wanglab/gogpt-training-data huggingface dataset:
Protein: Uroplakin-3a (UP3a) (Uroplakin III) (UPIII) (Q9JKX8)
Organism: Mus musculus (Mouse)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}.
Interaction partners:
- Uroplakin-2
- Uroplakin-1b
- Uroplakin-1a
Sequence:
MLLLWALLALGCLRCGWTVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSSEPLSGSYEVYLYAMVDSAMSRNVSVQDSAGVPLSTTFRQTQGGRSGPYKAAAFDLTPCGDLPSLDAVGDVTQASEILNAYLVRVGNNGTCFWDPNFQGLCNPPLTAATEYRFKYVLVNMSTGLVQDQTLWSDPIWTNRPIPYSAIDTWPGRRSGGMIVITSILGSLPFFLLVGFAGAIILSFVDMGSSDGEMTHDSQITQEAVPKTLGTSEPSYSSVNRGPPLDRAEVFSSKLQD
Protein: Ammonium transporter 1 member 4 (AtAMT1;4) (Q9SVT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity ammonium transporter in the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19073648}; Multi-pass membrane protein {ECO:0000269|PubMed:19073648}.
Interaction partners:
- Nitrogen regulatory protein P-II homolog
- Amino acid transporter AVT1E
- Ras-related protein RABB1a
- Peroxidase 28
- High affinity nitrate transporter 2.3
Sequence:
MASALSCSASDLIPLLSGGANATAAAAAAEYICGRFDTVAGKFTDAAYAIDNTYLLFSAYLVFAMQLGFAMLCAGSVRAKNTMNIMLTNVIDAAAGGLFYYLFGFAFAFGSPSNGFIGKHFFGMYDFPQPTFDYPYFLYQWTFAIAAAGITSGSIAERTQFVAYLIYSSFLTGLVYPIVSHWFWSSDGWASPARSENLLFQSGVIDFAGSGVVHMVGGIAGLWGALIEGPRIGRFGVGGKPVTLRGHSATLVVLGTFLLWFGWYGFNPGSFATIFKAYGETPGSSFYGQWSAVGRTAVTTTLAGCTAALTTLFGKRLIDGYWNVTDVCNGLLGGFAAITSGCSVVEPWAALVCGFVAAWVLMGCNRLAEKLQFDDPLEAAQLHGGCGAWGIIFTGLFAEKRYIAEIFGGDPNRPFGLLMGGGGRLLAAHVVQILVITGWVSVTMGTLFFILHKLKLLRIPAEDEIAGVDPTSHGGLAYMYTEDEIRNGIMVRRVGGDNDPNVGV
Protein: Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC 3.1.2.2) (Peroxisomal long-chain acyl-CoA thioesterase 1) (P41903)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Contributes to growth on fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10092594}.
Interaction partners:
- Fructose-1,6-bisphosphatase
- 3,2-trans-enoyl-CoA isomerase
- Very-long-chain enoyl-CoA reductase
- ATP-dependent 6-phosphofructokinase subunit beta
- ATP-dependent 6-phosphofructokinase subunit alpha
- Acyl-coenzyme A oxidase
- Delta
- Peroxisomal hydratase-dehydrogenase-epimerase
- Carnitine O-acetyltransferase, mitochondrial
- Peroxisomal 2,4-dienoyl-CoA reductase SPS19 [
Sequence:
MSASKMAMSNLEKILELVPLSPTSFVTKYLPAAPVGSKGTFGGTLVSQSLLASLHTVPLNFFPTSLHSYFIKGGDPRTKITYHVQNLRNGRNFIHKQVSAYQHDKLIFTSMILFAVQRSKEHDSLQHWETIPGLQGKQPDPHRYEEATSLFQKEVLDPQKLSRYASLSDRFQDATSMSKYVDAFQYGVMEYQFPKDMFYSARHTDELDYFVKVRPPITTVEHAGDESSLHKHHPYRIPKSITPENDARYNYVAFAYLSDSYLLLTIPYFHNLPLYCHSFSVSLDHTIYFHQLPHVNNWIYLKISNPRSHWDKHLVQGKYFDTQSGRIMASVSQEGYVVYGSERDIRAKF
Protein: Cartilage oligomeric matrix protein (COMP) (P35444)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P49747}.
Interaction partners:
- Ig gamma-1 chain C region
- Aggrecan core protein
- A disintegrin and metalloproteinase with thrombospondin motifs 7
- Integrin beta-1
- Platelet glycoprotein 4
- Syndecan-4
- Platelet glycoprotein 4
- Syndecan-1
- Integrin subunit alpha 3
- Integrin subunit alpha 2b
Sequence:
MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA
Protein: Tubulin polyglutamylase TTLL6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin--tyrosine ligase-like protein 6) (A4Q9E8)
Organism: Mus musculus (Mouse)
Function: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins. Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions. Mediates microtubule polyglutamylation in primary cilia axoneme which is important for ciliary structural formation and motility. Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating. Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26829768}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Note=CEP41 is required for its transport between the basal body and the cilium axoneme. {ECO:0000250|UniProtKB:Q8N841}.
Interaction partners:
- Centrosomal protein of 41 kDa
- Cytosolic carboxypeptidase 6
Sequence:
MLQCLTSESEEGAEEREESSTEDLEELKEFVTLAFVRENTQKRLQNAQQHGKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKTYICKPDSGCQGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPLRVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFNSYMKTHGYDVEQIWRGIEDVIIKTLISAHPVIKHNYHTCFPSHTLNSACFEILGFDILLDRKLKPWLLEVNHSPSFSTDSKLDKEVKDSLLYDALVLINLGNCDKKKVLEEERQRGRFLQQCPNREIRLEEVKGFQAMRLQKTEEYEKKNCGGFRLIYPGLNLEKYDKFFQDNSSLFQNTVASRARELYARQLIQELRQKQEKKVFLKKARKEETQGESAGEQARDKVVRLQRQRQQPKCKTVATCPPKQSLHPVTLVSCTSGLLLNIRGLKKGEISESLEQKDTKEAMLIPCKPVSARNYSSVPDLRSANPSCFEPEFHVPNAKVKEVKSAFMVNIESTAQPITSVESSRDATAPISTSLESLASMSLSTSPECSSPESVHMVSYNHKQQKASFHKPMQEKKSKPLMFSKSRHLDLNCTSMKNDINRQYLMSEILQKVQMKKKRPLFPAPKSQYPTLSKERCPHSRSSSRKKEMNSPSVFVLQASHSRAESLNDLLVVATQARLDPRPSRSHSGTTTRDSSTQDPKHTATA
Protein: Bonus, isoform A (Q9VDK5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDLEQLKNDFLPLIAGIKQEQLDAVPTDALPQMSTPNTASGAPTTSSLSSSSLSLSNPCDSAEKRSESNSSASAKFTLFKCVYCAQLLGSNDRPKLLECLHVACAQCVSTKFSELDRSLPPLIHCPVCDNASQQEFIVDNQFLIEQCTAGDSGDGVGLLGLTGEGQKSSAAASIQCSSCSDGAVATSWCVDCSEYICDSCVQAHQRLKITKDHTIKPKDEANNEQLAGAAGVDKLHMCQLHPQEKLSLFCETCDKLTCRDCQLSDHRDHKYKFAHEIATESRQALSTLVSEINYKRFLLSSATKVIDDRQQLIHDKKKDLIKEITAMAVKITNTVNTRGKQLIMRLNEVCDSKLKVLVEKKETLQLLSDNTDHCIDFMQNALEKGSDFAILSSKKSLVRHLQKLKCQRADIPNPEIPVRIQVQLNQVSDLQKVISQLGIIIVDGKPYPPTPSPNGTPQPQHPPRQPPSPNMAPPLRPGLPPGMPAGLSPNGPPVNFGPQNGPPLYSNAAQQQFNNLSMSRSFPGDGSGKVRFGGMPPVGMQRHGQPHVSSSTHPQNMDISLRGLLNNQAAQSPNAHMAFNGPPSYPGGPQGAPAPAHQPMGPQMRPHFMPGQQGFSQGGGPGGGPRDANFMNSNARFQSQYQRMANHAQQAAAAAAMAGAAGGGGGQIPSPGALQRPQMMSNPMQNVSAMQNSLGFHGSQAGFNTGPPQTSPQLGGGGMHSLAKWHIPQSAQQSNMCSQQGPLLPFANGRQTSENFKISLKSPNTLKNSTPPSLGGGGAGHQGHGNGSSSAQLNAAALGLGPAVSILSNVTSTNPKTPSPSTHENTKDFTEPIDKVRDDSINDLIATIAKLDSNGVQVLPEGRTKTTSPQVHSSTDLSNTQEVNNKNEQKDDPNEDWCAVCLDGGELMCCDKCPKVFHQNCHIPAISSLPDESESWQCLLCVNIKELTKTEGSEKSSSGELSALELRILQRICLELYCQYEQSLNFREPESPANTSYYEIVSSPMSLDVIRTRLDPSSPNHYKDIAGFVSDVRLIFSNTYLFYQEDTKTYSNAKYLENFFEEQLAKWLPQFEGTKPQGKRNTSNSPALLGVNATGSPSPIENGRKSCGSASLGDSDGACLPAKRARRSAHE
Protein: Casein kinase II subunit beta-2 (CK II beta-2) (O94281)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity).
Interaction partners:
- Casein kinase II subunit alpha
- Casein kinase II subunit beta
- U3 small nucleolar RNA-associated protein 21 homolog
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar ribonucleoprotein protein imp3
- Uncharacterized protein C1604.06c
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar ribonucleoprotein protein imp4
- KRR1 small subunit processome component homolog
Sequence:
MSRKNLIKLNHDPTVTYSTKDDADELFDDLSSSPLHENVSWISWFCSRPGREYFVEVKEDFIEDLFNLTGLNLAVPFYNEALDLILDRTAPDTLENFDMDVIETSAQILYGLIHQRYIITRTGLHQMAEKYSMGIFGCCPRVNCCYTHVLPAGLSDIVGKMPVMLFCPNCLDLYAPSSSRYKNIDGSFFGATFPHLFFESYPELNPKRSIPCGKIYQPRIYGFKVSELSKTGPRMQWLRMYLEDSGSDSESESD
Protein: GH28580p (Rho-type guanine nucleotide exchange factor, isoform E) (C3KGL5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}.
Interaction partners:
Sequence:
MDQPLVVQAEYSFMGSNNDELCFQKGDVITVTQREDGGWWEGTLNDKTGWFPSNYVNECKVQLPLTETIRPPEEIQEYRSVVLKDLLDSERAHVAELQGLLENFLEPMQQTQILSQDEYAQLMCNFVEIVRTHEDLLIQIEECNDRVGKLFLTSAPLMKKVHQAYCAAHPKAIVILDKYKDELEKYMERQGAATPGLLVLTTGLSKPFRRLDKYSAMLQELERHMESSHPDRGDTQRSVAVYKDIAATCSATRRQKELELQVLTGPVRGWQGQELSTLGDIIHMGSVAVGADHRDRYFVLFPQTLLFLSVSQRMSAFIYEGKLPLTGIIVNRLEDTDALKNAFEISSPLIDRIVAVCQGPNEANKWVELLNANNPSLPMGIKRQLSNLSNSSLGHLNAAHMSPPSSHILLPPGGRPPATPSSIPAGSSSGGSHSHQGSPATNSMSHHKRSQSFNHHLSYNQYTPTQPPPHHLHPPQPPSLPSHLGASGPRSSSAQTPNSKTAAPLQASSMDASPAIQAAAAAAAAAVGMGVPSARKGSTKANWTISCLRPTPPLRPSLLNATSGSGSGSGGSGGGGSSSSNALASYCSGRKNQPTYEEDALVLRVFEAYCAAYQNNARNTIHSGKWRSPSQMCFI
Protein: Proline-rich antigen homolog (Pra) (P9WIM7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aminoglycoside 2'-N-acetyltransferase
- Carboxyltransferase domain-containing protein
- Conserved protein
- Carboxyltransferase domain-containing protein
- Cystathionine gamma-synthase
- Three-Cys-motif partner protein TcmP
- Probable conserved Mce associated protein
- Possible exported protein
- Small ribosomal subunit protein uS9
- Glutamine synthetase
Sequence:
MTEQPPPGGSYPPPPPPPGPSGGHEPPPAAPPGGSGYAPPPPPSSGSGYPPPPPPPGGGAYPPPPPSAGGYAPPPPGPAIRTMPTESYTPWITRVLAAFIDWAPYVVLVGIGWVIMLVTQTSSCVTSISEYDVGQFCVSQPSMIGQLVQWLLSVGGLAYLVWNYGYRQGTIGSSIGKSVLKFKVVSETTGQPIGFGMSVVRQLAHFIDAIICFVGFLFPLWDAKRQTLADKIMTTVCVPI
Protein: Farnesol kinase, chloroplastic (EC 2.7.1.216) (Q67ZM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinase involved in negative regulation of abscisic acid (ABA) signaling. Substrate preference is farnesol > geraniol > geranylgeraniol, but has no activity with farnesyl phosphate. Can use CTP > ATP > GTP = UTP as phosphoryl donor.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- NAD
- CAAX prenyl protease 2
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- CAAX prenyl protease 1 homolog
- Solanesyl diphosphate synthase 2, chloroplastic
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- Solanesyl diphosphate synthase 1, chloroplastic
Sequence:
MATTSTTTKLSVLCCSFISSPLVDSPPSLAFFSPIPRFLTVRIATSFRSSSRFPATKIRKSSLAAVMFPENSVLSDVCAFGVTSIVAFSCLGFWGEIGKRGIFDQKLIRKLVHINIGLVFMLCWPLFSSGIQGALFASLVPGLNIVRMLLLGLGVYHDEGTIKSMSRHGDRRELLKGPLYYVLSITSACIYYWKSSPIAIAVICNLCAGDGMADIVGRRFGTEKLPYNKNKSFAGSIGMATAGFLASVAYMYYFASFGYIEDSGGMILRFLVISIASALVESLPISTDIDDNLTISLTSALAGFLLF
Protein: Sulfotransferase 2A1 (ST2A1) (EC 2.8.2.2) (Bile salt sulfotransferase) (EC 2.8.2.14) (Dehydroepiandrosterone sulfotransferase) (DHEA-ST) (DHEA-ST8) (Hydroxysteroid Sulfotransferase) (HST) (ST2) (SULT2A3) (Q06520)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism. In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2268288}.
Interaction partners:
- Cytochrome P450 2B6
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Sulfotransferase 1B1
- Sarcoplasmic reticulum histidine-rich calcium-binding protein
- Cholesterol side-chain cleavage enzyme, mitochondrial
- UDP-glucuronosyltransferase 1A8
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Sulfotransferase 1E1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
Sequence:
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVVDKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Protein: Glutamine synthetase (EC 6.3.1.2) (Q84UC1)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
- glutamate synthase
- glutamate synthase
- Ferredoxin--nitrite reductase, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- glutamine--fructose-6-phosphate transaminase
- Glutamate-glyoxylate aminotransferase
- Amidophosphoribosyltransferase
- amidophosphoribosyltransferase
- glutamate dehydrogenase
Sequence:
MAQILAPSTQCQARITKISPVATPISSKMWSSLVMKQNKKVARSAKFRVMAVNSGTINRVEDLLNLDITPFTDSIIAEYIWIGGTGIDVRSKSRTISKPVEHPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNILVICDAYTPQGEPIPTNKRHKAAEIFSNPKVEAEIPWYGIEQEYTLLQTDVKWPLGWPVGGYPGPQGPYYCAAGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEYQVGPSVGIEAGDHIWASRYILERITEQAGVVLTLDPKPIEGDWNGAGCHTNYSTKSMREDGGFEVIKKAILNLSLRHKIHIEAYGEGNERRLTGKHETASINTFSWGVANRGCSIRVGRDTEKNGKGYLEDRRPASNMDPYVVTALLAESTLLWEPTLEAEALAAQKIALKV
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)] (Q62165)
Organism: Mus musculus (Mouse)
Function: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Subcellular location: [Alpha-dystroglycan]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma. Postsynaptic cell membrane. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli.
Interaction partners:
- Dystrophin
- Agrin
- Alpha-sarcoglycan
- Delta-sarcoglycan
- Utrophin
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Laminin subunit alpha-2
- Gamma-sarcoglycan
- Pikachurin
- Beta-sarcoglycan
Sequence:
MSVDNWLLHPLWGQTFLLLLSVAVAQAHWPSEPSEAVRDWKNQLEASMHSVLSDFQEAVPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHNEPQSVRAASSDPGEVVPSACAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAVITPPTTTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHKRPQGDKAPARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Protein: FI01014p (Q2MGN0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQVIPNTPTPQMLTTSTPIEPMKPPPAFPTMSGANIHEQASDMILRASTIFEDVKHDEANVENVPHHGVETEPEDDSHYGGNGNSKIRIMPSVKLMATTLASDPKRKFVCPYDNCTKSYGKSSHLRSHLTWHTGIKPFVCSEPKCGKGFTRSDELNRHLRTHTGEKPFECIQCTKKFSRSDHLTKHLATHDRQLKGSTPKRTVPSSSGGVRLKPPKKQIHSESDSGFHFMAAMVGCGEPSMKHHHQQQQHNQHQQPVSIIDIHHKPIKIKLERPEHSDKYQIVSPEHQMDNHGHNQSQLPDFLNQAKPEVKYEPTEEIVNTLSQLPPADGPGTYGMPQFVQDRPFYCRQCEKRFKRQDDLNRHIRTHTGEKPYACQQCCRRFVRSDHLKKHQQTHLKIR
Protein: Lymphocyte cytosolic protein 2 (SH2 domain-containing leukocyte protein of 76 kDa) (SLP-76 tyrosine phosphoprotein) (SLP76) (Q60787)
Organism: Mus musculus (Mouse)
Function: Involved in T-cell antigen receptor mediated signaling.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Tyrosine-protein kinase SYK
- Proto-oncogene vav
- GRB2-related adaptor protein 2
- SH2/SH3 adapter protein Nck1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Tyrosine-protein kinase ITK/TSK
- Tyrosine-protein kinase ZAP-70
- Growth factor receptor-bound protein 2
- Guanine nucleotide exchange factor VAV3
- Linker for activation of T-cells family member 1
Sequence:
MALKNVPFRSEVLAWNSDNLADYFRKLNYRDCEKAVKKYHIDGARFLNLTENDIQKFPKLRMPLLSKLSQDINKNEERRSIFTRKPQIPRFLEETESHEEDDGGWSSFEDDYESPNDDDPDGEDDGDYESPNEEEQALVDDAADYEPPPSNNEEALQSSILPPNSFHNTNSMYIDRPPTGKVSQQPPVPPLRPKPALPPLPTGRNHSPLSPPHPNHEEPSRSGNNKTAKLPAPSIDRSTKPPLDRSLAPLDREPFILGKKPPFSDKPSAPLGREHLPKIQKPPLPPAMDRHERNERLGPVTTRKPPVPRHGRGPDRRENDEDDVHQRPLPQPSLPSMSSNTFPSRSVQPSSKNTFPLAHMPGAFSESNIGFQQSASLPPYFSQGPGNRPPLRSEGRNLPLPVPNRPQPPSPGEEETPLDEEWYVSYITRPEAEAALRKINQDGTFLVRDSSKKTANNPYVLMVLYKDKVYNIQIRYQEESQVYLLGTGLRGKEDFLSVSDIIDYFRKMPLLLIDGKNRGSRYQCTLTHAAGCL
Protein: Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (pABP-2) (P70486)
Organism: Rattus norvegicus (Rat)
Function: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells probably implying recruitment of CBX5 to telomeres. May be involved in transcriptional regulation of telomeric repeat-containing RNA (TERRA). Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with CBX5/HP1 alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-nuclear bodies (By similarity). {ECO:0000250}.
Interaction partners:
- Death domain-associated protein 6
- Methyl-CpG-binding protein 2
- SP100 nuclear antigen
- DNA
- DNA repair protein RAD51 homolog
- Histone H3.3
- Cellular tumor antigen p53
- DNA repair protein RAD52 homolog
- THO complex subunit 2
- RNA-binding motif protein 25-like 1.
Sequence:
GRSVVEFGDMVCKRQQSAVSSAGSEKPSGKEENVHSPEDKRVTKSKEKSKHLRTRTGRKVKSDVTDRFRKKEQSSESSEGEKKQGRQRTGTRGKKSTDLKEEKVKREREYESSSDGTEKLPEGEEIGLFSKGVKQNKNDTTDEAKKGKKWKDKSCEKKEELSDSVDRLPVKGESCDSSEDKKTRNRVSLREKKQFSLPAKSSGKRPECSSSDTERSVKGECCDSTDKRVKRIDLRERRSSNSKRSTKEVKSGSSSSDAEGSSEDAKKQKKQRMSAKKKNSNTKERKRKSLRATTTKRKQADITSSSSDIGDDDQNSAGEESSDEQKIKPVTENLVLPSHTGFCQSSGDEAFSKSVPATVDDDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPKEGEKKRIGKQSEETPGDDGSNQVNSESDSDSEESKKPRYRHRLLRHKLSLSDGESGGEKKTKPKEHKETKGRNRRKVSSEDSEDTDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRR