wanglab/gogpt-training-data huggingface dataset:
Protein: BTB/POZ domain-containing protein 3 (Q9Y2F9)
Organism: Homo sapiens (Human)
Function: Acts as a key regulator of dendritic field orientation during development of sensory cortex. Also directs dendrites toward active axon terminals when ectopically expressed (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from the cytosol to the nucleus in response to neuronal activity. {ECO:0000250}.
Interaction partners:
Sequence:
MVDDKEKNMKCLTFFLMLPETVKNRSKKSSKKANTSSSSSNSSKLPPVCYEIITLKTKKKKMAADIFPRKKPANSSSTSVQQYHQQNLSNNNLIPAPNWQGLYPTIRERNAMMFNNDLMADVHFVVGPPGGTQRLPGHKYVLAVGSSVFHAMFYGELAEDKDEIRIPDVEPAAFLAMLKYIYCDEIDLAADTVLATLYAAKKYIVPHLARACVNFLETSLSAKNACVLLSQSCLFEEPDLTQRCWEVIDAQAELALKSEGFCDIDFQTLESILRRETLNAKEIVVFEAALNWAEVECQRQDLALSIENKRKVLGKALYLIRIPTMALDDFANGAAQSGVLTLNETNDIFLWYTAAKKPELQFVSKARKGLVPQRCHRFQSCAYRSNQWRYRGRCDSIQFAVDKRVFIAGFGLYGSSCGSAEYSAKIELKRQGVVLGQNLSKYFSDGSSNTFPVWFEYPVQIEPDTFYTASVILDGNELSYFGQEGMTEVQCGKVTVQFQCSSDSTNGTGVQGGQIPELIFYA
Protein: Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc)) (Q9QZ82)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Adrenodoxin, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6
- Steroidogenic acute regulatory protein, mitochondrial
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Steroid 21-hydroxylase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cytochrome P450 7B1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3
Sequence:
MLAKGLSLRSVLVKGCQPFLSPTWQGPVLSTGKGAGTSTSSPRSFNEIPSPGDNGWLNLYHFWRESGTQKIHYHQMQSFQKYGPIYREKLGTLESVYIVDPKDASILFSCEGPNPERFLVPPWVAYHQYYQRPIGVLFKSSDAWKKDRIVLNQEVMAPGAIKNFVPLLEGVAQDFIKVLHRRIKQQNSGNFSGVISDDLFRFSFESISSVIFGERMGMLEEIVDPEAQRFINAVYQMFHTSVPMLNLPPDFFRLLRTKTWKDHAAAWDVIFNKADEYTQNFYWDLRQKRDFSQYPGVLYSLLGGNKLPFKNIQANITEMLAGGVDTTSMTLQWNLYEMAHNLKVQEMLRAEVLAARRQAQGDMAKMVQLVPLLKASIKETLRLHPISVTLQRYTVNDLVLRNYKIPAKTLVQVASFAMGRDPGFFPNPNKFDPTRWLEKSQNTTHFRYLGFGWGVRQCLGRRIAELEMTILLINLLENFRIEVQNLRDVGTKFSLILMPENPILFNFQPLKQDLGPAVTRKDNTVN
Protein: Triosephosphate isomerase 2 (TIM 2) (TPI 2) (EC 5.3.1.1) (Triose-phosphate isomerase 2) (Q92EU4)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Function: Involved in the glycerol metabolism. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22773791}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate kinase
- Transketolase
- Probable transaldolase 2
- Ribose-5-P isomerase B
- Rhamnulose-1-phosphate aldolase
- NAD-dependent glycerol dehydrogenase
- Lin2239 protein
- Lin0378 protein
- Lin2238 protein
Sequence:
MRKPLVGINMKNYINTRAQTSEWLEATIPLLENFSDVDTFIFPSMGTLETTANLLAGTSFGFGPQNMAPEKSGPLTGEFSVESIIDLNANYVEIGHAERKNLFHEKTSEIAKKIKLALDEKITPVVCVGEEVHANDTNELKNALKKQIEALFQTINLAQWENVVLAYEPEWAIGKASSAETNYIESAHQALREIIRELGGDETLVRIIYGGSVSKENAAEIVRQKNVDGLFVGRFGHKPQNFADIVSIVSKTKG
Protein: Paired-like homeobox 2b (A0A0G2JYE6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Tyrosine 3-monooxygenase
- Dopamine beta-hydroxylase
- Heart- and neural crest derivatives-expressed protein 2
- Transcription factor SOX-10
- Insulin gene enhancer protein ISL-1
Sequence:
MYKMEYSYLNSSAYESCMAGMDTSSLASAYADFSSCSQASGFQYNPIRTTFGATSGCPSLTPGSCSLGTLRDHQSSPYAAVPYKLFTDHGGLNEKRKQRRIRTTFTSAQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAAAAAAAAAKNGSSGKKSDSSRDDESKEAKSTDPDSTGGPGPNPNPTPSCGANGGGGGGPSPAGAPGAAGPGGPGGEPGKGGAAAAAAAAAAAAAAAAAAAAGGLAAAGGPGQGWAPGPGPITSIPDSLGGPFASVLSSLQRPNGAKAALVKSSMF
Protein: Glutaryl-CoA dehydrogenase, mitochondrial (GCD) (EC 1.3.8.6) (Q60759)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- 2-oxoadipate dehydrogenase complex component E1
- Dihydrolipoyl dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MSLRGVSARLLSRRSGLRFPRFPRTWSSAAAHTEKTQIRPAKSSRPVFDWKDPLILEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTVGK
Protein: ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1 (A0A8I5ZSU8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYVFPVYRLPNEKEIVQGVLAQRTAWRRNQTSARLFSRRLVPVDPGCVVC
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (Q2LIP5)
Organism: Oryza glumipatula
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
RVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRTASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPTDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFACGNGNAKYEILFLEIWTNGSLTPMEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: ADP-ribosylation factor 1 (EC 3.6.5.2) (P61209)
Organism: Drosophila melanogaster (Fruit fly)
Function: Small GTPase involved in protein trafficking between different compartments. Modulates vesicle budding and uncoating within the Golgi complex. In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Has a role in eye development. Required for cleavage furrow ingression in embryonic cells.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:27535433}; Lipid-anchor {ECO:0000250|UniProtKB:P84077}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:27535433}. Note=In the GDP-bound form, associates transiently with the membranes via its myristoylated N-terminus where guanine nucleotide-exchange factor (GEF)-mediated nucleotide exchange occurs (By similarity). Following nucleotide exchange, the GTP-bound form undergoes a conformational change, leading to the exposure of a myristoylated N-terminal amphipathic helix that provides stable membrane anchorage (By similarity). Localization to the Golgi is dependent on Asap (PubMed:27535433). {ECO:0000250|UniProtKB:P84080, ECO:0000269|PubMed:27535433}.
Interaction partners:
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Golgi microtubule-associated protein, isoform D
- ADP-ribosylation factor GTPase-activating protein 1
- AP-1 complex subunit gamma
- Coatomer subunit gamma
- Coatomer subunit beta
- ADP ribosylation factor 4
- ADP-ribosylation factor 6
- Phosphatidylinositol 4-kinase beta
- Inositol phosphatase interacting protein, isoform A
Sequence:
MGNVFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIGEAREELMRMLAEDELRDAVLLIFANKQDLPNAMNAAEITDKLGLHSLRNRNWYIQATCATSGDGLYEGLDWLSNQLKNANR
Protein: Homeobox and leucine zipper protein Homez (Homeodomain leucine zipper-containing factor) (Q8IX15)
Organism: Homo sapiens (Human)
Function: May function as a transcriptional regulator.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12925734}.
Interaction partners:
- Homeobox protein Hox-C8
Sequence:
MVRGWEPPPGLDCAISEGHKSEGTMPPNKEASGLSSSPAGLICLPPISEELQLVWTQAAQTSELDSNEHLLKTFSYFPYPSLADIALLCLRYGLQMEKVKTWFMAQRLRCGISWSSEEIEETRARVVYRRDQLHFKSLLSFTHHAGRPPEEVPPPPVPAPEQVGIGIGPPTLSKPTQTKGLKVEPEEPSQMPPLPQSHQKLKESLMTPGSGAFPYQSDFWQHLQSSGLSKEQAGRGPNQSHGIGTASWNHSTTVPQPQARDKPPPIALIASSCKEESASSVTPSSSSTSSSFQVLANGATAASKPLQPLGCVPQSVSPSEQALPPHLEPAWPQGLRHNSVPGRVGPTEYLSPDMQRQRKTKRKTKEQLAILKSFFLQCQWARREDYQKLEQITGLPRPEIIQWFGDTRYALKHGQLKWFRDNAVPGAPSFQDPAIPTPPPSTRSLNERAETPPLPIPPPPPDIQPLERYWAAHQQLRETDIPQLSQASRLSTQQVLDWFDSRLPQPAEVVVCLDEEEEEEEEELPEDDEEEEEEEEEDDDDDDDDVIIQD
Protein: Xaa-Pro aminopeptidase 3 (X-Pro aminopeptidase 3) (EC 3.4.11.9) (Aminopeptidase P3) (APP3) (B7ZMP1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B-mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9NQH7}. Cytoplasm {ECO:0000250|UniProtKB:Q9NQH7}. Note=Mainly mitochondrial. Translocates to the cytoplasm following TNFRSF1B activation. {ECO:0000250|UniProtKB:Q9NQH7}.
Interaction partners:
- Mitochondrial-processing peptidase subunit alpha
- Mitochondrial intermediate peptidase
- Mitochondrial-processing peptidase subunit beta
Sequence:
MPSLLSTPKLAPVLARLRGLSGCMSCLQRRYSLQPAPVKKIPNRYLGQPSPVTHPHLLRPGEVTPGLSQVEYALRRHKLMALVHKEAQGHSGTDHTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCGFQEPDSILVLQSFSGKQLPSHKAMLFVPRRDPGRELWDGPRSGTDGAIALTGVDEAYPLEEFQHLLPKLRAETNMVWYDWMKPSHAQLHSDYMQPLTEAKARSKNKVRSVQQLIQRLRLVKSPSEIKRMQIAGKLTSEAFIETMFASKAPIDEAFLYAKFEFECRARGADILAYPPVVAGGNRSNTLHYVKNNQLIKDGEMVLLDGGCESSCYVSDITRTWPVNGRFTAPQAELYEAVLEIQRACLTLCSPGTSLENIYSMMLTLIGQKLKDLGITKTSKESAFKAARKYCPHHVGHYLGMDVHDTPDMPRSLPLQPGMVITVEPGIYIPEDDRDAPEKFRGLGVRIEDDVVVTQDSPLILSADCPKEMNDIEQICSRTS
Protein: Phosphate-specific transport system accessory protein PhoU homolog 2 (Pst system accessory protein PhoU homolog 2) (P9WI95)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoP or a PhoR-PhoP complex to promote dephosphorylation of phospho-PhoP, or inhibit formation of the PhoR-PhoP transitory complex (By similarity). Important for tolerance to antibiotics.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphate import ATP-binding protein PstB 2
- Phosphate transport system permease protein PstA 1
- Phosphate import ATP-binding protein PstB 1
- Phosphate transport system permease protein PstA 2
- Phosphate transport system permease protein PstC 1
- Phosphate transport system permease protein PstC 2
- Probable conserved ATP-binding protein ABC transporter
- Antitoxin VapB47
- Hypoxic response protein 1
Sequence:
MRTAYHEQLSELSERLGEMCGLAGIAMERATQALLQADLVLAEQVISDHEKIATLSARAEESAFVLLALQAPVAGDLRAIVSAIQMVADIDRMGALALHVAKIARRRHPQHALPEEVNGYFAEMGRVAVELGNSAQEVVLSHDPEKAAQIREEDDAMDDLHRHLFTVLMDREWKHGVAAAVDVTLLSRFYERFADHAVEVARRVIFQATGAFP
Protein: Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial (EC 6.1.1.24) (Glutamate--tRNA(Gln) ligase EARS2, mitochondrial) (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) (Mitochondrial glutamyl-tRNA synthetase) (mtGluRS) (Q5JPH6)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:19805282}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Methionine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, mitochondrial
- Glutamyl-tRNA
- Probable proline--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, mitochondrial
- Lysine--tRNA ligase
Sequence:
MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS
Protein: Major capsid protein (Gene product E) (gpE) (Major head protein) (P03713)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Assembles to form an icosahedral capsid with a T=7 symmetry. The icosahedral capsid is about 60 nm in diameter and composed of 415 major capsid proteins. The assembly is primed by the interaction between capsid assembly protease and portal dodecamer, and major capsid proteins assemble cooperatively to form the procapsid with the help of capsid scaffolding protein. Major capsid protein forms hexons and pentons of the icosahedron. Viral genomic DNA is packaged into the procapsid through the portal vertex (By similarity). The packaging triggers a dramatic reconfiguration of the capsid shell, expanding from roughly 50nm to 60nm while the capsid thickness decreases. The capsid decoration protein binds the expanded capsid and stabilizes it.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04133, ECO:0000269|PubMed:265585}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04133, ECO:0000269|PubMed:265585}. Note=Forms the capsid icosahedric shell. {ECO:0000255|HAMAP-Rule:MF_04133, ECO:0000269|PubMed:265585}.
Interaction partners:
Sequence:
MSMYTTAQLLAANEQKFKFDPLFLRLFFRESYPFTTEKVYLSQIPGLVNMALYVSPIVSGEVIRSRGGSTSEFTPGYVKPKHEVNPQMTLRRLPDEDPQNLADPAYRRRRIIMQNMRDEELAIAQVEEMQAVSAVLKGKYTMTGEAFDPVEVDMGRSEENNITQSGGTEWSKRDKSTYDPTDDIEAYALNASGVVNIIVFDPKGWALFRSFKAVKEKLDTRRGSNSELETAVKDLGKAVSYKGMYGDVAIVVYSGQYVENGVKKNFLPDNTMVLGNTQARGLRTYGCIQDADAQREGINASARYPKNWVTTGDPAREFTMIQSAPLMLLADPDEFVSVQLA
Protein: Homeobox protein aristaless-like 4 (ALX-4) (O35137)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in skull and limb development.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRGFPGGDKFGTTFLSAGAKGQGFGDAKSRARYGAGQQDLAAPLESSSGARGSFNKFQPQPPTPQPPPAPPAPPAHLYLQRGACKTPPDGSLKLQEGSGGHNAALQVPCYAKESNLGEPELPPDSEPVGMDNSYLSVKETGAKGPQDRASAEIPSPLEKTDSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWIGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVSDFLSVSGAGSHVGQTHMGSLFGAAGISPGLNGYEMNGEPDRKTSSIAALRMKAKEHSAAISWAT
Protein: Serine racemase (AtSR) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17) (Q2PGG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine. Displays high substrate specificity for L-serine, whereas L-alanine, L-arginine, and L-glutamine were poor substrates.
Interaction partners:
- Serine hydroxymethyltransferase 4
- Serine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase 3, chloroplastic
- Serine hydroxymethyltransferase 7
- Serine hydroxymethyltransferase 2, mitochondrial
- Serine hydroxymethyltransferase 6
- Serine hydroxymethyltransferase 1, mitochondrial
- Serine hydroxymethyltransferase 5
- Tryptophan synthase
- Phosphoserine phosphatase, chloroplastic
Sequence:
MEANREKYAADILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRASLGDLTWPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPSCRDCKNIGIVLSGGNVDLGSLWDSFKSSK
Protein: Four and a half LIM domains 1 (A0A0D9SFI6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGED
Protein: U6 snRNA-associated Sm-like protein LSm2 (Small nuclear ribonucleoprotein D homolog SNP3) (P38203)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Subcellular location: Nucleus. Cytoplasm {ECO:0000305}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein G
- U4/U6 small nuclear ribonucleoprotein PRP3
- U4/U6 snRNA-associated-splicing factor PRP24
- LSM complex subunit LSM3
- Pre-mRNA-splicing factor 8
- U4/U6 small nuclear ribonucleoprotein PRP4
- LSM complex subunit LSM5
- Small nuclear ribonucleoprotein-associated protein B
- LSM complex subunit LSM6
Sequence:
MLFFSFFKTLVDQEVVVELKNDIEIKGTLQSVDQFLNLKLDNISCTDEKKYPHLGSVRNIFIRGSTVRYVYLNKNMVDTNLLQDATRREVMTERK
Protein: Apelin receptor 2 (Apelin receptor 3) (F1QJG4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Apelin
- Apelin receptor early endogenous ligand
- Apelin receptor A
- Apelin receptor B
- Adenylate cyclase-inhibiting G alpha protein
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MSGSLPFPSPSPFPSCDYTEWSPTWVLIPSVYLLVFVVGSLGNGLVLWVYLDRQARGRGRIGSGSKSSQTPDSPPCPSPTSTRTVTESLIISLALADLAFVMTLPLWAAYTALGYHWPFGQVLCQTSSYIVALNMYASVFSLTGLSVERYCVITRQRGNGSKQRTSSTRARWIVGIVWLAAGVLALPALLLRTVREPDLESGDDGDWQAGQSSSCLCDMDYSSLISSDLDPAEAEQAELMWSAALGLKSTLLGFLLPLVVLLVCYGWLGRLLSRHFSLGLRPDQKRQRRLLRIIITLVLAFFLCWLPFHTNKTLSAMVELGILPFSCRFDQWLVAAHPYSICLGYVNSCLNPLLYACCDPAFRKRCSGLLLCLWVKCKGQRAEEEKQQHQSSAVPSGTHEVTVSKDEQ
Protein: WD repeat-containing protein 82 (Q8BFQ4)
Organism: Mus musculus (Mouse)
Function: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes (By similarity). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (By similarity). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6UXN9}. Chromosome {ECO:0000269|PubMed:33767452}. Note=Associates with chromatin (By similarity). Recruited at sites of high RNA polymerase II occupancy (PubMed:33767452). {ECO:0000250|UniProtKB:Q6UXN9, ECO:0000269|PubMed:33767452}.
Interaction partners:
- CXXC-type zinc finger protein 1
- Histone-lysine N-methyltransferase SETD1B
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- Retinoblastoma-binding protein 5
- Symplekin
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Histone-lysine N-methyltransferase SETD1A
Sequence:
MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD