDQIPRTLEEFVGFH
Protein: HTH-type transcriptional regulator VqsM (Virulence and quorum sensing modulator protein) (Q9I1P2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Transcriptional regulator involved in both the repression (at least 99 genes, such as mexR and algU) and in the activation (at least 203 genes, such as mvfR, rsaL, vqsR and rpoS) of regulatory or putative regulatory proteins which are implicated in quorum sensing, virulence and multidrug resistance.
Interaction partners:
- Uncharacterized protein
- TonB C-terminal domain-containing protein
- Beta-lactamase-related domain-containing protein
- Secreted protein
- Regulatory protein RsaL
- DUF3218 domain-containing protein
- Quorum-sensing control repressor
Sequence:
MVTEHIFDFEWRPLQNYLRDRDIAIPPFAAEQESRSDALYNWIVSKGYSGKEGLNLGTYYHISDYGVIGLALLCAENVGDILKVIRAYVKLFNRDIANVGVKPRENYEVEIHISVNFKPEWNDASRQFHVNVIASATYKLIMDLLGNDFPISALTVPVHGADKTIYEGFFSLPVKHEGNDIIFSFPAHQLNRTLATANPAVFQSALTMAGESFNALLEVEMGGLRQRIELFLDSIPDQYPSLVTTAKYLRMNERTVRRRLADEGCTYRQIVDKARKERAIALLLNSSIPVDRISDILGYSETASFRHAFRRWTGQSTTEFRNSFH
Protein: Temporin-1Tg (TG) (Temporin-G) (P79875)
Organism: Rana temporaria (European common frog)
Function: Amphipathic alpha-helical antimicrobial peptide with activity against Gram-positive bacteria (M.luteus), Gram-negative bacteria (E.coli), and fungi (S.cerevisiae). Stimulates insulin release from pancreatic beta-cells in a dose-dependent manner, without increasing intracellular calcium. Does not protects BRIN-BD11 beta-cells against cytokine-induced apoptosis. In vivo, intraperitoneal injection together with a glucose load into mice improves glucose tolerance with a concomitant increase in insulin secretion.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTINLSLCEEERDADEERRDDLEERDVEVEKRFFPVIGRILNGILGK
Protein: Beta-D-glucan exohydrolase-like protein (Glycosyl hydrolase family protein) (Q9LZJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Bnm1 like protein
- Putative serine carboxypeptidase-like 30
- F8A5.27 protein
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- AT3g16670/MGL6_12
- Uncharacterized protein
- Probable pectate lyase 19
Sequence:
MAAAMFGVRSFFFSAVIVILFAGRYGEATAADRGYIKYKDPKVAVEERVEDLLIRMTLPEKLGQMCQIDRFNFSQVTGGVATVVPEIFTKYMIGSVLSNPYDTGKDIAKRIFQTNAMKKLSLSTRLGIPLLYAVDAVHGHNTFIDATIFPHNVGLGATRDPQLVKKIGAITAQEVRATGVAQAFAPCVAVCRDPRWGRCYESYSEDPAVVNMMTESIIDGLQGNAPYLADPKINVAGCAKHFVGDGGTINGINENNTVADNATLFGIHMPPFEIAVKKGIASIMASYSSLNGVKMHANRAMITDYLKNTLKFQGFVISDWLGIDKITPIEKSNYTYSIEASINAGIDMVMVPWAYPEYLEKLTNLVNGGYIPMSRIDDAVRRILRVKFSIGLFENSLADEKLPTTEFGSEAHREVGREAVRKSMVLLKNGKTDADKIVPLPKKVKKIVVAGRHANDMGWQCGGFSLTWQGFNGTGEDMPTNTKHGLPTGKIKGTTILEAIQKAVDPTTEVVYVEEPNQDTAKLHADAAYTIVVVGETPYAETFGDSPTLGITKPGPDTLSHTCGSGMKCLVILVTGRPLVIEPYIDMLDALAVAWLPGTEGQGVADVLFGDHPFTGTLPRTWMKHVTQLPMNVGDKNYDPLYPFGYGIKT
Protein: Vomeronasal type-1 receptor (Q3SXA2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MFSLENALYIQAGLGVLANMCLLVFYIFIILGHRPKPMDLISCQQTFIHIMLFFTAGDILHTDIFESMNIENDFKCKTTFYICRVMRGLSICTTCLLSVFQAVTISPNTSLLAKFKHKLKKYTINAFFYIWSFNLSFSSNLIFYVGAYTNVSETNQMKVTKYCSLFPMNYIIRGLILTVTTSRDVFLVGVMLITSTYMVIILFRHQRQCKHLHSIRHLRASPEKKATQTILLLVVFFVVMYWVDFIISSTSVLLWMYDPVILTVQKFVMNAYPTITPLVQISSDNRIINLLKNLQSKCH