wanglab/gogpt-training-data huggingface dataset:
Protein: Protein EVI2B (Ecotropic viral integration site 2B protein homolog) (EVI-2B) (CD antigen CD361) (P34910)
Organism: Homo sapiens (Human)
Function: Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Protein EVI2A
- Oligodendrocyte-myelin glycoprotein
- E3 ubiquitin-protein ligase RNF135
- Neurofibromin
- Lysosomal-associated transmembrane protein 5
- Cytohesin-interacting protein
- Arf-GAP with dual PH domain-containing protein 2
- Leukocyte surface antigen CD53
Sequence:
MDPKYFILILFCGHLNNTFFSKTETITTEKQSQPTLFTSSMSQVLANSQNTTGNPLGQPTQFSDTFSGQSISPAKVTAGQPTPAVYTSSEKPEAHTSAGQPLAYNTKQPTPIANTSSQQAVFTSARQLPSARTSTTQPPKSFVYTFTQQSSSVQIPSRKQITVHNPSTQPTSTVKNSPRSTPGFILDTTSNKQTPQKNNYNSIAAILIGVLLTSMLVAIIIIVLWKCLRKPVLNDQNWAGRSPFADGETPDICMDNIRENEISTKRTSIISLTPWKPSKSTLLADDLEIKLFESSENIEDSNNPKTEKIKDQVNGTSEDSADGSTVGTAVSSSDDADLPPPPPLLDLEGQESNQSDKPTMTIVSPLPNDSTSLPPSLDCLNQDCGDHKSEIIQSFPPLDSLNLPLPPVDFMKNQEDSNLEIQCQEFSIPPNSDQDLNESLPPPPAELL
Protein: ATP-dependent RNA helicase DDX60 PIN-like domain-containing protein (Q8CB98)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEKKYTGFLKIMSHLILETMSKADYSSLFNDFVESEFFLIDGDSLLITCACERSLKPGQSLHFFYLVERYLLDVISKGGQFAIVFFKDAEYAYFNVPELLTLRTALILHLQKNTTVEVWTKFSNCLSEEWNICLGQSCPYFLILADEGLNDLQTHLFNFVVIQAWAAKVNIVLFSGQTSDILRLYAYFMQSSHGMQMFFKENKRMIMIVYKSLIQQLEKYRDMALAHLFGDLKFNDMEEKVCETVSLLKQLWPEGSDIRCVFCVTSCSLFLEMYHCYLESREKGASEEMSKVKQKTDNCLTLKDMEDFCKLHCLSVALLLHVPLSQRARSRFITANWIQDLKTVLKMKKWCEYFILSNLDMFESWSLNLLHLSDLSDEPLLRNIAFYYENENKEGLDLNVGDAIMNEYVHLWDTVSKLVRKFDVGKPIPLRTTKVHFLEKTPSPIKESSQEMMPNLGFIPMSCNLVDEFTGDILKDLPFLMSDDPIVTSLVKHKEFDELVHWHSHRPLSDDYDRTKVNSGDRRDPNHLKRLQKYHSFQRFYGESLESVTSKTITTQGPKPKKDCIKSKSTKAHETKAE
Protein: Olfactory receptor (A2BHP6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MILSEKNNSGIIFTLLVFSDYPDLKVPLFLVFLVIYSITVVGNIGMILVIRINPQLHSPMYFFLSHLSFVDFCYSSIIAPKMLVNLVAKDITISFVECIVQYFLFCVFVVTEAFLLVVMAYDRFVAICNPLLYTVAMSQKLCITLVVGSYAWGFTCSLTLTCSTVQLSFHGVNRIDHFFCELSSLLALSSSDTLISQLLLFVFATFNAVSTLLLILLSYLFIVVTVLKMRSASGRRKAFSTCASHLAAITIFHGTILFLFCVPNSKNSRLTVKVGSVFYTVVIPMLNPIIYSLRNKDVQDTIRKIMTLISCVKNDRHN
Protein: Alpha-basrubrin (P83186)
Organism: Basella alba (Malabar spinach) (Basella rubra)
Function: Possesses antifungal activity against B.cinerea, M.arachidicola and F.oxysporum but not C.comatus and R.solani. Inhibits HIV-1 reverse transcriptase and cell-free translation.
Interaction partners:
Sequence:
GADFQECMKEHSQKQHQHQG
Protein: Regulator of telomere elongation helicase 1 (EC 5.6.2.-) (Novel helicase-like) (Q9NZ71)
Organism: Homo sapiens (Human)
Function: ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:23585563}. Note=Colocalizes with PCNA within the replication foci in S-phase cells. {ECO:0000255|HAMAP-Rule:MF_03065}.
Interaction partners:
- MMS19 nucleotide excision repair protein homolog
- Structure-specific endonuclease subunit SLX4
- Telomeric repeat-binding factor 1
- TERF1-interacting nuclear factor 2
- Telomerase reverse transcriptase
- Telomerase Cajal body protein 1
- Cytosolic iron-sulfur assembly component 2B
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit DKC1
- CST complex subunit CTC1
Sequence:
MPKIVLNGVTVDFPFQPYKCQQEYMTKVLECLQQKVNGILESPTGTGKTLCLLCTTLAWREHLRDGISARKIAERAQGELFPDRALSSWGNAAAAAGDPIACYTDIPKIIYASRTHSQLTQVINELRNTSYRPKVCVLGSREQLCIHPEVKKQESNHLQIHLCRKKVASRSCHFYNNVEEKSLEQELASPILDIEDLVKSGSKHRVCPYYLSRNLKQQADIIFMPYNYLLDAKSRRAHNIDLKGTVVIFDEAHNVEKMCEESASFDLTPHDLASGLDVIDQVLEEQTKAAQQGEPHPEFSADSPSPGLNMELEDIAKLKMILLRLEGAIDAVELPGDDSGVTKPGSYIFELFAEAQITFQTKGCILDSLDQIIQHLAGRAGVFTNTAGLQKLADIIQIVFSVDPSEGSPGSPAGLGALQSYKVHIHPDAGHRRTAQRSDAWSTTAARKRGKVLSYWCFSPGHSMHELVRQGVRSLILTSGTLAPVSSFALEMQIPFPVCLENPHIIDKHQIWVGVVPRGPDGAQLSSAFDRRFSEECLSSLGKALGNIARVVPYGLLIFFPSYPVMEKSLEFWRARDLARKMEALKPLFVEPRSKGSFSETISAYYARVAAPGSTGATFLAVCRGKASEGLDFSDTNGRGVIVTGLPYPPRMDPRVVLKMQFLDEMKGQGGAGGQFLSGQEWYRQQASRAVNQAIGRVIRHRQDYGAVFLCDHRFAFADARAQLPSWVRPHVRVYDNFGHVIRDVAQFFRVAERTMPAPAPRATAPSVRGEDAVSEAKSPGPFFSTRKAKSLDLHVPSLKQRSSGSPAAGDPESSLCVEYEQEPVPARQRPRGLLAALEHSEQRAGSPGEEQAHSCSTLSLLSEKRPAEEPRGGRKKIRLVSHPEEPVAGAQTDRAKLFMVAVKQELSQANFATFTQALQDYKGSDDFAALAACLGPLFAEDPKKHNLLQGFYQFVRPHHKQQFEEVCIQLTGRGCGYRPEHSIPRRQRAQPVLDPTGRTAPDPKLTVSTAAAQQLDPQEHLNQGRPHLSPRPPPTGDPGSQPQWGSGVPRAGKQGQHAVSAYLADARRALGSAGCSQLLAALTAYKQDDDLDKVLAVLAALTTAKPEDFPLLHRFSMFVRPHHKQRFSQTCTDLTGRPYPGMEPPGPQEERLAVPPVLTHRAPQPGPSRSEKTGKTQSKISSFLRQRPAGTVGAGGEDAGPSQSSGPPHGPAASEWGL
Protein: Early E3 18.5 kDa glycoprotein (E3-19K) (E3gp 19 kDa) (E19) (GP19K) (P04494)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Binds and retains class I heavy chains in the endoplasmic reticulum during the early period of virus infection, thereby impairing their transport to the cell surface. Also delays the expression of class I alleles that it cannot affect by direct retention. Binds transporters associated with antigen processing (TAP) and acts as a tapasin inhibitor, preventing class I/TAP association. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
Subcellular location: Host endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MIRYIILGLLTLASAHGTTQKVDFKEPACNVTFAAEANECTTLIKCTTEHEKLLIRHKNKIGKYAVYAIWQPGDTTEYNVTVFQGKSHKTFMYTFPFYEMCDITMYMSKQYKLWPPQNCVENTGTFCCTAMLITVLALVCTLLYIKYKSRRSFIEEKKMP
Protein: High frequency lysogenization protein HflD (P25746)
Organism: Escherichia coli (strain K12)
Function: Negative regulator of phage lambda lysogenization. Contributes to the degradation of the phage regulatory protein CII. Acts probably by holding CII on the membrane surface, away from the target promoters, but close to the FtsH protease.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11278968}. Cell inner membrane {ECO:0000269|PubMed:11278968}; Peripheral membrane protein {ECO:0000269|PubMed:11278968}; Cytoplasmic side {ECO:0000269|PubMed:11278968}.
Interaction partners:
- tRNA-specific 2-thiouridylase MnmA
- Adenylosuccinate lyase
- Prophage tail fiber assembly protein homolog TfaE
- Modulator of FtsH protease HflK
- Modulator of FtsH protease HflC
- Ribonuclease T
- Protein YcgL
- Large ribosomal RNA subunit accumulation protein YceD
Sequence:
MAKNYYDITLALAGICQSARLVQQLAHQGHCDADALHVSLNSIIDMNPSSTLAVFGGSEANLRVGLETLLGVLNASSRQGLNAELTRYTLSLMVLERKLSSAKGALDTLGNRINGLQRQLEHFDLQSETLMSAMAAIYVDVISPLGPRIQVTGSPAVLQSPQVQAKVRATLLAGIRAAVLWHQVGGGRLQLMFSRNRLTTQAKQILAHLTPEL
Protein: General transcription factor II-I repeat domain-containing protein 1 (GTF2I repeat domain-containing protein 1) (Binding factor for early enhancer) (Q9JI57)
Organism: Mus musculus (Mouse)
Function: May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00484, ECO:0000269|PubMed:12780350}.
Interaction partners:
- General transcription factor II-I
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- CAP-Gly domain-containing linker protein 2
- Histone-lysine N-methyltransferase PRDM16
- Tyrosine-protein kinase BAZ1B
Sequence:
MALLGKHCDIPTNGCGSERWNSTFARKDELINSLVSALDSMCSALSKLNTEVACVAVHNESVFVMGTEKGRVFLNTRKELQSDFLRFCRGPLWNDPEAGHPKKVQRCEGGGRSLPRSSLEQCSDVYLLQKMVEEVFDVLYSEAMGRATVVPLPYERLLREPGLLAVQGLPEGLAFRRPAEYDPKALMAILEHSHRIRFKLRRPPDDGGQDTKALVEMNGISLLPKGSRDCGLHGQASKVAPQDLTPTATPSSMANFLYSTSMPNHTIRELKQEVPTCPLTPSDLGMGWPVPEPHVPSTQDFSDCCGQTPAGPAGPLIQNVHASKRILFSIVHDKSEKWDPFIKEMEDINTLRECVQILFNSRYAEALGLDHMVPVPYRKIACDPEAVEIVGIPDKIPFKRPCTYGVPKLKRILEERHSIHFIIKRMFDERIFTGNKFTKDPMKLEPASPPEDTSTEVCRDSMLDLAGTAWSDMSSVSEDCGPGTSGEIAMLRPIKIEPEELDIIQVTVSDPSPTSEEMTDSLPGHLPSEDSGYGMEMPADKGPSEEPWSEERPAEESPGDVIRPLRKQVEMLFNTKYAKAIGTSEPVKVPYSKFLMHPEELFVLGLPEGISLRRPNCFGIAKLRKILEASNSIQFVIKRPELLTDGVKEPVLDTQERDSWDRLVDETPKRQGLQENYNTRLSRIDIANTLREQVQDLFNKKYGEALGIKYPVQVPYKRIKSNPGSVIIEGLPPGIPFRKPCTFGSQNLERILSVADKIKFTVTRPFQGLIPKPETKILTTGHEAGKTTRPRRLQQDTWQPDEDDANRLGEKVILREQVKELFNEKYGEALGLNRPVLVPYKLIRDSPDAVEVKGLPDDIPFRNPNTYDIHRLEKILKAREHVRMVIINQLQPFAEVCNDPKVPEEDDSNKLGKKVILREQVKELFNEKYGEALGLNRPVLVPYKLIRDSPDAVEVKGLPDDIPFRNPNTYDIHRLEKILKAREHVRMVIINQLQPFGDVCNNAKVPAKDNIPKRKRKRVSEGNSVSSSSSSSSSSSNPESVASTNQISLVVKSRGSELHPNSVWPLPLPRAGPSTAPGTGRHWALRGTQPTTEGQAHPLVLPTR
Protein: Ubiquitin conjugation factor E4 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase E4) (F1M8V2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU369083}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Ubiquitin thioesterase OTU1
- Nuclear protein localization protein 4 homolog
- Ubiquilin-1
- Ubiquilin 2
- Nicotinamide-nucleotide adenylyltransferase
- UV excision repair protein RAD23 homolog B
- RAD23 homolog A, nucleotide excision repair protein.
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
Sequence:
MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASVPGPSQSLGLNVHNTTPATSPIGAAGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIATAARSPDRNLMLNTGSSSGTSPMFCSLGSFSASSLSSLGASGGASTWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLARAAKECSLDSDYFKYPLMALGELCETKFGKTHPMCNLVASLPLWLPKSLSPGSGRELQRLSYLGAFFSFSVFAEDDAKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAAIVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRINATMEDVNEWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDPAYPDITLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNQEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQSSDH
Protein: Tubulin beta chain (Q5SQY0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MNMPSTPLAPTTGTATCSWSASTCTTTRPAVRPPSFPHRPPGNAALPSLMPSRPTQVAGQCGAGNNWAKGHYTEGAELMESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSKTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGRYLTAAAIFRGRMPMREVDEQMFNIQDKNSSYFADWLPNNVKTAVCDIPPRGLKMSATFIGNNTAIQELFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA
Protein: glucan endo-1,3-beta-D-glucosidase (EC 3.2.1.39) (Q9M2T6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At1g53790
- Uncharacterized protein
- GDSL esterase/lipase At5g55050
- Exocyst subunit Exo70 family protein
Sequence:
MAKAPPSISLLLLLCAAVFLTIPAVISAIGVNYGTLGNLPPPTQVANFIKTQTSIDSVKIFDVNPDILRAFAGTGISVVVTVPNGDIPALANGRQARRWVSVNILPFHPQTKIKYISVGNEILLTGDNNMINNLLPAMRNLNNALVRAGVRDVKVTTAHSLNIIAYDLTGAPSSGRFRPGWDKGILAPILAYHRRTKSPFMVNPYPYFGFDPKNVNFAIFRTPYKAVRDPFTRHVYTNMFDALMDSTYSAMKALGYGDVNIVVGETGWPSACDAPWCSPANAAWFNLNIIKRAQGQGTPLMPNRRFETYIFGLFNEEGKPGPTAERNWGLFRADFSPVYDVGLLRNGQGGGGRPALPAPSTAGGKWCVARSGATNTQLQDSINWVCGQGVDCKPIQAGGSCFNPSSLRTHASFVMNAYFQSHGRTDGACNFSGTGMIVGNNPSNGACKY
Protein: Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5) (O88813)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villus axis of the small intestine (By similarity). May have a role in the survival of glioma cells (By similarity). May activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. It was suggested that it may also stimulate fatty acid oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16263710}. Endoplasmic reticulum {ECO:0000269|PubMed:16263710}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q9ULC5}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Palmitoyl thioesterase CPT1C
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Peroxisomal acyl-coenzyme A oxidase 1
- Fatty acid CoA ligase Acsl3
- Diacylglycerol O-acyltransferase 2
Sequence:
MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPMPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVRNGIIRRNSLWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE
Protein: Nuclear receptor subfamily 5 group A member 2 (FTZ-F1 beta) (Liver receptor homolog 1) (LRH-1) (Q9QWM1)
Organism: Rattus norvegicus (Rat)
Function: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development (By similarity). Activates the transcription of CYP2C38 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00482}. Chromosome {ECO:0000250|UniProtKB:O00482}.
Interaction partners:
- Nuclear receptor subfamily 0 group B member 2
- Nuclear receptor subfamily 0 group B member 1
- Catenin beta-1
- Nuclear receptor coactivator 3
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Cytochrome P450 7A1
- Nuclear receptor coactivator 2
- Zinc finger protein 217
- Cytochrome P450 family 8 subfamily B member 1
- Homeobox protein NANOG
Sequence:
MSASSITGDFQDFLKHGLPAIAPAPGSETPHSPKLEEKHREKRAGLPDRHRRPIPARSRLVMLPKVETEASGLVRSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNQKRYTCIENQNCQIDKTQRKRCPYCRFKKCIDVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTSAIQNIHSASKGLPLSHVALPPTDYDRSPFVTSPISMTMPPHGSLHGYQPYGHFPNRAIKSEYPDPYSSSPESMMGYSYMDGYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQNNRNRQEKLSAFGLLCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVAHGKEGTIFLVTGEHVDYSSIISNTEVAFNNLLSLAQELVVRLRSLQFDQREFVCLKFLVLFSSDVKNLENFQLVEGVQEQVNAALLDYTLCNYPQQTEKFGQLLLRLPEIRAISKQAEDYLYYKHVNGDVPYNNLLIEMLHAKRA
Protein: Mast cell protease 4 (mMCP-4) (EC 3.4.21.-) (MSMCP) (Myonase) (Serosal mast cell protease) (P21812)
Organism: Mus musculus (Mouse)
Function: Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing.
Interaction partners:
- Chymase
- Mast cell carboxypeptidase A
- Tryptase beta-2
- High affinity immunoglobulin epsilon receptor subunit alpha
- Angiotensinogen
- Angiotensin-converting enzyme
- Interleukin-33
- Renin-1
Sequence:
MQALLFLMALLLPSGAGAEEIIGGVESRPHSRPYMAHLEITTERGFTATCGGFLITRQFVMTAAHCSGREITVTLGAHDVSKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLLCAGVAHGIVSYGRGDAKPPAVFTRISSYVPWINRVIKGE
Protein: Maintenance of telomere capping protein 5 (SEH-associated protein 3) (Q03897)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in telomere capping.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}.
Interaction partners:
- Vacuolar membrane-associated protein IML1
- Protein transport protein SEC13
- SEH-associated protein 4
- Nucleoporin SEH1
- Nitrogen permease regulator 3
- Restriction of telomere capping protein 1
- Nitrogen permease regulator 2
- Mitochondrial inner membrane protease subunit 1
- Protein SLM4
- Protein LST4
Sequence:
MCSSINEGPYNSPTFGKSLSLKVDGGFNAVSINPSGRDIVLASRQGLYIIDLDDPFTPPRWLHHITPWQVADVQWSPHPAKPYWIVSTSNQKAIIWNLAKSSSNAIEFVLHGHSRAITDINFNPQHPDVLATCSVDTYVHAWDMRSPHRPFYSTSSWRSAASQVKWNYKDPNVLASSHGNDIFVWDLRKGSTPLCSLKGHVSSVNSIDFNRFKYSEIMSSSNDGTVKFWDYSKSTTESKRTVTTNFPIWRGRYLPFGEGYCIMPMVGGNNAVYLINLCDDDDSEQNKKTKLQPIYAFKGHSDRVIDFLWRSRHTCDGDYDDREFQLVTWSKDCDLKLWPISDSIYGKVNFDRGKRLEEKLPDYDYCSYNKEPENRENVQKNEFRRLRENFVTTSGLKKNKTNHITWLSGIRMNSATSQEDLFNETKIQNLGEEVSAIGHKFPKVVFEKISVSTRELCLTLNGPWSEENPDDYIFLRISINFPLNYPNKGDPPKFTIEENSNLTMSKRQEILSNLATIGQKYTDSNLYCLEPCIRFVLGEKVSLEDIEEGQEPLLNFDIADHIDFEELSSLDSSYSDSQNPENLSSQSDIESYKEALVFPDTSNQGLDFGRNLALDTTPVPNGCGSCWTATGELFCFFANEKKPEKKQNAIIKLSQKEAGVEKHPFKIEPQVLYDKEVDSSVITAADELKARPKRYVDTLGLGGGTNGDSRTYFDDETSSDDSFDSVADDWDDILRNDIIVRTKIPILRGNFKAFSSVHSESGKTVESTKKNKNLVISKNFSSLLSDRKELALEYLFMDATPEGFARNNALVAEKFDLDEISHCWQILSDMLIDQSDYDPYTTIWNNHPMGIKWFIKEAIVYFERQQNLQMLAMLCCVILSARRKKIPARYYGQELENMEGTIVFNDNESQNTSFWKGSDAFSTRSRSSTVTPNFYGNHLRGKNIHGGDNSSIRSDDHHARLRTHNTLNGSSKFTEPAQKQGSRAISSSPFHSRMPDIKVELLHDDIIEAYEQEDLLHLEVSDIPKFQTYIYQYSKLLFRWGLPLERVKILKVSTDFRSSYSSQGIPPNNNKKSPYNGVLTHWIENNEFGEEKFLARNCNYCDLRVTRSSFICGNCQHVLHSSCARIWWEIGDECPSGCGCNCPEMFDA
Protein: DnaJ homolog subfamily C member 5 homolog (Cysteine string protein) (Q03751)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have an important role in presynaptic function.
Subcellular location: Membrane; Lipid-anchor.
Interaction partners:
- Pleiotropic regulator 1
- Cell division cycle 5, isoform A
- Protein crooked neck
- Heat shock 70 kDa protein cognate 4
- Protein BUD31 homolog
- Pre-mRNA-processing factor 19
- Synaptotagmin 1
- Septin-interacting protein 1
- ATP-dependent RNA helicase DHX15 homolog
- Ras-related protein Rab-3
Sequence:
MSAPGMDKRKLSTSGDSLYEILGLPKTATGDDIKKTYRKLALKYHPDKNPDNVDAADKFKEVNRAHSILSNQTKRNIYDNYGSLGLYIAEQFGEENVNAYFVVTSPAVKAVVICCAVITGCCCCCCCCCCCNFCCGKFKPPVNESHDQYSHLNRPDGNREGNDMPTHLGQPPRLEDVDLDDVNLGAGGAPVTSQPREQAGGQPVFAMPPPSGAVGVNPFTGAPVAANENTSLNTTEQTTYTPDMVNQKY
Protein: Transcriptional activatory protein CaiF (P0AE58)
Organism: Escherichia coli (strain K12)
Function: Potential transcriptional activator of carnitine metabolism.
Interaction partners:
- Carbamoyl phosphate synthase small chain
- Carbamoyl phosphate synthase large chain
- Chaperone protein DnaJ
Sequence:
MCEGYVEKPLYLLIAEWMMAENRWVIAREISIHFDIEHSKAVNTLTYILSEVTEISCEVKMIPNKLEGRGCQCQRLVKVVDIDEQIYARLRNNSREKLVGVRKTPRIPAVPLTELNREQKWQMMLSKSMRR
Protein: ADP-ribosylation factor GTPase activating protein, putative (Q580U2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEKENGNKDKRRKEKHRKHHRDRRESCNGVVNSSAAKTRPETAVAIEGADEEVENWDENRTRVDQLCQTYPNNMCNDCNNAGTRWASVNHGVFLCIRCSGIHRSLGVHVSKVKSANMDKWSAAEVHLMELIGNQRAKLLYEAHLPKDMKPMTFAESDATLQTFIQRKYQEKAFSVEAVDEKLRQYHKEARYGKKPKRNSSASRKKKANDGANDKAERSLKGEDTIKALYGSNAEVISKMSKRTGPIRGTFGVVNVGPEAYDERRKTLLEQFGFS
Protein: Transcription factor HEC2 (Basic helix-loop-helix protein 37) (AtbHLH37) (bHLH 37) (Protein HECATE 2) (Transcription factor EN 117) (bHLH transcription factor bHLH037) (Q9SND4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the female reproductive tract development and fertility.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Copper transport protein family
- Thioredoxin family protein
- B3 domain-containing transcription factor NGA4
- B3 domain-containing protein REM2
Sequence:
MDNSDILMNMMMQQMEKLPEHFSNSNPNPNPHNIMMLSESNTHPFFFNPTHSHLPFDQTMPHHQPGLNFRYAPSPSSSLPEKRGGCSDNANMAAMREMIFRIAVMQPIHIDPESVKPPKRKNVRISKDPQSVAARHRRERISERIRILQRLVPGGTKMDTASMLDEAIHYVKFLKKQVQSLEEHAVVNGGGMTAVAGGALAGTVGGGYGGKGCGIMRSDHHQMLGNAQILR
Protein: Protein NETWORKED 4A (F4KEW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific actin binding protein. Associates with F-actin at the tonoplast. May be part of a membrane-cytoskeletal adapter complex.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:22840520}. Note=Arranged into short filaments and foci. {ECO:0000269|PubMed:22840520}.
Interaction partners:
- Myb-like HTH transcriptional regulator family protein
- Vesicle-associated protein 1-1
- Protein IQ-DOMAIN 2
- Protein KINESIN LIGHT CHAIN-RELATED 1
Sequence:
MDYDLLRSKKSIKRVESTKSNPWWWDSHIGLKNSKWLENNLDEMDRSVKRMVKLIEEDADSFAKKAEMYYQSRPELIALVDEFHRMYRALAERYENITGELRKGSPLELQSQGSGLSDISASDLSALWTSNEVNRLGRPPSGRRAPGFEYFLGNGGLPSDLYHKDGDDSASITDSELESDDSSVTNYPGYVSIGSDFQSLSKRIMDLEIELREAKERLRMQLEGNTESLLPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQLARYLPSGLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQLCFSLDYSRDEYKRLRIAFSGHPPTRPSSILAS