wanglab/gogpt-training-data huggingface dataset:
Protein: Glutathione S-transferase F14 (AtGSTF14) (EC 2.5.1.18) (GST class-phi member 14) (Q9C6C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- At5g44000
- AT5g45020/K21C13_21
- Glutathione S-transferase U21
- Glutathione S-transferase family protein
- Glutathione S-transferase U15
- Glutathione S-transferase U28
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase DHAR2
- Glutathione S-transferase U11
Sequence:
MADSKMKLHCGFIWGNSAALFCINEKGLDFELVFVDWLAGEAKTKTFLSTLNPFGEVPVLEDGDLKLFEPKAITRYLAEQYKDVGTNLLPDDPKKRAIMSMWMEVDSNQFLPIASTLIKELIINPYQGLATDDTAVQENKEKLSEVLNIYETRLGESPYLAGESFSLADLHHLAPIDYLLNTDEEELKNLIYSRPNVAAWVEKMKMRPAWLKTVVMKNHIVDLMKQRRLPIKLDSSCHESTVVAQKNAIAIENK
Protein: Ribonuclease toxin YhaV (EC 3.1.-.-) (Ribonuclease YhaV) (P64594)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity in vitro. Overexpression leads to growth arrest after 30 minutes; these effects are overcome by concomitant expression of antitoxin SohA (PrlF). Massive overexpression is toxic. Unlike most other characterized TA systems degrades rRNA, and co-folding of the both TA proteins is necessary in vitro for inhibition of the RNase activity. It is not known if it has any sequence-specificity. Acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression.
Interaction partners:
- Antitoxin PrlF
- Toxin YoeB
- Antitoxin YefM
- mRNA interferase toxin YafQ
- mRNA interferase toxin MqsR
- mRNA interferase toxin RelE
- mRNA interferase toxin HigB
- Endoribonuclease toxin ChpB
- Antitoxin DinJ
- Endoribonuclease toxin MazF
Sequence:
MDFPQRVNGWALYAHPCFQETYDALVAEVETLKGKDPENYQRKAATKLLAVVHKVIEEHITVNPSSPAFRHGKSLGSGKNKDWSRVKFGAGRYRLFFRYSEKEKVIILGWMNDENTLRTYGKKTDAYTVFSKMLKRGHPPADWETLTRETEETH
Protein: Chromosome 11 open reading frame 54 (E9PSC3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFIL
Protein: Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G) (P9WMJ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Molecular chaperone. Has ATPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
Interaction partners:
- Chaperone protein DnaK
- Conserved hypothetical proline rich protein
- Conserved hypothetical proline and threonine rich protein
- Hypothetical alanine and valine rich protein
- Chaperone protein DnaJ 2
- Chaperone protein DnaJ 1
- Co-chaperonin GroES
- Chaperonin GroEL 1
- Tetratrico peptide repeat group 5 domain-containing protein
- Omega-hydroxy-beta-dihydromenaquinone-9 sulfotransferase Stf3
Sequence:
MNAHVEQLEFQAEARQLLDLMVHSVYSNKDAFLRELISNASDALDKLRIEALRNKDLEVDTSDLHIEIDADKAARTLTVRDNGIGMAREEVVDLIGTLAKSGTAELRAQLREAKNAAASEELIGQFGIGFYSSFMVADKVQLLTRKAGESAATRWESSGEGTYTIESVEDAPQGTSVTLHLKPEDAEDDLHDYTSEWKIRNLVKKYSDFIAWPIRMDVERRTPASQEEGGEGGEETVTIETETLNSMKALWARPKEEVSEQEYKEFYKHVAHAWDDPLEIIAMKAEGTFEYQALLFIPSHAPFDLFDRDAHVGIQLYVKRVFIMGDCDQLMPEYLRFVKGVVDAQDMSLNVSREILQQDRQIKAIRRRLTKKVLSTIKDVQSSRPEDYRTFWTQFGRVLKEGLLSDIDNRETLLGISSFVSTYSEEEPTTLAEYVERMKDGQQQIFYATGETRQQLLKSPHLEAFKAKGYEVLLLTDPVDEVWVGMVPEFDGKPLQSVAKGEVDLSSEEDTSEAEREERQKEFADLLTWLQETLSDHVKEVRLSTRLTESPACLITDAFGMTPALARIYRASGQEVPVGKRILELNPSHPLVTGLRQAHQDRADDAEKSLAETAELLYGTALLAEGGALEDPARFAELLAERLARTL
Protein: Sialidase-4 (EC 3.2.1.18) (N-acetyl-alpha-neuraminidase 4) (Neuraminidase 4) (Q8BZL1)
Organism: Mus musculus (Mouse)
Function: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Efficiently hydrolyzes gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3. Hydrolyzes poly-alpha-(2->8)-sialylated neural cell adhesion molecule NCAM1 likely at growth cones, suppressing neurite outgrowth in hippocampal neurons. May desialylate sialyl Lewis A and X antigens at the cell surface, down-regulating these glycan epitopes recognized by SELE/E selectin in the initiation of cell adhesion and extravasation (By similarity). Has sialidase activity toward mucin, fetuin and sialyllactose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22393058}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Microsome membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8WWR8}; Peripheral membrane protein. Cell projection, neuron projection {ECO:0000269|PubMed:22393058}. Lysosome lumen {ECO:0000250|UniProtKB:Q8WWR8}.
Interaction partners:
- Arylsulfatase A
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Galactocerebrosidase
- Galactosylceramide sulfotransferase
- Alpha-galactosidase A
- Lysosomal protective protein
- Beta-galactosidase
- Sialidase-1
Sequence:
MGPTRVPRRTVLFQRERTGLTYRVPALLCVPPRPTLLAFAEQRLSPDDSHAHRLVLRRGTLTRGSVRWGTLSVLETAVLEEHRSMNPCPVLDEHSGTIFLFFIAVLGHTPEAVQIATGKNAARLCCVTSCDAGLTWGSVRDLTEEAIGAALQDWATFAVGPGHGVQLRSGRLLVPAYTYHVDRRECFGKICWTSPHSLAFYSDDHGISWHCGGLVPNLRSGECQLAAVDGDFLYCNARSPLGNRVQALSADEGTSFLPGELVPTLAETARGCQGSIVGFLAPPSIEPQDDRWTGSPRNTPHSPCFNLRVQESSGEGARGLLERWMPRLPLCYPQSRSPENHGLEPGSDGDKTSWTPECPMSSDSMLQSPTWLLYSHPAGRRARLHMGIYLSRSPLDPHSWTEPWVIYEGPSGYSDLAFLGPMPGASLVFACLFESGTRTSYEDISFCLFSLADVLENVPTGLEMLSLRDKAQGHCWPS
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (V9HW04)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR
Protein: Transducer of Cdc42-dependent actin assembly protein 1 homolog (Q19253)
Organism: Caenorhabditis elegans
Function: Plays a role in protein trafficking, actin organization and embryonic morphogenesis. Potentially acts as cdc-42 effector. May play a role in hypodermal P-cell nuclear positioning. Together with toca-2, is required for protein trafficking regulating yolk protein clathrin-mediated endocytosis by oocytes during oogenesis and retrograde recycling and the sorting of recycling endosome cargo proteins such as mig-14. Also, together with toca-2, controls the distribution of actin at cell junctions.
Subcellular location: Cell junction {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:23150597}. Apical cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Basolateral cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Cytoplasmic vesicle {ECO:0000269|PubMed:19798448}. Cytoplasm {ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23150597}. Recycling endosome {ECO:0000269|PubMed:25775511}. Note=Co-localizes with ajm-1 at cell junctions (PubMed:19798448). Co-localizes with toca-2, rme-1, cdc-42 and wve-1 on recycling endosomes (PubMed:25775511). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
Interaction partners:
- Cell division control protein 42 homolog
- CRIB domain-containing protein
- Wiskott-Aldrich syndrome protein family member
- Unconventional myosin-Ie
- Transducer of Cdc42-dependent actin assembly protein 2 homolog
- Osteoclast-stimulating factor 1
- tRNA-intron lyase
- SH3 domain-containing protein
- WH1 domain-containing protein
- Actin
Sequence:
MNDSCSWDQLWDQQGTLNEYTGKGIDLLERIMAYSKERASIELEYSSKLKALSKKTAMKMKSESELWNSVSYVKGFHDVIAGIVPVATQHELIAENLKSAVIPFTTQKIAEYRVAKKQLESDNSNLGKQLRMVIDEMAKSHKEYVKCYKETEAAMLKYAKAEKNMDISRLELEKTKNNYQQKCGMLEESKQTYAVMTTKANEEQSAHYDRKLPQLLDNYKKLHTNRILDTVEILSKCVEAESCVNQIIASCHNDMRRDIGLIDPSRDANLVVENMKSGHPVPQPFVFEDLGHPQDRSSFMGGGASGPAGSMDGMDATMKKGGTLMSKNGKGVARKQSMHQKFFGGGTADKKTDSGDYGTLPPQQRARKIAGKISDLEKEKDRATQSREGVSKMQAAYRENPKLGNPSDCDAQLAQYGHEIDALSNQIQKFKILLDDVNAQLGAGGLSATSVGGSDTPPSIRSVSSASSGVTSRVNTINDAHRTNGGVGGGRRESFSGSNGGSDTDPTINGNGHGRDELYEECSNPNPVLGEAIAQFAFDGAQDGTIRMEANEKLWLIEKDEGDGWTRVRKENNSADGFVPSSYLKVTWFGKV
Protein: IGF-II mRNA-binding protein, isoform K (Q0KHU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHSNNNSSRLNNNISNNYYQQKQSLIRYLDRVTTSKILISGIPMQTRFEDIEPLLKPYGIVKQCEAISSKDQNTQTVHITFENPEQAQRAAVGLNGVEFEGSKLHAEQLDKNQRRSQRNQRNPYPGMPGPGRQADFPLRILVQSEMVGAIIGRQGSTIRTITQQSRARVDVHRKENVGSLEKSITIYGNPENCTNACKRILEVMQQEAISTNKGELSPECSEICLKILAHNNLIGRIIGKSGNTIKRIMQDTDTKITVSSINDINSFNLERIITVKGLIENMSRAENQISTKLRQSYENDLQAMAPQSLMFPGLHPMAMMSTPGNGMVFNTSMPFPSCQSFAMSKTPASVVPPVFPNDLQETTYLYIPNNAVGAIIGTRGSHIRSIMRFSNASLKIAPLDADKPLDQQTERKVTIVGTPEGQWKAQYMIFEKMREEGFMCGTDDVRLTVELLVASSQVGRIIGKGGQNVRELQRVTGSVIKLPEHALAPPSGGDEETPVHIIGLFYSVQSAQRRIRAMMLSTNPPPITKKQKAAKEQLQQQQQSLAGAASSGSQQQQPQSPSQQQALPPQLHHQPVSSASSSSTPPAHHQQQASTAATSHQLQQQQPSPPPPGNATAAAAQQQQQLASSQQ
Protein: Kinase (EC 2.7.-.-) (Q7KV26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- inositol-polyphosphate 5-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Uncharacterized protein, isoform C
- LD06095p
- Multiple inositol polyphosphate phosphatase 1
- Multiple inositol polyphosphate phosphatase 1
Sequence:
MIVQQQQQQQLSNEGEPKTLPGATASNSDEGCNVTGGGLSPYSSDNEDNSLSPRQRKMKVTRCASSDSALGLDVDDGGMDVPLPPQRRMTLTVTDLPLRPALLPLAEPTALPDSPLTSPTGGGNPSVGVPTKVLLEERVVAAPGSRRESTQSSYSELGVSGLPLGVRYVRTPSVVVSDYSDDITACGISMEEMEYFRLQRARGQRRCSLEAGHHSHSGGHGAHGHGGSGAAGMSPGCGKDDGQSDVSAASSCSNLYYCGSTISALDGGECIVNGVRVALARKSSTQSSSLSDEEEEEEDDDEDRDEQDRDEDDRDAEEMLQEDYERGDRERERERQISELMAATQLGDRQRDRSKKSSGWRKIRNIVQWTPFFQTYKKQRYPWVQLAGHQGNFKAGPEPGTVLKKLCPKEEECFQILMHDLLRPYVPVYKGQVTSEDGELYLQLQDLLSDYVQPCVMDCKVGVRTYLEEELSKAKEKPKLRKDMYDKMIQIDSHAPTAEEHAAKAVTKPRYMVWRETISSTATLGFRIEGIKKSDGTSSKDFKTTKSREQIKLAFLEFLSGHPHILPRYIQRLRAIRATLAVSEFFQTHEVIGSSLLFVHDQTHASIWLIDFAKTVELPPQLRIDHYSAWKVGNHEDGYLIGINNLIDIFVELQASMEAEAHAQAQAEAIQSPVSGSGGDQAEQTGEESKP
Protein: Nephrocystin-1 (Juvenile nephronophthisis 1 protein) (O15259)
Organism: Homo sapiens (Human)
Function: Together with BCAR1 it may play a role in the control of epithelial cell polarity (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling (By similarity). May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development (By similarity). In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity).
Subcellular location: Cell junction {ECO:0000250|UniProtKB:Q9QY53}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9QY53}. Cell projection, cilium {ECO:0000269|PubMed:16885411}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:16885411}. Cell junction, tight junction. Note=In the retinal photoreceptor cell layer, localizes at the connecting cilium (By similarity). Colocalizes with E-cadherin and BCAR1 at or near the cell-cell adherens junctions (By similarity). Localized to respiratory cilia axoneme (PubMed:16308564, PubMed:16885411). Localized to the transition zone of respiratory cilia (PubMed:16885411). Localized to the transition zone of photoreceptor-connecting cilia and renal monocilia (By similarity). In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates at basolateral tight junctions (By similarity). {ECO:0000250|UniProtKB:Q9QY53, ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:16885411}.
Interaction partners:
- Nephrocystin-4
- Protein fantom
- Meckelin
- Jouberin
- Nephrocystin-3
- Centrosomal protein of 290 kDa
- Inversin
- Tectonic-like complex member MKS1
- Coiled-coil and C2 domain-containing protein 2A
- X-linked retinitis pigmentosa GTPase regulator
Sequence:
MLARRQRDPLQALRRRNQELKQQVDSLLSESQLKEALEPNKRQHIYQRCIQLKQAIDENKNALQKLSKADESAPVANYNQRKEEEHTLLDKLTQQLQGLAVTISRENITEVGAPTEEEEESESEDSEDSGGEEEDAEEEEEEKEENESHKWSTGEEYIAVGDFTAQQVGDLTFKKGEILLVIEKKPDGWWIAKDAKGNEGLVPRTYLEPYSEEEEGQESSEEGSEEDVEAVDETADGAEVKQRTDPHWSAVQKAISEAGIFCLVNHVSFCYLIVLMRNRMETVEDTNGSETGFRAWNVQSRGRIFLVSKPVLQINTVDVLTTMGAIPAGFRPSTLSQLLEEGNQFRANYFLQPELMPSQLAFRDLMWDATEGTIRSRPSRISLILTLWSCKMIPLPGMSIQVLSRHVRLCLFDGNKVLSNIHTVRATWQPKKPKTWTFSPQVTRILPCLLDGDCFIRSNSASPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGVPIPAKTYELFLNGGTPYEKGIEVDPSISRRAHGSVFYQIMTMRRQPQLLVKLRSLNRRSRNVLSLLPETLIGNMCSIHLLIFYRQILGDVLLKDRMSLQSTDLISHPMLATFPMLLEQPDVMDALRSSWAGKESTLKRSEKRDKEFLKSTFLLVYHDCVLPLLHSTRLPPFRWAEEETETARWKVITDFLKQNQENQGALQALLSPDGVHEPFDLSEQTYDFLGEMRKNAV
Protein: Transcription elongation factor 1 homolog (O13868)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription elongation factor spt5
- Transcription elongation factor spt4
- Transcription factor iws1
- Cell division control protein 73
- Uncharacterized protein C13E7.08c
- FACT complex subunit spt16
- DNA-directed RNA polymerase II subunit rpb4
- Transcription elongation factor spt6
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MGKRKAKAKVKPKRRAPPLDTTFTCLFCNHEKSVSCSLDKQSGVGNLHCKICGQSHQCLITALSAPIDVYSDWIDACDAVANQAKEVDNINDQEAYSPEAAYEEEKE
Protein: Sorting nexin-14 (Q5PNP1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in maintaining normal neuronal excitability and synaptic transmission. May be involved in several stages of intracellular trafficking (By similarity). Required for autophagosome clearance, possibly by mediating the fusion of lysosomes with autophagosomes. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), a key component of late endosomes/lysosomes. Does not bind phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BHY8}.
Interaction partners:
- Sorting nexin-13
- Synergin, gamma.
- Sorting nexin 2.
- Pseudouridine 5'-phosphatase.
Sequence:
MSDPHSFLGCVRRGLRFDMFKDVARQYPVIFCIFTVMISSTIILNQYLHILMVFWSFLAGVITFYCSLSPEYLLPNILISIKTKRKPQEQHELFPLGHSCAVCGKNQCKRHRPTLLLENYQPWLNLKVPSKVDASISEVLELVLENFVYPWYRDITDDEACVDELRQTIRFFAAVLAHRAQRVDVPSVVMDKMMKAAMKHIEIIAKAQQKVRNTDGLEQAALAEYGADLHVALRSRKDELLYLRKLTELLFPYVMPPKATDCRSLALLIREVMTGSVFLPIMDFVADPDTVNHMVLIFIDDSPPEPVTDPPSTLVPFLERFADPRTKKSSVLKLDLKEIREQQDLLFRFMSFLKEEGAVHVLQFCLTVEEFNDRILCPDLSDDEKQRLHEEVKKIYETYCLEESIDKISFDPFIIEEIHSIAEGPYTGVVKLQTMRCLFEAYEHVLCLLEKVFTPMFCHSDEYFRHLLCGAESPARNSKLNRNTSKRGESFGISRIGSKIKGVFKSSTMEGAMLPQYAMIEGEDDTVEEAVMVFEDDSPGPMDAVGTPGTLRNLSAWTISIPYVDFYDDEVKKERIPVFCIDVERNDRKNVGHETESWSVYRKYVEFYVLESKLTEFHGPFQDAQLPSKRIIGPKNYEFLSSKRGEFEEYLQKLLHHPELSNSQLLADFLSPFSMESQFRDKMLPDVNLGKIFKSVPGKLIKEKGQNLEPFIQSFFSSCESPKPKPSRPELTILSPTAENNKKLFNELYRNNANLPEGLEKKHNQNYFMELMEVDGAYDYMMYIGRVVFRMPDWLHHLLSGVRILLKRTLEAYVGHYFQYKLEQIMEEHRLVSLVTLLRDAVFCESTEERSPEDKQRRAKQTFEEMMNYLPDIVGKCIGEEAKYDGVKMLFNTIQQPLLNKQMTYVLLDIAIQELFPELSKNQKQGLSVSTRWM
Protein: U3 small nucleolar RNA-associated protein 7 (U3 snoRNA-associated protein 7) (U three protein 7) (P40055)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
Interaction partners:
- RNA cytidine acetyltransferase
- rRNA processing protein RCL1
- U3 small nucleolar RNA-associated protein MPP10
- U3 small nucleolar RNA-associated protein 18
- U3 small nucleolar RNA-associated protein 13
- Ribosome biogenesis protein ENP2
- rRNA-processing protein FCF1
- U3 small nucleolar RNA-associated protein 16
- Periodic tryptophan protein 2
- Protein SOF1
Sequence:
MGHKKNGHRRQIKERENQNKFERSTYTNNAKNNHTQTKDKKLRAGLKKIDEQYKKAVSSAAATDYLLPESNGYLEPENELEKTFKVQQSEIKSSVDVSTANKALDLSLKEFGPYHIKYAKNGTHLLITGRKGHVASMDWRKGQLRAELFLNETCHSATYLQNEQYFAVAQKKYTFIYDHEGTELHRLKQHIEARHLDFLPYHYLLVTAGETGWLKYHDVSTGQLVSELRTKAGPTMAMAQNPWNAVMHLGHSNGTVSLWSPSMPEPLVKLLSARGPVNSIAIDRSGYYMATTGADRSMKIWDIRNFKQLHSVESLPTPGTNVSISDTGLLALSRGPHVTLWKDALKLSGDSKPCFGSMGGNPHRNTPYMSHLFAGNKVENLGFVPFEDLLGVGHQTGITNLIVPGAGEANYDALELNPFETKKQRQEQEVRTLLNKLPADTITLDPNSIGSVDKRSSTIRLNAKDLAQTTMDANNKAKTNSDIPDVKPDVKGKNSGLRSFLRKKTQNVIDERKLRVQKQLDKEKNIRKRNHQIKQGLISEDHKDVIEEALSRFG
Protein: Pentapeptide repeat family protein (O50390)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MQQWVDCEFTGRDFRDEDLSRLHTERAMFSECDFSGVNLAESQHRGSAFRNCTFERTTLWHSTFAQCSMLGSVFVACRLRPLTLDDVDFTLAVLGGNDLRGLNLTGCRLRETSLVDTDLRKCVLRGADLSGARTTGARLDDADLRGATVDPVLWRTASLVGARVDVDQAVAFAAAHGLCLAGG
Protein: Citramalyl-CoA lyase, mitochondrial (EC 4.1.3.25) ((3S)-malyl-CoA thioesterase) (EC 3.1.2.30) (Beta-methylmalate synthase) (EC 2.3.3.-) (Citrate lyase subunit beta-like protein, mitochondrial) (Citrate lyase beta-like) (Malate synthase) (EC 2.3.3.9) (Q8R4N0)
Organism: Mus musculus (Mouse)
Function: Mitochondrial citramalyl-CoA lyase indirectly involved in the vitamin B12 metabolism. Converts citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway (By similarity). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite. Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate (By similarity). Also displays malyl-CoA thioesterase activity. Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (By similarity). Also has very weak citramalate synthase activity in vitro (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18614015}.
Interaction partners:
- Succinyl-CoA:glutarate CoA-transferase
Sequence:
MALCVLRNTVRGAAALPRLKASHVVSVYKPRYSSLSNHKYVPRRAVLYVPGNDEKKIRKIPSLKVDCAVLDCEDGVAENKKNEARLRIAKTLEDFDLGTTEKCVRINSVSSGLAEVDLETFLQARVLPSSLMLPKVEGPEEIRWFSDKFSLHLKGRKLEQPMNLIPFVETAMGLLNFKAVCEETLKTGPQVGLCLDAVVFGGEDFRASIGATSNKDTQDILYARQKVVVTAKAFGLQAIDLVYIDFRDEDGLLRQSREAAAMGFTGKQVIHPNQIAVVQEQFTPTPEKIQWAEELIAAFKEHQQLGKGAFTFRGSMIDMPLLKQAQNIVTLATSIKEK
Protein: NUCB1 protein (Q96BA4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MREMEEERLRMREHVMKNVDTNQDRLVTLEEFLASTQRKEFGDTGEGWETVEMHPAYTEEELRRFEEELAAREAELNAKAQRLSQETEALGRSQGRLEAQKRELQQAVLHMEQRKQQQQQQQGHKAPAAHPEGQLKFHPDTDDVPVPAPAGDQKEVDTSEKKLLERLPEVEVPQHL
Protein: N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54) (Q8BH82)
Organism: Mus musculus (Mouse)
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain. May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation. As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- Monoglyceride lipase
- Glycerophosphodiester phosphodiesterase 1
- 
- N-acylethanolamine-hydrolyzing acid amidase
- G-protein coupled receptor 55
- Lysophosphatidylserine lipase ABHD12
- Monoacylglycerol lipase ABHD6
- Cannabinoid receptor 1
- Diacylglycerol lipase-beta
Sequence:
MDEYEDSQSPAPSYQYPKETLRKRQNSVQNSGGSVSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNISIPNVLRWLIMEKNHSGVPGSKEELDKELPVLKPYFVSDPEDAGVREAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPSQYMGPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDLQTKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLSCEDFFILKHGESRYLNTDDRAFEET
Protein: RT06796p1 (Tombola) (Q9VMQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Testis-specific zinc finger protein topi
- Cookie monster
- Always early, isoform A
- LD06557p
- Lin-52, isoform A
- LD07342p
Sequence:
MPSPKKRSVDKADGKKGKGQGAGGVKGCCCKRSQCIKNYCDCYQSMAICTKFCRCVGCRNTEVRELVDPNSVAKNSSAVKRQKAAAMSAKAAAAAAKAGIDVQGKALQVAASTLALPGKALMTPPKYTLVAGKPPMASSHINPIPISRPIATAATPARAVKQPAEPPMPVNLIIPVRHDDRRDRNLFVQPVNAALLECMLIQATEAEQLGLNELQVCQLVLEEFMRGYKNILEKICEYSKDYY