wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin alpha-4A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Tubulin alpha-1 chain) (P81948)
Organism: Bos taurus (Bovine)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}.
Interaction partners:
- Doublecortin domain-containing protein
- Cell division control protein 42 homolog
- Tubulin beta-4B chain
- Tubulin beta-4A chain
- Gap junction alpha-1 protein
- Tubulin beta-2B chain
- Zona occludens protein 1
- MARVEL domain containing 2
- Tubulin beta-5 chain
- Serine/threonine-protein kinase PLK1
Sequence:
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE
Protein: E3 ubiquitin-protein ligase RNF144A (EC 2.3.2.31) (RING finger protein 144A) (UbcM4-interacting protein 4) (Ubiquitin-conjugating enzyme 7-interacting protein 4) (P50876)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24979766, ECO:0000269|PubMed:30171075}; Single-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:24979766, ECO:0000269|PubMed:37955227}. Endosome membrane {ECO:0000269|PubMed:30171075}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:37955227}.
Interaction partners:
- DNA-dependent protein kinase catalytic subunit
Sequence:
MTTTRYRPTWDLALDPLVSCKLCLGEYPVEQMTTIAQCQCIFCTLCLKQYVELLIKEGLETAISCPDAACPKQGHLQENEIECMVAAEIMQRYKKLQFEREVLFDPCRTWCPASTCQAVCQLQDVGLQTPQPVQCKACRMEFCSTCKASWHPGQGCPETMPITFLPGETSAAFKMEEDDAPIKRCPKCKVYIERDEGCAQMMCKNCKHAFCWYCLESLDDDFLLIHYDKGPCRNKLGHSRASVIWHRTQVVGIFAGFGLLLLVASPFLLLATPFVLCCKCKCSKGDDDPLPT
Protein: Small ribosomal subunit protein eS6B (40S ribosomal protein S6-B) (RP9) (S10) (YS4) (P0CX38)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
Sequence:
MKLNISYPVNGSQKTFEIDDEHRIRVFFDKRIGQEVDGEAVGDEFKGYVFKISGGNDKQGFPMKQGVLLPTRIKLLLTKNVSCYRPRRDGERKRKSVRGAIVGPDLAVLALVIVKKGEQELEGLTDTTVPKRLGPKRANNIRKFFGLSKEDDVRDFVIRREVTKGEKTYTKAPKIQRLVTPQRLQRKRHQRALKVRNAQAQREAAAEYAQLLAKRLSERKAEKAEIRKRRASSLKA
Protein: NAD(+) hydrolase sarm1 (NADase sarm1) (EC 3.2.2.6) (Sterile alpha and TIR motif-containing protein 1) (Tir-1 homolog) (Q6IDD9)
Organism: Drosophila melanogaster (Fruit fly)
Function: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site. Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, it is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting axon destruction. Involved in the down-regulation of the tracheal immune response to Gram-negative bacteria. This is likely by mediating Tollo signaling in the tracheal epithelium.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, axon {ECO:0000269|PubMed:22678360}.
Interaction partners:
- LD20892p
- Nicotinamide-nucleotide adenylyltransferase
- Axundead, isoform F
- GH01161p
Sequence:
MKAAEIKRDLTNIQKSMSEINDLAKERITGGPGSISTTSASAITAPSTMSQTTTSRLAPKLTSAHPSIDDLRGLSRQDKITQLQKKIRASFENLVDHDDSNVIVTLPDDDDCPHNHFGSGLNLTHPTAAQLSASGLSGSSKTIDTIKFQEKSMKTESKTKVVTDGFSSEQATSNSAEMKRLQAGDIDYQESKGASAMRNRLEVDGVKTEENAAVIKEALSLRTGDITQQASNNVAASSITVQSENFSADKKAISQSQQSQTMTSNGIISQEKHVSSASQANYSMSHKGVSSTGSSMITSSSQMSAMNGQMLKLADLKLDDLKSLTAGSGQQEIEQTINKYSNMLTSIVSSLQEDERGGSAITVHDVGGKKSQYLEKINEVIRRAWAVPTHGHELGYSLCNSLRQSGGLDLLMKNCVKPDLQFSSAQLLEQCLTTENRKHVVDNGLDKVVNVACVCTKNSNMEHSRVGTGILEHLFKHSEGTCSDVIRLGGLDAVLFECRTSDLETLRHCASALANLSLYGGAENQEEMILRKVPMWLFPLAFHNDDNIKYYACLAIAVLVANKEIEAEVLKSGCLDLVEPFVTSHDPSAFARSNLAHAHGQSKHWLKRLVPVLSSNREEARNLAAFHFCMEAGIKREQGNTDIFREINAIEALKNVASCPNAIASKFAAQALRLIGETVPHKLSQQVPLWSVEDVQEWVKQIGFNDYIDKFNESQVDGDLLLKLNQDNLRADIGIGNGILLKRFERELQNLKRMADYSSKDTAKMHQFLSEIGTDYCTYTYAMLNAGIDKCALPHVNEDMLMTECGIHNSIHRLRILNAVKNLENSLPSSSEENMAKTLDVFVSYRRSNGSQLASLLKVHLQLRGFSVFIDVERLEAGKFDNGLLNSIRQAKNFVLVLTPDALHRCINDEDCKDWVHREIVAALNSNCNIIPIIDQQFDWPEVERLPEDMRSVAHFNGVNWIHDYQDACIDKLERFLRGEKNIDRIAAMVPGTPGSVSYQRMHSNDSDYQSGGAGAGSGAGTGGGGGGGVTGSVVDGLMVAANGSGQANHQANRYRQSPSPARQRGSTSQLSGYSRAPSKRSQILTPYRTQQAALLHKTGAGSASMQNMMPLAYLPPRRSSAAGLGHGSGSGMGSGYRSHSVDGLLDQAGSTPEQRIAAAAAKVTAGSTALTNASSTSTLQPEEEVTDAALNDSVTRRDKHTLSPPGNVQQHRKSRSLDHILSKQTLAELLPPSSELADGTQSMQNLAIPMTPQPQRRDTSSSSKSPTPERPPQPAMERVRERQSPEGVSATESEREDQPEECLRHGNQQRASASVHRGASLTSNKTSNSSLGSNFSAGGNNKTIFNRTMKKVRSLIKKP
Protein: Fatty acid-binding protein, brain (Brain lipid-binding protein) (BLBP) (Brain-type fatty acid-binding protein) (B-FABP) (Fatty acid-binding protein 7) (Mammary-derived growth inhibitor related) (O15540)
Organism: Homo sapiens (Human)
Function: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Fatty-acid amide hydrolase 1
- Recombining binding protein suppressor of hairless
- Neurogenic locus notch homolog protein 3
- Excitatory amino acid transporter 1
- Glial fibrillary acidic protein
- Nestin
- Protein S100-B
- Fatty acid-binding protein, adipocyte
- Paired box protein Pax-6
Sequence:
MVEAFCATWKLTNSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFQLGEEFDETTADDRNCKSVVSLDGDKLVHIQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEKA
Protein: GSK-3-binding protein FRAT2 (Frequently rearranged in advanced T-cell lymphomas 2) (FRAT-2) (Q8K025)
Organism: Mus musculus (Mouse)
Function: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Proto-oncogene FRAT1
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-2
- FRAT3
Sequence:
MPCRREEEEEAGDEAEGEEDDDSFLLLQQSVTLGGSTDVDRLIVQIGETLQLDTAHDRPASPCAAPGPPPAPPRVLAALSADKTGTPARRLLRPTGSAETGDPAPPGAVRCVLGERGRVRGRSAPYCVAEIAPGASALPGPGRRGWLPGSVASHRIQQRRWTAGGARAADDDPHRLLQQLVLSGNLIKEAVRRLQRAVAAVAATSPASAPGSGGGRSGPDSVTLQPSGAWL
Protein: Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (iGnT) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1) (Q8BWP8)
Organism: Mus musculus (Mouse)
Function: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23217742}; Single-pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus. {ECO:0000250|UniProtKB:O43505}.
Interaction partners:
- Ribitol-5-phosphate xylosyltransferase 1
- Xylosyl- and glucuronyltransferase LARGE2
- Xylosyl- and glucuronyltransferase LARGE1
- Protein O-mannose kinase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Ribitol-5-phosphate transferase FKTN
- D-ribitol-5-phosphate cytidylyltransferase
- Protein O-mannosyl-transferase 2
Sequence:
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQEQYFEFFPPSPRSVDQVKSQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPEMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNTSYPNNLLRNLAREEANYALVIDVDMVPSEGLWRGLREMLDQSNHWDGTALVVPAFEIRRSRRMPMNKNELVQLYQVGEVRPFYYGLCTPCHAPTNYSRWVNLPEESLLRPAYVVPWRDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFNFEVLNEGFLVHKGFKEALKFHPQKEAENQRNKILYRQFKQELKARYPNSPHRC
Protein: Dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase (H2N-cP phosphodiesterase) (H2Neo-cP phosphodiesterase) (EC 3.1.4.56) (7,8-dihydro-D-neopterin 2',3'-cyclic phosphate phosphodiesterase) (Q58247)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Cyclic phosphodiesterase that hydrolyzes the cyclic phosphate of 7,8-dihydroneopterin 2',3'-cyclic phosphate (H2N-cP) and converts it to a mixture of 7,8-dihydroneopterin 2'-phosphate (H2N-2'P) and 7,8-dihydroneopterin 3'-phosphate (H2N-3'P). Is also able to utilize other phosphodiesters as substrates in vitro: hydrolysis of bis-pNPP and pNPPC produces nitrophenyl phosphate, and that of 2',3'-cAMP produces 3'-AMP. ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN cannot serve as substrates.
Interaction partners:
- GTP cyclohydrolase MptA
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
- Dihydroneopterin aldolase
Sequence:
MERLIKLAEQIKDEELRKKVIEFLKNPKATHPGIVDTGISVEEAPASINWHHRYEGGLIEHTISVTKIALKMADVLEEVYGVEVNRDYIIAGALLHDIMKPYNYIRKEDGTFDHYDMFNLDHLTLAVAELYKRDFPIEVIKIVASHHGDHSPTRPNSIEAYIVHYADEADSKINDVAVRVCQARSRDLGISEQEIYKAVNPLKVYEVRSREGKLKTIEFLKDILKSIGIISEDEKKDENNESLENKESN
Protein: ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein (F4IWM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATQAAQAITVTDLEAILDRFVEKLEEKLDSVVQRLQAQQEEYRRGIREIFAKFFPKLLPILGSQSFQRRCILAGEEEPMLHKLAGEDLFLLIRAIIRPRSSWLDSTVPFPRLLVARQESHRRSFSGYYGSDSQESSDGVVSRRKSWERKRYRESKDGDIRSSEQSARNGSLFWTNSKKAWEQVGLDSQEKNDNAADSIRVLYIGFQGTAPQVAMEVEHDIISRDAAWKGQKKQSQVAMVGRERLPPLVKDSHCEEEHREARVSRPLDENLRRCLSNFENYFGENNIPEQERLQIVYSNLEGDIGQWIKHLWKKNSPTSWKEFKCMMARETKTTMKVNHQPHYSGIQQEGSVREYRERFEALCLGSVILPGQGLEALFLQGLQPSLQTAVRELKPNGIVQMMDTAQWLEESNSLMVYGSGLSVQTEPKVYPTTQAELRSMVLMGYMREDLKDTPRPANEDTGTLKQEHELPGTEVATCRGMRFYGYILQQEVSFSYRLASDVKRSCQEISLRINDIDIVEDYCVWDLKRDVVDVILGYEWLSKLGETEVNWQNQSFSFIHNQDWVTLCPKNKDLEQGTKRVKMRSEKEQGGMRNELESDCGIVAYYLADKVALKGESNVSCVEVTNDRDCEDEKRGENQEMKLSTEYPKEVSWFNEFEQIGILVKMQFTRPPEVFLGQVMEQENVKATIEVDVCVEKQKREIEDHLVLGLKTGEDKVRLMVGSFSKQQDRVYKCCMMLEMLLVSNGVSSLENTRALKRSAEMSRWKQFGVTHKEGKERGSSQTGFGGTIDPRAKTKHETKANKAMINAREFHFQFLPP
Protein: Cell surface glycoprotein MUC18 (Cell surface glycoprotein P1H12) (Melanoma cell adhesion molecule) (Melanoma-associated antigen A32) (Melanoma-associated antigen MUC18) (S-endo 1 endothelial-associated antigen) (CD antigen CD146) (P43121)
Organism: Homo sapiens (Human)
Function: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Laminin subunit alpha-4
- Vascular endothelial growth factor receptor 2
- Rho-related GTP-binding protein RhoB
- Platelet endothelial cell adhesion molecule
- Endoglin
- Integrin beta-1
- Frizzled-3
- Thy-1 membrane glycoprotein
- 5'-nucleotidase
- Hematopoietic progenitor cell antigen CD34
Sequence:
MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH
Protein: F-box/kelch-repeat protein At5g60570 (Q9FKJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At1g30200
- At5g27920
- Probable methyltransferase PMT24
- AT3G11930 protein
- Tubby-like F-box protein 9
- Tubby-like F-box protein 2
- F-box protein PP2-A13
- GRR1-like protein 1
- Ubiquitin-conjugating enzyme E2 5
- Probable methyltransferase PMT21
Sequence:
MAAEEHSNKRREVSASASASASASVVVNLRVGEEDNDGHRLRLGSSDSVLPGLIDDVALNCLAWVPRSDYPSLSCVNKKYNKLINSGHLFALRKELGIVEYLVFMVCDPRGWLMFSPMKKKWMVLPKMPCDECFNHADKESLAVDDELLVFGRELFQFAIWKYSLRSRCWVKCEGMHRPRCLFASGSLGGIAIVAGGTDMNGNILASAELYDSSSGRWEMLPNMHSPRRLCSGFFMDGKFYVIGGMSSPNVSVTFGEEFDLETRKWRKIEGMYPNVNRAAQAPPLVVVVNNELFTLEYSTNMVKKYDKVKNKWEVMGRLPPMVDSSNGWGLAFKPCGDQLLVFCGQRGPHGEGIVVNSWCPKSGAKDGNLDWKVLGVKENVGVFVYNCAVMGC
Protein: N6-adenosine-methyltransferase non-catalytic subunit MTB (Methyltransferase-like protein 1) (Protein EMBRYO DEFECTIVE 1691) (Protein METTL14 homolog) (Q94AI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable non-catalytic subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs. Associates with MTA, FIP37, VIR and HAKAI to form the m6A writer complex which is essential for adenosine methylation at specific mRNA sequences. N6-methyladenosine (m6A) plays a role in mRNA stability, processing, translation efficiency and editing.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:28503769}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28503769}.
Interaction partners:
- FKBP12-interacting protein of 37 kDa
- N
- Protein virilizer homolog
- E3 ubiquitin-protein ligase HAKAI homolog
- Far-red impaired responsive
- ASI1-immunoprecipitated protein 2
- YTH domain-containing protein ECT4
- YTH domain-containing protein ECT3
- YTH domain-containing protein ECT2
- At4g36090
Sequence:
MKKKQEESSLEKLSTWYQDGEQDGGDRSEKRRMSLKASDFESSSRSGGSKSKEDNKSVVDVEHQDRDSKRERDGRERTHGSSSDSSKRKRWDEAGGLVNDGDHKSSKLSDSRHDSGGERVSVSNEHGESRRDLKSDRSLKTSSRDEKSKSRGVKDDDRGSPLKKTSGKDGSEVVREVGRSNRSKTPDADYEKEKYSRKDERSRGRDDGWSDRDRDQEGLKDNWKRRHSSSGDKDQKDGDLLYDRGREREFPRQGRERSEGERSHGRLGGRKDGNRGEAVKALSSGGVSNENYDVIEIQTKPHDYVRGESGPNFARMTESGQQPPKKPSNNEEEWAHNQEGRQRSETFGFGSYGEDSRDEAGEASSDYSGAKARNQRGSTPGRTNFVQTPNRGYQTPQGTRGNRPLRGGKGRPAGGRENQQGAIPMPIMGSPFANLGMPPPSPIHSLTPGMSPIPGTSVTPVFMPPFAPTLIWPGARGVDGNMLPVPPVLSPLPPGPSGPRFPSIGTPPNPNMFFTPPGSDRGGPPNFPGSNISGQMGRGMPSDKTSGGWVPPRGGGPPGKAPSRGEQNDYSQNFVDTGMRPQNFIRELELTNVEDYPKLRELIQKKDEIVSNSASAPMYLKGDLHEVELSPELFGTKFDVILVDPPWEEYVHRAPGVSDSMEYWTFEDIINLKIEAIADTPSFLFLWVGDGVGLEQGRQCLKKWGFRRCEDICWVKTNKSNAAPTLRHDSRTVFQRSKEHCLMGIKGTVRRSTDGHIIHANIDTDVIIAEEPPYG
Protein: Disintegrin and metalloproteinase domain-containing protein 1b (ADAM 1b) (EC 3.4.24.-) (Fertilin subunit alpha-b) (Q8R534)
Organism: Mus musculus (Mouse)
Function: May play a role in spermatogenesis and sperm maturation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
Sequence:
MERLKLGKIPEHWCIRLVAMLLLAIIFLPSTFCDIGSVYNSSYETVIPERLPGKGGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSYHNGILRQEMPLLSQDCHYEGYMEGVPGSFVSVNICSGLRGVLIKEETSYGIEPMLSSKNFEHVLYTMEHQPVVSCSVTPKDSPGDTSHPPRSRKPDDLLVLTDWWSHTKYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEKLVGRVRHDVAHLIVGHRPGENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTCGPKHFCLMGEKIGKDSGFSNCSSDHFLRFLHDHRGVCLLDEPGRQSRMRRAANCGNGVVEDLEQCDCGSDCDKSQCCDENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSDRKAQDGSKCHESFLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSSQFPKKYTKCSDKNVMCGKLICTEVAFLPQIQPNNLLLQVPETEDWCWSVAVFDMRDSLHEEYVKDNTYCGKDKVCKNSICEDFTPFSFPCSPSKQCNKHGVCNDLGNCHCSFGFAPPDCKEEGTGGSVDSGPAVNLSNDSSPGPNSTQSSTEELILNLKLIVLAVILVLMILLIIICIISAYTKSETASEAGPSELEELPEGEKEEQEEVLPEEAKGEEEELEYGKEEAEEQGAVEEEGAEEANEEAAAEKKDEDEEEGEE
Protein: Insulin-induced gene 1 protein (INSIG-1) (Immediate-early protein CL-6) (Insulin-induced growth response protein CL-6) (Q08755)
Organism: Rattus norvegicus (Rat)
Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139. Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15503}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15503}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Sterol regulatory element-binding protein 2
- E3 ubiquitin-protein ligase AMFR
- Insulin-induced gene 2 protein
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Lanosterol 14-alpha demethylase
- Sterol regulatory element-binding protein 1
- Isopentenyl-diphosphate Delta-isomerase 1
- Delta
Sequence:
MPRLHDHVWSYPSAGAARPYSLPRGMIAAALCPQGPGAPEPEPAPRGQREGTAGFSARPGSWHHDLVQRSLVLFSFGVVLALVLNLLQIQRNVTLFPDEVIATIFSSAWWVPPCCGTAAAVVGLLYPCIDSHLGEPHKFKREWASVMRCIAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGLGLGITIAFLATLITQFLVYNGVYQYTSPDFLYIRSWLPCIFFSGGVTVGNIGRQLAMGVPEKPHSD
Protein: Pup--protein ligase (EC 6.3.1.19) (Proteasome accessory factor A) (Pup-conjugating enzyme) (P9WNU7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.
Interaction partners:
- Proteasome subunit alpha
- Protein PafB
- Proteasome-associated ATPase
- Protein PafC
- Proteasome subunit beta
- Prokaryotic ubiquitin-like protein Pup
- Putative glutamate--cysteine ligase 2
- Sec-independent protein translocase protein TatA
- Bacterial proteasome activator
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
Sequence:
MQRRIMGIETEFGVTCTFHGHRRLSPDEVARYLFRRVVSWGRSSNVFLRNGARLYLDVGSHPEYATAECDSLVQLVTHDRAGEWVLEDLLVDAEQRLADEGIGGDIYLFKNNTDSAGNSYGCHENYLIVRAGEFSRISDVLLPFLVTRQLICGAGKVLQTPKAATYCLSQRAEHIWEGVSSATTRSRPIINTRDEPHADAEKYRRLHVIVGDSNMSETTTMLKVGTAALVLEMIESGVAFRDFSLDNPIRAIREVSHDVTGRRPVRLAGGRQASALDIQREYYTRAVEHLQTREPNAQIEQVVDLWGRQLDAVESQDFAKVDTEIDWVIKRKLFQRYQDRYDMELSHPKIAQLDLAYHDIKRGRGIFDLLQRKGLAARVTTDEEIAEAVDQPPQTTRARLRGEFISAAQEAGRDFTVDWVHLKLNDQAQRTVLCKDPFRAVDERVKRLIASM
Protein: Glutathione S-transferase A4 (EC 2.5.1.18) (GST A4-4) (GSTA4-4) (GST class-alpha member 4) (Glutathione S-transferase 5.7) (GST 5.7) (P24472)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase theta-1
- Glutathione S-transferase omega-1
- Glutathione S-transferase theta-2
- Glutathione S-transferase Mu 1
- Glutathione peroxidase 2
- Glutathione peroxidase 1
- Microsomal glutathione S-transferase 1
- Glutathione S-transferase kappa 1
- Glutathione peroxidase 3
- Glutathione S-transferase omega-2
Sequence:
MAAKPKLYYFNGRGRMESIRWLLAAAGVEFEEEFLETREQYEKMQKDGHLLFGQVPLVEIDGMMLTQTRAILSYLAAKYNLYGKDLKERVRIDMYADGTQDLMMMIAVAPFKTPKEKEESYDLILSRAKTRYFPVFEKILKDHGEAFLVGNQLSWADIQLLEAILMVEELSAPVLSDFPLLQAFKTRISNIPTIKKFLQPGSQRKPPPDGPYVEVVRTVLKF