wanglab/gogpt-training-data huggingface dataset:
Protein: Dedicator of cytokinesis protein 5 (Lens rupture protein 2) (Rupture of lens cataract protein) (B2RY04)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18396277}. Cell membrane {ECO:0000250|UniProtKB:Q9H7D0}. Cell projection, podosome {ECO:0000269|PubMed:27505886}. Note=Associated with the edge of the plasma membrane in intestinal epithelial cells spreading on type IV collagen. {ECO:0000250|UniProtKB:Q9H7D0}.
Interaction partners:
- Engulfment and cell motility protein 1
- Adapter molecule crk
- Engulfment and cell motility protein 2
- Crk-like protein
- Rho-related GTP-binding protein RhoG
- Ras-related C3 botulinum toxin substrate 1
- Cell division control protein 42 homolog
- Engulfment and cell motility protein 3
Sequence:
MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEATVEDGGQHETVIPGELPLVQELTNTLREWAVIWRKLYVNNKVTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTVALFRAHEVASKRIEEKIQEEKSILQNLDLRGQAIFSTVHTYGLYVNFKNFVCNIGEDAELFIALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSTDLIRPRISLVCQIVRVGRMELKEGKKHTCGLRRPFGVAVMDISDIVHGKVDDEEKQHFIPFQQIAMETYIRQRQLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHLVDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVFDEEGNLLEKAIHPGAGYEGVSEYKSVVYYQVKQPCWYETVKVFIAIEEVTRCHIRFTFRHRSSQESRDKSERAFGVAFVKLMNADGTTLQDGRHDLVVYKGDNKKMEDAKYYLTLPGTKAELEEKELQASKNPSVFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEVDGGEIVKFLQDTLDALFNIMMEMSDNETYDFLVFDALVFIISLIGDIKFQHFNPVLETYIYKHFSATLAHVKLSKVLNFYVANAEDPSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQSEDGDEFNDSIRQLFLAFNTLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPMELSVLFCKFIQSIPDNQLVRQKLNCMTKIVESSLFQQAECREVLLPLLTDQLSGQLDDHSTKPDHEASSQLLSNILEVLDRTDVGPTSAHVQLIMERLLRRINRTVIGMSRQSPHIGSFVACMIAVLRQMEDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAINQFAEVLTKSFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSEAKRNKIVKKYGDMRKEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNLSGNGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLANSGEAFAFLVSSLLENLLDYRTIIIHDESKENRMSCTVNVLNFYKDKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQRDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGSLLKKRALFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYLQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFSYSRPFRKGEKDPENEFATMWIERTTYRTAYTFPGILKWFEAKEISVEEISPLENAIETMELTNERVSNCVQQHAWDHSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQIPLLTEGIRIHGEKLTEQLKPLHARLSSCFRELKEKVEKLYGVITLPPSMTERKPSRAGSMVLPYILSSTLRRLSVTSVASSVISTSSNSSDNASSRPGSDGSILEPLFERRASSGARVEDLPPKEDSENRISKFKRKDWNLSKSQVIAEKAPEPDVMSPGKKTQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLTASVPPPPPPKSKPYESSQRNSAEIAPPLPVRRDSKAPPPPPPKARKSGILSSEPGSQ
Protein: GEO04167p1 (GH10517p) (Q8SXB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPRRSLLCCLLVSSILVLHQAQANIETNDVNDPSYYMLQGVRVYPNDRQCVMVGGLCVAESDCIEPTSNKGLCPTSAGEGVECCYELRSNPTPASHR
Protein: Trafficking protein particle complex subunit 3 (BET3 homolog) (O43617)
Organism: Homo sapiens (Human)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 10
Sequence:
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDKMGFNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSSLIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
Protein: Large ribosomal subunit protein uL4m (Q9V3D0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL9m
- Ribosomal protein
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL13m
Sequence:
MLNNILKTSRQVLYPVARTFSRSGNHGNVVTEAAATVGAPPATRSPLILPQDYTDCLPVSRNTARQAWIENTDAVAERKVGLIELHPDVFAAQPRVDIIQENVEWQSKYRYVSMAHTKTRAEVRGGGRKPWPQKGGGRARHGSLRSPMLKGGGVVHGPRSPTTHFYMLPFYKRVLGLTSTLSVKLAQDDLHIIDNVDIPTGDAEFLKDLIAERNWGPSVLIVDEDHMFPANICQASDDLGYVNLMPTFGLNVYSMLKHDTLVLTVAAVKHLEQRLLYQLNRNDAASKGGKFKLDQV
Protein: Actin-related protein 2/3 complex subunit 3 (B2GV73)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR016315}.
Interaction partners:
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
Sequence:
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSRSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPASKQEDETMRAYLQQLRQETGLRLCDKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
Protein: Chloride channel protein ClC-Ka (Chloride channel Ka) (ClC-K1) (Q9WUB7)
Organism: Mus musculus (Mouse)
Function: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. May be the basolateral chloride channel mediating net chloride absorption in CTAL cells.
Subcellular location: Basolateral cell membrane {ECO:0000305|PubMed:11734858}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Barttin
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Chloride channel protein ClC-Kb
Sequence:
MEELVGLREGSSGKPVTLQELWGPCPRIRRGIRGGLEWLKERLFRAREDWYFLVALGVLMALISYAMNFAIGRVVRAHKWLYREVGDGHLLRYLSWTVYPVALLSFSSGFSQSITPFSGGSGLPELKTMLSGVVLENYLDIKNFGAKVVGLSCTLATGSTIFLGKVGPFVHLSVMISAYLGRVRAKAVGDTESKAKEVEMLSAAAAVGVATVFAAPFSGVLFSIEVMSSHFSVWNYWRGFFAATCGAFMFRLLAVFNSEQETITSIYKTRFRVDVPFDLPEIFFFVALGFICGILSCVYLFCQRNFLRFIKTNRYTSKLLATSKPSYAALVALVLASVTYPPGVGRFMASRLSMAEHLHSLFDNNSWALMTRNASPPWPSEPDPQNLWFEWYHPRFTIFGTLAFFLIMKFWMLILATTIPMPAGYFMPIFIIGAAIGRLLGEALSVAFPEGIVAGGEVYPIMPGGYALAGAAAFSGAVTHTISTALLAFELTGQIVHALPVLMAVLAANVISQNLQPSFYDGTIMAKKLPYLPWIRGRQIGSYPVTVEHFMNSNLTTLAKDMPLEEVVKVVTSTDVSQYPLVETRESQTLVGIVERTHLVQALQTQPASWAPGQERFLQDILAGGCPTQPVTLQLSPETSLYQAHRLFELLTLQALFVTSRGRAVGSVSWVELKKAISTLINPPAPK
Protein: Ribose-phosphate pyrophosphokinase 2 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase II) (PRS-II) (Q9CS42)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Interaction partners:
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Amidophosphoribosyltransferase
- Phosphoribosyl pyrophosphate synthase-associated protein 2
- Transketolase
- Ribokinase
- Transketolase-like protein 1
- Ribose-5-phosphate isomerase
- Transketolase-like protein 2
- Phosphopentomutase
- ADP-ribose pyrophosphatase, mitochondrial
Sequence:
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGCGEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENITEWRNCIIVSPDAGGAKRVTSIADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATKVYAILTHGIFSGPAISRINSAAFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
Protein: C2H2 zinc finger transcription factor (Q9U1K4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNHHMHQGLLGKVEAGAAAFGGVYSRHPYDWPFNAVTHKEAASVNSGWWDMHSAAGSWLDMGGAGMHSTMANYASENYSSALSHSLLGSGQHLLQDTYKSMLPGQGVGVGVGVGMGGFSLPHSSPSAAAAAAATAAAAAGGSPQGGSPSTPSPRSQRRYAGRATCDCPNCQEAERLGPAGVHLRKKNIHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRGDHLAKHVKTHNGTANHQANGHNGGLKKGSSESCSDSEEAANQSGESNGLGGVGSGPQTGGAGGGGGGSSSGNGAGTLAVSGSVTTGAGAGSGTGSSNSNSNSGGSSGSVSGSVSGSGSHPGTPTSLHAHSANGTSSSLLGGGLHLATPHQMVAAGGSPVMLHQQQQQQQHQQQQQQQQQQQQQQHQQQQQQQHQQQQQQHQQQQQQHHQQQQQHHHQQFGQQQHPHAHHLHHHAHHAHHLATGGSPGLDPSSLVDIKPPMV
Protein: Hydroxyproline O-arabinosyltransferase 2 (EC 2.4.2.58) (Q494Q2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase involved in the O-arabinosylation of several proteins including extensins and small signaling peptides. Catalyzes the transfer of the initial L-arabinose to the hydroxyl group of Hyp residues. Contributes redundantly with HPAT1 and HPAT3 to arabinosylation of EXT3.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:24036508}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Arabinosyltransferase RRA1
- Arabinosyltransferase RRA2
- Arabinosyltransferase XEG113
- Hydroxyproline O-arabinosyltransferase 3
- Hydroxyproline O-arabinosyltransferase 1
- Arabinosyltransferase RRA3
- Protein PSY1
- Hydroxyproline O-galactosyltransferase GALT6
- Hydroxyproline O-galactosyltransferase HPGT2
- Hydroxyproline O-galactosyltransferase GALT3
Sequence:
MGFRGKYFFPILMTLSLFLIIRYNYIVSDDPPLRQELPGRRSASSGDDITYTVKTPSKKTKRLFHTAVTATDSVYSTWQCRVMYYWYNRFRDEPGSDMGGYTRILHSGRPDGLMDEIPTFVADPLPSGVDKGYVVLNRPWAFVQWLQQAHIEEDYILMAEPDHIIVKPIPNLARGNLAAAFPFFYIEPKKYESVLRKFFPKENGPISRIDPIGNSPVIVTKNALMKIAPTWMNVSLAMKNDPQTDKAFGWVLEMYAYAVSSALHGVSNILHKDFMIQPPWDTETKKTFIIHYTYGCDFDMKGKMMVGKIGEWRFDKRSYGDKPPPRNLTLPPRGVPESVVTLVTMINEATANIPNWES
Protein: Cytotoxic granule-associated RNA binding protein tiar-1 (TIA1/TIAL RNA-binding protein homolog) (Q95QV8)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:26865701, ECO:0000269|PubMed:32432401, ECO:0000269|PubMed:34661238}. Nucleus {ECO:0000269|PubMed:23913578, ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:26865701, ECO:0000269|PubMed:34661238}. Cytoplasm, Stress granule {ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:26865701, ECO:0000269|PubMed:32432401, ECO:0000269|PubMed:34661238, ECO:0000269|PubMed:38161334}. Note=Diffusely cytoplasmic but localizes to stress granules in response to stress (PubMed:25061667, PubMed:26865701). Also detected in the nucleus (PubMed:25061667, PubMed:26865701). Heat shock stress granules are larger and more abundant than those caused by starvation (PubMed:26865701). Gonad stress granules form before, and dissociate after, those in the oocytes (PubMed:26865701). Pretreatment at 24 degrees Celsius results in smaller gonad stress granules and does not affect those formed in the oocytes (PubMed:26865701). Located in stress granules in the intestine in response to heat shock, starvation and dietary restriction (PubMed:32432401). Requires gtbp-1 and hsf-1 to localize to stress granules (PubMed:32432401). {ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:26865701, ECO:0000269|PubMed:32432401}.
Interaction partners:
- Ras GTPase-activating protein-binding protein gtbp-1
- ATP-dependent RNA helicase cgh-1
- m7GpppN-mRNA hydrolase dcap-2
- MADF domain-containing protein
- DRBM domain-containing protein
Sequence:
MSFFNPPANSNHGYNDDVNTGYNARMHSKLAEREGFHLGNGSDEPRTLYVGNLDSTVTEDFIATLFNQIGSVTKTKVIFDGSNDPYAFVEFSDHGQASQALQTMNKRLLLDREMKVNWAVEPGQQQSKIDTTRHFHVFVGDLSSEVDNQKLREAFQPFGDVSDAKVIRDTNTTKSKGYGFVSYPKREEAERAIEQMNGQWLGRRTIRTNWATRKPGDQEKPSHYNEKSYDEIYNQTSGDNTSVYVGNIASLTEDEIRQGFASFGRITEVRIFKMQGYAFVKFDNKDAAAKAIVQMNNQDVGGQLVRCSWGKTGDTGKTPGGSYGYGYGNSSSGGNSQPYSGYGGGGAYGGGQGGGGHGGPGQQQSNANSQYWQYYAQYYNNPQLMQQWSNYWQQQGGAPQQQNSGGHQ
Protein: Receptor expression-enhancing protein 6 (Q66IF1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required correct function and survival of retinal photoreceptors. Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a role in clathrin-coated intracellular vesicle trafficking of proteins from the endoplasmic reticulum to the retinal rod plasma membrane (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9JM62}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q9JM62}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ankyrin repeat domain 33Bb.
- Atlastin-1
- Reticulon
- Reticulon
Sequence:
MFAIFTKIKDRVEAFLNEKNIVTDCLNKIEEKTGIKKRYLAYGAAGVTGAFLLLGYGASLICNLIGFVYPAYFSIKAIESPGKEDDTQWLTYWVIYGFFSVGEFFSDIFLHWFPFYYVCKCLFLLWCMAPVSWNGSQVLYRHVVRPFFLKHEAAVDGMVSNISVKAMSAAENVTREVLHTLVRNRTVGPAESEPRSLPSSAHTEPTVD
Protein: Zinc finger C3HC-type protein 1 (Nuclear-interacting partner of ALK) (hNIPA) (Nuclear-interacting partner of anaplastic lymphoma kinase) (Q86WB0)
Organism: Homo sapiens (Human)
Function: Essential component of a SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events.
Subcellular location: Nucleus {ECO:0000269|PubMed:12748172}. Nucleus envelope {ECO:0000269|PubMed:34440706}. Note=Resident of the nuclear basket (NB) (PubMed:34440706). Occurs at the nuclear envelopes (NE) of all TPR-containing cell types, including proliferating and non-dividing, terminally differentiated cells of different morphogenetic origin (PubMed:34440706). {ECO:0000269|PubMed:34440706}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- G2/mitotic-specific cyclin-B1
Sequence:
MAAPCEGQAFAVGVEKNWGAVVRSPEGTPQKIRQLIDEGIAPEEGGVDAKDTSATSQSVNGSPQAEQPSLESTSKEAFFSRVETFSSLKWAGKPFELSPLVCAKYGWVTVECDMLKCSSCQAFLCASLQPAFDFDRYKQRCAELKKALCTAHEKFCFWPDSPSPDRFGMLPLDEPAILVSEFLDRFQSLCHLDLQLPSLRPEDLKTMCLTEDKISLLLHLLEDELDHRTDERKTTIKLGSDIQVHVTACILSVCGWACSSSLESMQLSLITCSQCMRKVGLWGFQQIESSMTDLDASFGLTSSPIPGLEGRPERLPLVPESPRRMMTRSQDATFSPGSEQAEKSPGPIVSRTRSWDSSSPVDRPEPEAASPTTRTRPVTRSMGTGDTPGLEVPSSPLRKAKRARLCSSSSSDTSSRSFFDPTSQHRDWCPWVNITLGKESRENGGTEPDASAPAEPGWKAVLTILLAHKQSSQPAETDSMSLSEKSRKVFRIFRQWESLCSC
Protein: LH1 beta polypeptide (D2Z0P1)
Organism: Thermochromatium tepidum (Chromatium tepidum)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004249}.
Interaction partners:
Sequence:
MAEQKSLTGLTDDEAKEFHAIFMQSMYAWFGLVVIAHLLAWLYRPWL
Protein: Protein RDM16 (Pre-mRNA-splicing factor RDM16) (Protein RNA-directed DNA methylation 16) (Q9C7E7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in the RNA-directed DNA methylation (RdDM) pathway. Acts as a pre-mRNA splicing factor, likely by affecting Pol V transcripts. Affects DNA methylation of transposable elements (TEs) and preferentially influences NRPD1- and ROS1-targeted loci.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:24068953}.
Interaction partners:
- Nuclear protein-like
- U4/U6 small nuclear ribonucleoprotein Prp31 homolog
- Sm-like protein LSM5
- At2g32600/T26B15.16
- Protein STABILIZED1
- Sm-like protein LSM4
- Pre-mRNA-processing-splicing factor 8A
- Pre-mRNA-processing-splicing factor 8B
- Sm-like protein LSM8
- Peptidyl-prolyl cis-trans isomerase CYP22
Sequence:
MDKERYSRSHRDDRDRDSSPDHSPQREGGRRRDRDVDSKRRDSDHYRSSRRGDREDERDRTKDRRGRSVERGEREGSRDREKHHHERSHEGSKEKESRSKRKDREEENGARDGKKKSRFADGNGERRSRFEDVAIEVENKDAQVSEGSGATNPTSGVTMGASTYSSIPSEASAAPSQTLLTKVSSISTTDENKASVVRSHEVPGKSSTDGRPLSTAGKSSANLPLDSSALAAKARKALQLQKGLADRLKNLPLLKKATKPTSEGSPHTRVPPSTTTPAVSTGTSFASTLPHTGLAGFGSIANIEAVKRAQELAANMGFHQDREFAPVINLFPGQAPSDMTVAQRPEKPPVLRVDALGREIDEHGNVISVTKPSNLSTLKVNINKKKKDAFQILKPQLEADLKENPYFDTRMGIDEKKILRPKRMSFQFVEEGKWTRDAENLKFKSHFGEAKAKELKVKQAQLAKANDDINPNLIEVSERVPRKEKPKEPIPDVEWWDANVLTNGEYGEITDGTITESHLKIEKLTHYIEHPRPIEPPAEAAPPPPQPLKLTKKEQKKLRTQRRLAKEKEKQEMIRQGLLEPPKAKVKMSNLMKVLGSEATQDPTKLEKEIRTAAAEREQAHTDRNAARKLTPAEKREKKERKLFDDPTTVETIVSVYKIKKLSHPKTRFKVEMNARENRLTGCSVMTDEMSVVVVEGKSKAIKRYGKLMMKRINWEEAERKEGNEDEEEEVNGGNKCWLVWQGSIGKPSFHRFHVHECVTESTAKKVFMDAGVVHYWDLAVNYSDD
Protein: Defective pharyngeal development protein 4 (Ce-fkh-1) (Fork head-HNF-3 homolog) (Q17381)
Organism: Caenorhabditis elegans
Function: Acts as a transcription factor required for formation of the pharyngeal primordium. Binds to the consensus sequence 5'-T[AG]TT[TG][AG][TC]-3' with variations of the sequence affecting onset of target gene expression. Becomes associated with pharyngeal target promoters by the 8E cell stage, playing a role in inducing large-scale chromatin decompaction, prior to the activation of transcription. Binding with target sequences in pharyngeal cells may be repressed by the nuclear lamina protein emr-1. Activates a wide array of pharyngeal genes including ceh-22, pax-1 and myo-2 and represses ectodermal genes lin-26 and elt-3, ensuring pharyngeal cell fate. Required for recruitment of htz-1 to a subset of pharyngeal promoters to ensure gene activation and also acts synergistically with tbx-2 in pharyngeal development. Acts in the regulation of diet-restriction-mediated longevity by increasing expression of sod-1, sod-2, sod-4 and sod-5 but not sod-3. Positively regulates the expression of the transcription factor hlh-6 in the pharyngeal gland. May regulate gene expression in the intestine.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:17476212, ECO:0000269|PubMed:9584117, ECO:0000269|PubMed:9649499}. Note=Present in nuclei of all cells of larval and adult pharynx but variable in neuronal nuclei. {ECO:0000269|PubMed:17476212, ECO:0000269|PubMed:9584117, ECO:0000269|PubMed:9649499}.
Interaction partners:
- Ribosomal protein S6 kinase beta
- Protein skinhead-1
- Non-specific serine/threonine protein kinase
- Transcription factor elt-2
- Transcription factor elt-3
- Homeobox protein ceh-22
- Nuclear hormone receptor family member daf-12
- Transcription factor elt-7
- Helix-loop-helix protein 30
- Insulin-like receptor
Sequence:
MTSPSSDEDIIDIRVIKEEPESEPDSEAEPATTTNSTDSEDSVEQENKKLLETEKNRKREQKHKMLPNGTTSGTSDTGNQVPATSSAASSVDYTAMNAQDYLPTYSNTTLNYQPYQYQTAANGLLNYNNYSQYATANQLGSNYISPANFMQGGGISPLGFTTGTTGATTAAASVATSSASAVIGRSNGRSSSTVAASPADRSYSGVSGGQGQELTIQEFETVTEKIRRHGTYGQSKPPYSYISLITMAIQKSNSRQLTLSEIYNWIMDLFPYYQNNQQRWQNSIRHSLSFNDCFVKVARSPDKPGKGSFWTLHEHCGNMFENGCYLRRQKRFKVKEREPSRKKRNANSQQLHQQQHIPKMEIKEEDPTSITTTSSLGAYSLIPQISTKKEIKEELKAVQDATAAAANLGLIDPSGTPSAVNHSQPTSVISSVGTLGTTQAQMTLNGQYASPYLYSSDFATILPQSQNFLNNTLYNTTSSYPGIDYTNGVYQNTLYSSTNPNSAANL
Protein: Leucine aminopeptidase 2, chloroplastic (EC 3.4.11.1) (Leucyl aminopeptidase 2) (AtLAP2) (Proline aminopeptidase 2) (EC 3.4.11.5) (Prolyl aminopeptidase 2) (Q944P7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Does not seem to possess Cys-Gly dipeptidase activity.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Puromycin-sensitive aminopeptidase
- Glutathione hydrolase 2
- Glutathione hydrolase 1
- Glutathione hydrolase 3
- Putative inactive glutathione hydrolase 4
- Glutathione synthetase, chloroplastic
- Leucine aminopeptidase 1
- Glutamate--cysteine ligase, chloroplastic
- Leucine aminopeptidase 3, chloroplastic
- Gamma-glutamylcyclotransferase 2-3
Sequence:
MAVTLVTSFASSSSRFHFRSFSSSPSSLSSCFVRFQFPSRLRLAFAVTPLYSSSRAMAHTISHATLGLTQANSVDHPKISFSGKEIDVTEWKGDILAVGVTEKDMAKDVNSKFENPILKKLDAHLGGLLADVSSEEDFSGKPGQSTVLRLPGLGSKRVGLIGLGKSASTPSAFQSLGEAVAAAAKASQASSVAVVLASSESVSNESKLCSASAIASGTVLGLFEDSRYKSESKKPSLKSVDIIGFGSGPELEKKLKYAEHVSYGVIFGKELVNSPANVLTPAVLAEEALNLASMYSDVMTANILNEEQCKELKMGSYLAVAAASANPPHFIHLIYKPSSGPVKTKLALVGKGLTFDSGGYNIKTGPGCLIELMKFDMGGSAAVLGAAKAIGQIKPPGVEVHFIVAACENMISGTGMRPGDVLTASNGKTIEVNNTDAEGRLTLADALVYACNQGVDKVVDLATLTGACIIALGTSMAGIYTPSDKLAKEVIAASERSGEKLWRMPMEESYWEMMKSGVADMVNTGGRAGGSITAALFLKQFVSEDVEWMHIDMAGPVWNEKKKAATGFGVATLVEWVQNHSSS
Protein: BcDNA.GH07312 (Metabotropic GABA-B receptor subtype 2, isoform B) (Q9Y133)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MFRPSWFPFASLLFLLLWSTACGRTAKRSDVYIAGFFPYGDGVENSYTGRGVMPSVKLALGHVNEHGKILANYRLHMWWNDTQCNAAVGVKSFFDMMHSGPNKVMLFGAACTHVTDPIAKASKHWHLTQLSYADTHPMFTKDAFPNFFRVVPSENAFNAPRLALLKEFNWTRVGTVYQNEPRYSLPHNHMVADLDAMEVEVVETQSFVNDVAESLKKLREKDVRIILGNFNEHFARKAFCEAYKLDMYGRAYQWLIMATYSTDWWNVTQDSECSVEEIATALEGAILVDLLPLSTSGDITVAGITADEYLVEYDRLRGTEYSRFHGYTYDGIWAAALAIQYVAEKREDLLTHFDYRVKDWESVFLEALRNTSFEGVTGPVRFYNNERKANILINQFQLGQMEKIGEYHSQKSHLDLSLGKPVKWVGKTPPKDRTLIYIEHSQVNPTIYIVSASASVIGVIIATVFLAFNIKYRNQRYIKMSSPHLNNLIIVGCMMTYLSIIFLGLDTTLSSVAAFPYICTARAWILMAGFSLSFGAMFSKTWRVHSIFTDLKLNKKVIKDYQLFMVVGVLLAIDIAIITTWQIADPFYRETKQLEPLHHENIDDVLVIPENEYCQSEHMTIFVSIIYAYKGLLLVFGAFLAWETRHVSIPALNDSKHIGFSVYNVFITCLAGAAISLVLSDRKDLVFVLLSFFIIFCTTATLCLVFVPKLVELKRNPQGVVDKRVRATLRPMSKNGRRDSSVCELEQRLRDVKNTNCRFRKALMEKENELQALIRKLGPEARKWIDGVTCTGGSNVGSELEPILNDDIVRLSAPPVRREMPSTTEVTEMTSVDSVTSTHVEMDNSFVSVQSTVMAPSLPPKKKKQSIVEHHSHAPAPTMMQPIQQQLQQHLQQHQQMQQQHLQQQQHQQMQQQQQQQQHHHRHLEKRNSVSAQTDDNIGSITSTAGKRSGGDCSSMRERRQSTASRHYDSGSQTPTARPKYSSSHRNSSTNISTSQSELSNMCPHSKPSTPAVIKTPTASDHRRTSMGSALKSNFVVSQSDLWDTHTLSHAKQRQSPRNYASPQRCAEHHGGHGMTYDPNTTSPIQRSVSEKNRNKHRPKPQKGTVCQSETDSERERDPPPNSQPCVQPRKVSRSSNIQHAAHHHSSPNVAPDKQRSRQRGKQDSSIYGASSETELLEGETAILPIFRKLLTEKSPNYRGRSAVGQSCPNISIKCDIVEYL
Protein: dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase (EC 4.3.1.30) (dTDP-D-quinovose dehydrogenase) (dTDP-D-quinovose:S-adenosyl-L-methionine 1-oxidoreductase) (EC 1.1.99.-) (Q9ZGH1)
Organism: Streptomyces venezuelae
Function: Involved in the biosynthesis of dTDP-alpha-D-desosamine, a sugar found in several bacterial macrolide antibiotics. Catalyzes the SAM-dependent deamination of dTDP-4-amino-4,6-deoxyglucose (dTDP-viosamine) to yield dTDP-3-keto-4,6-deoxyglucose. It can also catalyze the oxidative dehydrogenation of the non-physiological substrate dTDP-D-quinovose to dTDP-3-keto-6-deoxy-d-glucose. It can also deaminate dTDP-3-amino-3,6-deoxyglucose.
Interaction partners:
Sequence:
MTAPALSATAPAERCAHPGADLGAAVHAVGQTLAAGGLVPPDEAGTTARHLVRLAVRYGNSPFTPLEEARHDLGVDRDAFRRLLALFGQVPELRTAVETGPAGAYWKNTLLPLEQRGVFDAALARKPVFPYSVGLYPGPTCMFRCHFCVRVTGARYDPSALDAGNAMFRSVIDEIPAGNPSAMYFSGGLEPLTNPGLGSLAAHATDHGLRPTVYTNSFALTERTLERQPGLWGLHAIRTSLYGLNDEEYEQTTGKKAAFRRVRENLRRFQQLRAERESPINLGFAYIVLPGRASRLLDLVDFIADLNDAGQGRTIDFVNIREDYSGRDDGKLPQEERAELQEALNAFEERVRERTPGLHIDYGYALNSLRTGADAELLRIKPATMRPTAHPQVAVQVDLLGDVYLYREAGFPDLDGATRYIAGRVTPDTSLTEVVRDFVERGGEVAAVDGDEYFMDGFDQVVTARLNQLERDAADGWEEARGFLR
Protein: Capsid protein (CP) (Coat protein) (P03630)
Organism: Pseudomonas phage PP7 (Bacteriophage PP7)
Function: Forms the phage shell; binds to the phage RNA.
Subcellular location: Virion {ECO:0000269|PubMed:109813}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000250|UniProtKB:P03612}.
Interaction partners:
Sequence:
MSKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCSTSVCGELPKVRYTQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR