wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2) (Q91XU8)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29253589}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cardiolipin synthase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase 5
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Phospholipase D1
- Phospholipase D2
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysocardiolipin acyltransferase 1
Sequence:
MTELRQRAVREDAPPEDKESESEAKLDGETASDSESRAETAPPPTSIDDTPEVLNRALSNLSSRWKNWWVRGILTMAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSLVGWKTMRMYPFQIHSALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLKSHLTDKGILMSALEEE
Protein: SEC14 cytosolic factor (Phosphatidylinositol/phosphatidylcholine transfer protein) (PI/PC TP) (P53989)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol transfer protein SFH5
Sequence:
MVSEAEFLASYPQKCPAGSLPGTPGNTDEAQEGALKQLRSELEAAGFKERLDDSTLLRFLRARKFDVALAKEMFENCEKWRKEYGTNTIMQDFHYDEKPLVAKYYPQYYHKTDKDGRPVYFEELGAVNLTEMEKITTQERMLKNLVWEYESVVNYRLPACSRAAGYLVETSCTVMDLKGISISSAYSVLSYVREASYISQNYYPERMGKFYLINAPFGFSTAFRLFKPFLDPVTVSKIFILGSSYQSELLKQIPAENLPSKFGGKSEVDEAAGGLYLSDIGPWRDAKYIGPEGEAPEMFSMK
Protein: Ribonuclease D (RNase D) (EC 3.1.13.5) (P09155)
Organism: Escherichia coli (strain K12)
Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonuclease R
- Ribonuclease T
- Small ribosomal subunit protein bS1
- Polyribonucleotide nucleotidyltransferase
- RNA 3'-terminal phosphate cyclase
- ATP-dependent DNA helicase RecQ
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS11
- Exoribonuclease 2
- Ribonuclease BN
Sequence:
MNYQMITTDDALASLCEAVRAFPAIALDTEFVRTRTYYPQLGLIQLFDGEHLALIDPLGITDWSPLKAILRDPSITKFLHAGSEDLEVFLNVFGELPQPLIDTQILAAFCGRPMSWGFASMVEEYSGVTLDKSESRTDWLARPLTERQCEYAAADVWYLLPITAKLMVETEASGWLPAALDECRLMQMRRQEVVAPEDAWRDITNAWQLRTRQLACLQLLADWRLRKARERDLAVNFVVREEHLWSVARYMPGSLGELDSLGLSGSEIRFHGKTLLALVEKAQTLPEDALPQPMLNLMDMPGYRKAFKAIKSLITDVSETHKISAELLASRRQINQLLNWHWKLKPQNNLPELISGWRGELMAEALHNLLQEYPQ
Protein: DNA-binding protein inhibitor ID-2 (Inhibitor of DNA binding 2) (Inhibitor of differentiation 2) (P41136)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Restricts the CLOCK and BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15563451, ECO:0000269|PubMed:20861012}. Nucleus {ECO:0000269|PubMed:15563451}.
Interaction partners:
- Transcription factor E2-alpha
- Oligodendrocyte transcription factor 1
- Oligodendrocyte transcription factor 2
- Transcription factor 4
- Homeobox protein Nkx-2.5
- Myoblast determination protein 1
- Interleukin-7 receptor subunit alpha
- Transcription factor 12
- Nuclear factor interleukin-3-regulated protein
- Eomesodermin homolog
Sequence:
MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVTKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKVLCG
Protein: A-type voltage-gated potassium channel KCND3 (Potassium voltage-gated channel subfamily D member 3) (Voltage-gated potassium channel subunit Kv4.3) (Q62897)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12006572, ECO:0000269|PubMed:19213956}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19213956}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:19213956}. Note=Interaction with palmitoylated KCNIP2 and KCNIP3 enhances cell surface expression. {ECO:0000269|PubMed:12006572}.
Interaction partners:
- A-type potassium channel modulatory protein KCNIP1
- A-type potassium channel modulatory protein KCNIP2
- A-type potassium channel modulatory protein DPP6
- Inactive dipeptidyl peptidase 10
- Calsenilin
- Kv channel-interacting protein 2x
- A-type voltage-gated potassium channel KCND1
- Kv channel-interacting protein 4
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-2
Sequence:
MAAGVAAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDDELAFYGILPEIIGDCCYEEYKDRKRENAERLMDDNESENNQESMPSLSFRQTMWRAFENPHTSTLALVFYYVTGFFIAVSVITNVVETVPCGTVPGSKELPCGERYSVAFFCLDTACVMIFTVEYLLRLFAAPSRYRFIRSVMSIIDVVAIMPYYIGLVMTNNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPASFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRVAKTGSSNAYLHSKRNGLLNEALELTGTPEEEHMGKTTSLIESQHHHLLHCLEKTTGLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPSTRSPSLSSHSGLTTTCCSRRSKKTTHLPNSNLPATRLRSMQELSTIHIQGSEQPSLTTSRSSLNLKADDGLRPNCKTSQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSITSNVVKVSVL
Protein: Probable O-methyltransferase Rv1220c (MtbOMT) (EC 2.1.1.-) (P9WJZ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably specifically methylates an O atom of its substrate.
Interaction partners:
- HTH-type transcriptional regulatory protein RaaS
- Conserved protein
- D-alanyl-D-alanine carboxypeptidase DacB1
- Uncharacterized protein
Sequence:
MDGTPGHDDMPGQPAPSRGESLWAHAEGSISEDVILAGARERATDIGAGAVTPAVGALLCLLAKLSGGKAVAEVGTGAGVSGLWLLSGMRDDGVLTTIDIEPEHLRLARQAFAEAGIGPSRTRLISGRAQEVLTRLADASYDLVFIDADPIDQPDYVAEGVRLLRSGGVIVVHRAALGGRAGDPGARDAEVIAVREAARLIAEDERLTPALVPLGDGVLAAVRD
Protein: E3 ubiquitin-protein ligase SDIR1 (EC 2.3.2.27) (Protein SALT- AND DROUGHT-INDUCED RING FINGER 1) (RING-type E3 ubiquitin transferase SDIR1) (Q9M2S6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that acts as a positive regulator of abscisic acid-related stress signal transduction. Interacts with and ubiquitinates ATP1/SDIRIP1 to modulate ATP1/SDIRIP1 stability through the 26S proteasome pathway. Regulates abscisic acid (ABA) and salt stress responses by negatively affecting ATP1/SDIRIP1 stability. The SDIR1-ATP1/SDIRIP1 complex plays an important role in ABA signaling through the ubiquitination pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25616872}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable pterin-4-alpha-carbinolamine dehydratase, chloroplastic
- E3 ubiquitin-protein ligase AIRP1
- E3 ubiquitin-protein ligase AIRP2
- E3 ubiquitin-protein ligase RHA2A
- Probable E3 ubiquitin-protein ligase XERICO
- E3 ubiquitin-protein ligase RHA2B
- E3 ubiquitin-protein ligase KEG
- E3 ubiquitin-protein ligase RMA1
- E3 ubiquitin protein ligase DRIP1
- Zinc finger A20 and AN1 domain-containing stress-associated protein 5
Sequence:
MSFVFRGSRGDLESGFSGGFLPERRAMRVHGARPVNSNSLAFLVTVLLLFMILNSHQMPPNFLLWLVLGVFLMATTLRMYATCQQLQAHAQAQAAAASGLFSHTELRLHVPPSIALATRGRLQGLRLQLALLDREFDDLDYETLRALDSDNVSTTSMSEEEINALPVHKYKVLDPENGCSLAKQASTSSSAEKMLDSANESKKGTEDELTCSVCLEQVTVGEIVRTLPCLHQFHAGCIDPWLRQQGTCPVCKFRAHSGWQEQDEIDDDASDMV
Protein: Gamma-aminobutyric acid permease (GABA permease) (4-aminobutyrate carrier) (4-aminobutyrate permease) (Gamma-aminobutyrate permease) (P25527)
Organism: Escherichia coli (strain K12)
Function: Transporter for gamma-aminobutyrate (GABA). Transport is driven by the membrane potential. Can also transport a number of GABA analogs such as nipecotic acid or muscimol.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11311234, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9806886}; Multi-pass membrane protein {ECO:0000269|PubMed:9806886}.
Interaction partners:
- 4-aminobutyrate aminotransferase GabT
- HTH-type transcriptional repressor GlaR
- Succinate-semialdehyde dehydrogenase [NADP
- L-2-hydroxyglutarate dehydrogenase
- Glutarate 2-hydroxylase
Sequence:
MGQSSQPHELGGGLKSRHVTMLSIAGVIGASLFVGSSVAIAEAGPAVLLAYLFAGLLVVMIMRMLAEMAVATPDTGSFSTYADKAIGRWAGYTIGWLYWWFWVLVIPLEANIAAMILHSWVPGIPIWLFSLVITLALTGSNLLSVKNYGEFEFWLALCKVIAILAFIFLGAVAISGFYPYAEVSGISRLWDSGGFMPNGFGAVLSAMLITMFSFMGAEIVTIAAAESDTPEKHIVRATNSVIWRISIFYLCSIFVVVALIPWNMPGLKAVGSYRSVLELLNIPHAKLIMDCVILLSVTSCLNSALYTASRMLYSLSRRGDAPAVMGKINRSKTPYVAVLLSTGAAFLTVVVNYYAPAKVFKFLIDSSGAIALLVYLVIAVSQLRMRKILRAEGSEIRLRMWLYPWLTWLVIGFITFVLVVMLFRPAQQLEVISTGLLAIGIICTVPIMARWKKLVLWQKTPVHNTR
Protein: Ankyrin repeat-containing protein 01_02 (B3CRR2)
Organism: Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi)
Interaction partners:
Sequence:
MNNYLRLRAHLLYVTTRSIFSHTNSNPLLYAAKHNYLDVVKHLIEHGVDINTQNLRGSTALHIAAYNGNIQMGMFLLANHAEVDTQNVYSNTALYYAVEQSNIEMASILLSYGANPNFQCHFNVTPFEIAWVKYIDNPELHFEMMKLLVTNIVKTEHCNAVDTNLPGFLHNKGLINESEQLKELEQQCHNEIEEMMSISVGENGKSFFDIFVLQKDINTLARCANNPDIVLCQDKFFMYSSFIEKSIKEGKARAKMLQGAVESIDEIFESNQDANQKSQISWLHLPLEVRMMILENLSNTDLTKLQHNDTAEADAEAELEGAYAIYEEE
Protein: Phox domain-containing protein (Q54UN7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- von Willebrand factor A domain-containing protein DDB_G0292028
- Winged helix repair factor 1
- EGF-like domain-containing protein
- EGF-like domain-containing protein
- EGF-like domain-containing protein
- WW domain-containing protein
- Transmembrane protein
- von Willebrand factor A domain-containing protein DDB_G0292188
- Transmembrane protein
- C2 domain-containing protein DDB_G0290753
Sequence:
MGTIYITNQRIVWCAEGDDDDSDNLVTIDIQKIVHQVVTTSQSQQAWKIKTQYATDFIFIFPEPFTREDLHEIIHCFKNSQSQVSNNRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPKLSPPSMTSSPSQYQYQQPQQQRQQPQQQQQYQRQHQPPYHQDSFYPKIVDEDDDEDAVDEVYENEDILQQQQQRQTKEQMLKQQQQLQLQQQQLQQQQQQQLQQQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQQQQQQQQQQQQQQQQMYQQQRQNNNHQQQTNQPQQMQQQQQMKQQQQQQQQQQQQQQQMQNRNNNYQQQNNSRNVINEDNFNNIQLPTTTTTTTTNNNQKDSSPPTKSNNNNNNNQNKKMNEFEDGFFNVPINMVGDDGDSRWEEESNGMPVSGFYDLEVRDPRTHAEENGVYVSYQIIGKYKDDESDQQQQQQQQQEVTNAVSTRRRYREFEWLHSQLSQPSNHHSRIPSLPQKSIYQYWNNTDVALLRQRCSALDQFMKSISVSASLRNHAAVKLFMTQKPIPIQINSLTEIISNNILSPQGALTSLTQAVITTATGVSGGGISTNNNNYLDSIDPNFTNESSVERDYWISRKLMSKWKRIPKRLPFSKFLVVILGTVSAGKSSFINNFFNLQVKVSADEQLDTHFTLIETVPRDRFYELSNQQPMKSKFTKEQLAQRIKGEAVSDPRHGHVFLYLDKTFTLSRYDAQFSNYRDIISNLNLVRTVLINEDYLTGAPDEISNQKKTIFIDSPGFEPKTEHDPEKLLGSIRVVQFFQSTSDLTLFMMKAKELALVSSQIQIVELCVLYKTYGADVVDHMVTQMFNKKGESKSFFSLFEMVKGLVEQIRLKNIPKTQESNGTSVWDGIKFVMTQIDTINSNLKEQYFELGRLLGKGLMFLDPPTYRQCKAIALPIDREFSSPQERSQKCGDLDELLHYIYNLNRGSTYNSRLECAIEEMTTDLLNNIQRSWTNYLFNSDYNLVLQLKERSKNRVSGPSHMHSNSLRR
Protein: N-alpha-acetyltransferase 15, NatA auxiliary subunit (N-terminal acetyltransferase 1) (NMDA receptor-regulated protein 1) (Protein tubedown-1) (Q80UM3)
Organism: Mus musculus (Mouse)
Function: Auxillary subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase (NAT) activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes. {ECO:0000250}.
Interaction partners:
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- Huntingtin-interacting protein K
- N-alpha-acetyltransferase 20
- N-terminal amino-acid N
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 60
Sequence:
MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPGNWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDRFLRMNFSKGCPPVFNTLRSLYRDKEKVAIVEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYVLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSGHPWLHECMIRLFHSVCESKDLPETVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDSSSQKRAIELATTLDGSLTNRNLQTCMEVLEALCDGSLGDCKEAAEAYRASCHKLFPYALAFMPPGYEEDMKITVNGDSSAETEELANEI
Protein: Beta-galactosidase 2 (Lactase 2) (EC 3.2.1.23) (Q9LFA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Beta-galactosidase 17
- Aldose 1-epimerase
- Aldose 1-epimerase
- beta-galactosidase
- Beta-hexosaminidase 3
- Beta-hexosaminidase 2
- Beta-hexosaminidase 1
- Alpha-galactosidase 2
- Alpha-galactosidase 3
- Alpha-galactosidase 1
Sequence:
MSMHFRNKAWIILAILCFSSLIHSTEAVVTYDHKALIINGQRRILISGSIHYPRSTPEMWPDLIKKAKEGGLDVIQTYVFWNGHEPSPGNYYFQDRYDLVKFTKLVHQAGLYLDLRIGPYVCAEWNFGGFPVWLKYVPGMVFRTDNEPFKIAMQKFTKKIVDMMKEEKLFETQGGPIILSQIENEYGPMQWEMGAAGKAYSKWTAEMALGLSTGVPWIMCKQEDAPYPIIDTCNGFYCEGFKPNSDNKPKLWTENWTGWFTEFGGAIPNRPVEDIAFSVARFIQNGGSFMNYYMYYGGTNFDRTAGVFIATSYDYDAPIDEYGLLREPKYSHLKELHKVIKLCEPALVSVDPTITSLGDKQEIHVFKSKTSCAAFLSNYDTSSAARVMFRGFPYDLPPWSVSILPDCKTEYYNTAKIRAPTILMKMIPTSTKFSWESYNEGSPSSNEAGTFVKDGLVEQISMTRDKTDYFWYFTDITIGSDESFLKTGDNPLLTIFSAGHALHVFVNGLLAGTSYGALSNSKLTFSQNIKLSVGINKLALLSTAVGLPNAGVHYETWNTGILGPVTLKGVNSGTWDMSKWKWSYKIGLRGEAMSLHTLAGSSAVKWWIKGFVVKKQPLTWYKSSFDTPRGNEPLALDMNTMGKGQVWVNGHNIGRHWPAYTARGNCGRCNYAGIYNEKKCLSHCGEPSQRWYHVPRSWLKPFGNLLVIFEEWGGDPSGISLVKRTAK
Protein: Guanylate kinase 2 (AtGK2) (EC 2.7.4.8) (GMP kinase 2) (Q9M682)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for recycling GMP and indirectly, cGMP. Required for normal development of the gametophyte and embryo, in association with GK1.
Interaction partners:
- GMP synthase
- Hypoxanthine phosphoribosyltransferase
- Adenine phosphoribosyltransferase 5
- Adenine phosphoribosyltransferase 4
- Adenine phosphoribosyltransferase 1, chloroplastic
- Adenine phosphoribosyltransferase 3
- Adenine phosphoribosyltransferase 2
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
Sequence:
MGEAPAFFVDHLENGYTNGFGVKSEPKNRDTSVLIGDRSFVIGGNHEGNPLFLGVQIHDKVTNKWSSPSVLGTGPKPCKGYSAIVLPKGRILVIKKGSASDDSIWFLEVDTPFIREQKKLLGREVVAWSKGVRGNAEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPRCMEKNGVHYHFTDKTVMEKEIKDGKFLEFASVHGNLYGTSIESVEVVTDSGKRCILDIDVQGARSVKASSLDAIFIFVCPPSMKELEDRLRARGTETEEQIQKRLRNADAEIKAGKSSGIFEHKLYNDNLEECYKTLKNLLGINDLAPVNGVEVEGINLPKEHTVTKMDDKILIQETGEGTKNKMIVLDLSSINGGAPGRTRGIVLDTVKSS
Protein: Huntingtin-interacting protein K (Huntingtin yeast partner K) (Q9CR41)
Organism: Mus musculus (Mouse)
Function: Component of several N-terminal acetyltransferase complexes (By similarity). Inhibits the N-terminal acetylation activity of the N-terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex) (By similarity). Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex (By similarity). May play a role in the NatA complex-mediated N-terminal acetylation of PCNP (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NX55}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX55}. Note=Within the NatA/HYPK complex, may localize to ribosomes. {ECO:0000250|UniProtKB:Q9NX55}.
Interaction partners:
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- Huntingtin
- N-alpha-acetyltransferase 60
- N-alpha-acetyltransferase 11
- N-terminal amino-acid N
- Olfactory receptor 2C1
Sequence:
MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN
Protein: Transforming growth factor beta regulator 4 (C9J347)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAHLVKRCTCLLREAARQAPAMAPVGRLRLAWVAHKTLTSSATSPISHLPGSLMEPVEKERASTPYIEKQVDHLIKKATRPEELLELLGGSHDLDSNQAAMVLIRLSHLLSEKPEDKGLLIQDAHFH
Protein: Rolling pebbles isoform 7 (Q8WS24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MPSLQQIALAMEGDQSELQTPPLPINPPPKVMANGIVYGFRTRHLSCIEENDSDSLHGSSIPHAYDMMQQADETFQKLNANEEQDESGSEAGGLENLDDTIAMIDESRLLEADYLDELVAEEQLQEQDEDEEESSDLVDSGNVEEDFWQPSFNRNDIMMTSVYGALNGSLTSEVSSTAAPGYSECATPRKEAEPVYATPEKRRASNRSFDSTCASLTSSLYGGSMNSSLDLKYSSLGGGDSVSGGISGTSTLRGTSVPPMDLSMISSDGVSALDWGSASVSCVLDSGDGNPAEELNEEMAAKCLSAAESDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSSSMSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGDHTHQHHHRDNQPEGKESNALNTSTCSDSAVTRRRRKNVSNHNLKTSARHGASSENRLNRLSLAGTSVYAGHLSSLVFGKIKSLWSVNSSNSSEAGLNQLAGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: At1g70340 (Dicer-like protein (DUF936)) (F17O7.12) (O64602)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAALAPGILQKLIQGMKTGIKPTREHRSSMLQVTDIVPIDLDEKSLEPKQGFLIKISDSSHSIYVSLPSDQDDVVLSNKLQLGQFIYVDRLEPGSPVPVIKGAKPIPGRHPLLGTPETLVVPKERTDQEIGSKPRRGSWGQNVDFSSSPFVVKPMALEFDHSTPAKRSVSARFAASPIRRGGVRCSFGGGVLGKLEGESPATAMLRKSCFVSSASKFPRSRSVCDRQAKKNNASLFSPFKSSLEAQEDVVPLSTSKKIKPEKDTNLSGRLNILSKEATQLREVAQKVALQALREATITEIVVRHTKTFTNLSKSAKADCPAVCFEKFMEFHQQMAQTIGELTSIEVAATPDAENKSQNINARTENQKPTEEGSSSILHEIAYNSIDQEKRRSKRRIVLKQQSEGKTVRSNDENKNPASGGISNTIRLAKEIEDEAANWFMEFIEIALEKGMKKSRGPDDADVKKVPQSLILGVLNWIEVEQSDSNNNKRRRVHPKASKITRKLRIKLKNP
Protein: Peroniin-1.2 (P86489)
Organism: Litoria peronii (Emerald spotted tree frog) (Hyla peronii)
Function: Induces contraction of intestinal smooth muscle in isolated guinea pig ileum.
Subcellular location: Secreted {ECO:0000269|PubMed:19642086}.
Interaction partners:
Sequence:
QPWIPFV
Protein: WFS1 (Q9JLT5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSGTPPPSPSGPPPPPAPQPQARARLNATTSLEQDKIEPPRAPRPQPDSSAGRSAGEATTPEPRAPHASSREGTDKAGPMKADVEIPFEEILEKAKAGDPKAQTEVGKHYLRLANDADEELNSCSAVAWLILAAKQGRREAVKLLRRCLADRKGITSENEAEVKQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVSELLENVGQVNEQDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVELTKKYAKGIIPNNLFLQDEDEDEDELSGKSPEDLPLRQKVVKYPLHAIMEIKEYLIDVASKAGMHWLSTIVPTHHINALIFFFIISNLTIDFFAFFIPLVVFYLSFVSMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYIHFLLSVVFVIFSFPLASKDCIPCSELAVVSAFFTVTSYMSLSSSAEPYTRRALVTEVAAGLLSLLPTMPVDWPFLKALGQTFFTVPIGHFIILNVSLPCLLYVYLFYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLQSTGLGLVRASIGYFLFLFALPILVAGLALMGTVQFARWFLSLDLTKIMVTTVICSVPLLFRWWTKANFSVVGMVKSLTRSSIVKLILVWLTAILLFCWFYVYRSEGMKVYNSTLTWQQYGFLCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTEIDNSAESAINMLPFFLGDWMRCLYGEAYPSCSSGNTSTAEEELCRLKQLAKHPCHIKKFDRYKFEITVGMPFGTNGNRGHEEDDITKDIVLRASSEFKDVLLNLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMTQLSPARRHVKIEQDWRSTVHGALKFAFDFFFFPFLSAA
Protein: Homeobox protein Hox-B4 (Homeobox protein Hox-2.6) (P10284)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B3
- Homeobox protein Hox-B5
- Homeobox protein Hox-B6
- Homeobox protein Hox-B7
- Homeobox protein Hox-D4
- Homeobox protein Hox-A5
- Cullin-4A
Sequence:
MAMSSFLINSNYVDPKFPPCEEYSQSDYLPSDHSPGYYAGGQRRESGFQPEAAFGRRAPCTVQRYAACRDPGPPPPPPPPPPPPPPGLSPRAPVQPTAGALLPEPGQRSEAVSSSPPPPPCAQNPLHPSPSHSACKEPVVYPWMRKVHVSTVNPNYAGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRVEIAHALCLSERQIKIWFQNRRMKWKKDHKLPNTKIRSGGTAGAAGGPPGRPNGGPPAL