wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Deubiquitinating enzyme 45) (Ubiquitin thioesterase 45) (Ubiquitin-specific-processing protease 45) (Q70EL2)
Organism: Homo sapiens (Human)
Function: Catalyzes the deubiquitination of SPDL1. Plays a role in the repair of UV-induced DNA damage via deubiquitination of ERCC1, promoting its recruitment to DNA damage sites. May be involved in the maintenance of photoreceptor function. May play a role in normal retinal development (By similarity). Plays a role in cell migration.
Subcellular location: Photoreceptor inner segment {ECO:0000269|PubMed:30573563}. Cytoplasm {ECO:0000269|PubMed:25538220}. Nucleus {ECO:0000269|PubMed:25538220}.
Interaction partners:
- DNA excision repair protein ERCC-1
Sequence:
MRVKDPTKALPEKAKRSKRPTVPHDEDSSDDIAVGLTCQHVSHAISVNHVKRAIAENLWSVCSECLKERRFYDGQLVLTSDIWLCLKCGFQGCGKNSESQHSLKHFKSSRTEPHCIIINLSTWIIWCYECDEKLSTHCNKKVLAQIVDFLQKHASKTQTSAFSRIMKLCEEKCETDEIQKGGKCRNLSVRGITNLGNTCFFNAVMQNLAQTYTLTDLMNEIKESSTKLKIFPSSDSQLDPLVVELSRPGPLTSALFLFLHSMKETEKGPLSPKVLFNQLCQKAPRFKDFQQQDSQELLHYLLDAVRTEETKRIQASILKAFNNPTTKTADDETRKKVKAYGKEGVKMNFIDRIFIGELTSTVMCEECANISTVKDPFIDISLPIIEERVSKPLLWGRMNKYRSLRETDHDRYSGNVTIENIHQPRAAKKHSSSKDKSQLIHDRKCIRKLSSGETVTYQKNENLEMNGDSLMFASLMNSESRLNESPTDDSEKEASHSESNVDADSEPSESESASKQTGLFRSSSGSGVQPDGPLYPLSAGKLLYTKETDSGDKEMAEAISELRLSSTVTGDQDFDRENQPLNISNNLCFLEGKHLRSYSPQNAFQTLSQSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQKYQEETSFAEKKVEGVYTNARKQLLISAVPAVLILHLKRFHQAGLSLRKVNRHVDFPLMLDLAPFCSATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRTPSRKLSEHNTKKKNVPGLKAADNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYERVL
Protein: Myelin basic protein (MBP) (20 kDa microtubule-stabilizing protein) (Myelin A1 protein) (P02687)
Organism: Bos taurus (Bovine)
Function: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity).
Subcellular location: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
Interaction partners:
- Myelin-associated glycoprotein
- Calmodulin-like protein 4
- Myelin proteolipid protein
- Myelin-oligodendrocyte glycoprotein
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Oligodendrocyte transcription factor 2
- Glial fibrillary acidic protein
- EF-hand domain-containing protein
- EF-hand calcium-binding domain-containing protein 11
- CALML5 protein
Sequence:
AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR
Protein: 5'-deoxynucleotidase (EC 3.1.3.89) (Q38DT8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- p-nitrophenylphosphatase, putative
- Uncharacterized protein
Sequence:
MDTIEFLHTVGKLKETMRTGWVETGVHQPESVSDHMYRAALLCMMCPDSSLNRDRLVRMALCHDVGESIIGDISPKMGVPAAEKHKREKEAILHLRGLLPHDSPLEKELQELWEEYETQGTPEARFLRDIDLLEMVTQAHAYEKTHPELNFDSFYVSGEKIKHPWVRSIYDNLVSTRPSRKS
Protein: CXXC-type zinc finger protein 1 (A1A5S2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Retinoblastoma-binding protein 5
- WD repeat-containing protein 82
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Protein dpy-30 homolog
- WD repeat-containing protein 5
- [histone H3]-lysine
- [histone H3]-lysine
- Biorientation of chromosomes in cell division 1-like 1
- Histone-lysine N-methyltransferase PRDM9
- Host cell factor 1
Sequence:
MEGDGSDLEPPDAGEDSKSENGENAPIYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREKDPKLEIRYRHKKCRERDGSERDGSEPRDEGGGRKRPASDPELQRRAGSGTGVGAMLARGSASPHKSSPQPLVATPSQHHQQQQQQQQQQQIKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQCQLRARESYKYFPSSLSPVTPSEALPRPRRPPPTQQQPQQSQKLGRIREDEGTVLSSVVKEPPEATATPEPLSDEDLALDPDLYQDFCAGAFDDHVPWMSDAEESPFLDPALRKRAVKVKHVKRREKKSEKKKEERYKRHRQKQKHKDKWKHPERADAKDPASLPQCLGPGCVRAAQPGSKYCSDDCGMKLAANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEENNENDSDDTDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGATRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVPADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALMLHQTIQHDPLTTDLRSSADR
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q7KQK7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein phosphatase PPM5, putative
Sequence:
MLKKKKDYENADLEDCNTKEIKGYSKVGSEKNIKKKMTSIKESSSRDEEEEDANVNKNIKKFKEGNKKDNISKNCNIVEKKNNKSKEEKINIKEAIIKNVKVPDNYEIKHLIGRGSYGYVYLAYDKNANKNVAIKKVNRMFEDLIDCKRILREITILNRLKSDYIIRLHDLIIPEDLLKFDELYIVLEIADSDLKKLFKTPIFLTEQHVKTILYNLLLGEKFIHESGIIHRDLKPANCLLNQDCSVKICDFGLARTINSDKDIHIVNDLEEKEENEEPGPHNKNLKKQLTSHVVTRWYRAPELILLQENYTNSIDIWSTGCIFAELLNMMKSHINNPTNRFPLFPGSSCFPLSPDHNSKKVHEKSNRDQLNIIFNVIGTPPEEDLKCITKQEVIKYIKLFPTRDGIDLSKKYSSISKEGIDLLESMLRFNAQKRITIDKALSHPYLKDVRKENLENFSTEKIILPFDDWMVLSETQLRYIFLKEIQSFHADLIIPAKLNIHQKSFYNM
Protein: Matrix metalloproteinase 14 (Membrane-inserted) alpha (Matrix metalloproteinase-14a precursor (EC 3.4.24.80)) (Membrane-type matrix metalloproteinase 1 alpha) (Q7T2J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLPKLQTLPRLLPLALASVFLVQSGTSDKEVRPEAWLQQYGYLPPGDVRAQAIRSPKSINSAISAMQKFYGLTVTGTMDPATLSAMQRPRCGVPDKFGSELKSNLRKKRYVAQGSKWDKREVTFSIQNYTPKVGERATHEAIKKAFRVWEAVTPLKFREIPYSQINGKVEKFADIMLFFAEGFHGDSTPFDGEGGFLAHAYFPGHGIGGDTHFDEAEPWTTGNVDKGGNDVFLVAVHELGHALGLEHSGDPSAIMAPFYQWMDTENFVLPEDDRRGIQQIYGAGSEDKPQPPAPRPPTRTPDRPSFGPDICEGHFDTIAFLRGEMFVFKEKWFWRVRDGKPQQGYPMPIGHFWKGLPPSINAAYERNDGKFVFFKGDKYWVFNEAKMEEGYPKTFKELGTGLPRDKLDAAIFYTPTGNTYFFRGTKYYRFNEESRSVDSDYPKDIGVWQGVPDNVKGAFMSEDGANAYFYKANKYWKFNNQQLKVEPGFPKSVLTNWMGCEAEEPKRRAGTDEEVLIIEVDGSEGGAMGGAAAIVIPLFLLACVLVTLGALLFFRRYGTPRRLLYCHRSLLDKV
Protein: Fucolectin-1 (Q9I931)
Organism: Anguilla japonica (Japanese eel)
Function: Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:10924498}.
Interaction partners:
Sequence:
MKVKTIMLLFQILAISTIKSADVPNRYIQENVAVRGKATQSTLPSGAGAVLSLPGFAIDGNRDSDFSHGSCSHTTNSPNPWWRVDLLQLYTITSVTITNRGDCCGERISGARILIGNSLENNGINNPACSVIGSMETGETRTFHCPQPMIGRYVTVYLPKTEVLQLCEVEVNALLPVN
Protein: CFTR inhibitory factor, Cif (Q9HZR3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- CifR
- Morphinone reductase
- Probable epoxide hydrolase
- Hemolytic phospholipase C
- Probable major facilitator superfamily
Sequence:
MILDRLCRGLLAGIALTFSLGGFAAEEFPVPNGFESAYREVDGVKLHYVKGGQGPLVMLVHGFGQTWYEWHQLMPELAKRFTVIAPDLPGLGQSEPPKTGYSGEQVAVYLHKLARQFSPDRPFDLVAHDIGIWNTYPMVVKNQADIARLVYMEAPIPDARIYRFPAFTAQGESLVWHFSFFAADDRLAETLIAGKERFFLEHFIKSHSSNTEVFSERLLDLYARSYAKPHSLNASFEYYRALNESVRQNAELAKTRLQMPTMTLAGGGHGGMGTFQLEQMKAYADDVEGHVLPGCGHWLPEECAAPMNRLVIDFLSRGR
Protein: Flavin-containing monooxygenase FMO GS-OX-like 7 (EC 1.8.-.-) (Flavin-monooxygenase glucosinolate S-oxygenase-like 7) (Q9SXD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates.
Interaction partners:
- Protein trichome birefringence-like 11
- At2g44720/F16B22.21 family protein)
- BTB/POZ domain-containing protein At4g01160
- Diacylglycerol kinase 4
- Phytosulfokine receptor 1
Sequence:
MVPAVNPPTTSNHVAVIGAGAAGLVAARELRREGHSVVVFERGNHIGGVWAYTPNVEPDPLSIDPTRPVIHSSLYSSLRTIIPQECMGFTDFPFSTRLENGSRDPRRHPGHSEVLAYLRDFVREFKIEEMIRFETEVVRVEQAGENPKKWRVKSRNFGDISDEIYDAVVVCNGHYTEPRHALIPGIDTWPGKQIHSHNYRVPEQVKDQVVVVIGSSVSGVDISRDIANVTKEVHISSRSTKPETYEKLPGYDNLWLHSNIETVREDGSVVFKNGKTVYADTIMHCTGYKYYFPFLDTKGEVTVEDNRVGPLYKHVFPPALSPGLSFIGLPWQVIPFPMFELQSKWVAAVLAGRVSLPSQEEMEDTKMFYLKLEASCIPKRYTHLMAELDSQFVYNNWLADQCDYPRIEKWREQMFYKVFKRIQSQASTYKDDWDDDHLIAEAYEDFVKFPSNYPSSLIEREYTS
Protein: Small ribosomal subunit protein mS47 (3-hydroxyisobutyryl-CoA hydrolase-like protein 2, mitochondrial) (EC 3.1.2.-) (Q8RXN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000303|PubMed:36423343, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Probable enoyl-CoA hydratase 1, peroxisomal
- Small ribosomal subunit protein mS29
- At1g64880
- 50S ribosomal protein L33
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL29m
- Uncharacterized protein
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein uS2m
Sequence:
MQTVKALRRVSEPLQWVRSVSYGRRFSALPNYSASDADFEDQVLVEGKAKSRAAILNNPSSLNALSAPMVGRLKRLYESWEENPAISFVLMKGSGKTFCSGADVLSLYHSINEGNTEESKLFFENLYKFVYLQGTYLKPNIAIMDGVTMGCGGGISLPGMFRVATDKTVLAHPEVQIGFHPDAGASYYLSRLPGYLGEYLALTGQKLNGVEMIACGLATHYCLNARLPLIEERIGKLLTDDPAVIEDSLAQYGDLVYPDSSSVLHKIELIDKYFGLDTVEEIIEAMENEAANSCNEWCKKTLKQIKEASPLSLKITLQSIREGRFQTLDQCLTHEYRISICGVSKVVSGDFCEGIRARLVDKDFAPKWDPPRLEDVSKDMVDCYFTPASELDDSDSELKLPTAQREPYF
Protein: TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II) (P37173)
Organism: Homo sapiens (Human)
Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and thus regulates a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1310899, ECO:0000269|PubMed:25893292}; Single-pass type I membrane protein {ECO:0000269|PubMed:1310899}. Membrane raft {ECO:0000269|PubMed:25893292}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:34568316}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-2 proprotein
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Endoglin
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 7
- Activin receptor type-1-like
Sequence:
MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK
Protein: Nucleolar protein 5, putative (Q8IJV7)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 2
- rRNA 2'-O-methyltransferase fibrillarin
- U3 small nucleolar RNA-associated protein 20 C-terminal domain-containing protein
- rRNA biogenesis protein RRP5, putative
- U3 small nucleolar RNA-associated protein 12, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- Periodic tryptophan protein 2, putative
- U3 small nucleolar RNA-associated protein 4, putative
- KRR1 small subunit processome component
Sequence:
MLILVETAAGYGLFKVENSKLIESDVKDIEKCFVTSEEARKNVSLYSFSKFKKFQNAFDETNKLMESKLGKGLKKFLKKNIIKPKLNEPLALCDKTLGGLIKKKYNINVTYTNSTQEIIRGIRTHLYELLVGVNEEDSKLLKLSLSHSLNRFKLKFSADKVDVMIVQAVGLLEDLDKEINVFSMRLKEWYGWHFPELGKVITDNKIYAKCVKLIGFRNNAKNVNLLEETTEEIQKEIKQLAEISMGTEIEDDDLNCINELADRLLELTDYRESLATYLKYRMNSIAPNLTYLVGDLVGAKLIAKAGSLMSLAKHPSSTLQILGSEKALFRALKTKSKTPKYGLIYHATLVGQTAPKLKGRISRSLAAKLSLCTRVDALGNFVEPSIAITCKSHLEKRLEYITSNLQKKLSNPNNNVKAQQQGQQNKYNPNQKNDGQNNFNSFNKRKSDFRFKREADKNNKKFIKKQKRK
Protein: Probable proline--tRNA ligase, mitochondrial (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) (O74765)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Isoleucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Lysine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Glutamate--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
- Probable glutamate--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, mitochondrial
- Putative leucine--tRNA ligase, cytoplasmic
Sequence:
MLQHLRNRASIEVLGKAIRKYNVPESANQLLIDMGFIQPSMPGIFQYLPLGLRVQNKICDLLHISMRSLGASAISLAHLSSKEIWEKSGRWQKTGSELFRLHDRNDREMCLAPTHEEDVTRTMATIIDSQKQLPIRVYQIGRKFRDELRPRGGLLRGREFMMKDLYTFDIDKASAMKTYEDVLQAYHTFFKEVGLPFVMVKAATGNIGGNLSHEFHYRHPVGEDVIYTCPSCHYSTNSEMLDLSKTSSDISCPNCNDQLTSTTAIEVGHAFYLGKIYSSKFNATVEVKNKQEVLHMGCYGIGVSRLIAAVAHVTKDAKGLVWPSSIAPWKVLVVPTSDNHIQSAETVYDATANVVGFDNVLLEDRQNRAFGYKMRDAELIGYPFVIVVGSRFQEEGICEIIVRSSGERYKLDKDSLHQVLLGNFL
Protein: Proteasome subunit alpha type-3 (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit alpha-7) (alpha-7) (P25788)
Organism: Homo sapiens (Human)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
- Proteasome maturation protein
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit beta type-9
- 26S proteasome regulatory subunit 4
- Proteasome subunit beta type-8
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit beta type-2
Sequence:
MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
Protein: Protein MBD-R2 (Q9VGA4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:20620954}. Chromosome {ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:20620954}. Note=Associates with promoters of housekeeping genes on X chromosome and autosomes genes. {ECO:0000269|PubMed:20620953}.
Interaction partners:
- GH01794p
- Reduction in Cnn dots 1, isoform E
- Paired amphipathic helix protein Sin3a
- F-box-like/WD repeat-containing protein ebi
- KAT8 regulatory NSL complex subunit 2
- Protein will die slowly
- Histone acetyltransferase MOF
- Non-specific lethal 1, isoform M
- Protein male-specific lethal-3
- Chromatin assembly factor 1 p55 subunit
Sequence:
MGRRCCVANCPSTSRLLEHNGVTYHSFPLDPIIRAIWIKNSRISLERQITKSVLVCSRHFRRLDFNTIRNGKYLLKPRVFPTVFPWGKMDTAEIEADQRALQHASVEGTTETPGNAQSSTNDDVIKATVDQIVAQILSESAERKATEEGKTGKAADDVKNTPESGEDANKAAAKEPSGTPVAASSEATVPAPGSASSSNSPLPGTPPKYSNPHNLTIGARLEALSVEGNWLPARIVEVNETEQTLLVRFERNHKLKVSPSTSGSFQEWMAIKSERLRQRLSNRVLPVFELDEKCMARWSGPRKFPGTIRKLLGNDTYEVLFDDGYVKNVRAVHMNKMPKQLPPVQVAEEGASKSPTPVGTPVSSAPVAPKRASTGSLGGSSGSSGSKKSKCAPQRRDWPLLDMASLDIASLGLPEIPHDGEWTCHWVNDQPIGTEGFLIVGEHQKPTVIVQDWRLPPGWIKHMYQRSNVLGKWDVILVSPSGKRFRSKSDLKLFLESQNLVYNPDVYDFSIHRRRAKDINAYVYTHGYNPQPPPKPRPMDVSMNSTLDQSITSQHSLPSTPMPVKESQYMEAPVASLMPPAELMSPQTQPADETKPKIEAEILEASEGGTSQLMLADPHVVENGFAFIGGLKVKIQDNLYVCPREDCAKTYRKEDFLLIHIRHYHKEFAEHVSHCPKMQELAVKRTHPSSIDQVEAVPKNQIPNQQFFAKMHQQDLQQSRSFKRQSVSATATSSTPSDITPTKALLSPKMEPPSVSPTVESGIKQEDVSLDAGPTQSFNPSLSRSCKRARLSPSKRPSGSRKSNRQRSQRRPILSDNPAGHGLTEQDVEETRQSFNTPTPDTRIDSKKRRSGAATTPISSIDSPAMGDSVSTPSSNDQTDINAALAPPPAETLSKAPQYIKENGELIRIVRMRQEEIINCICEYGEEDGLMIQCELCLCWQHGACNGIVKEADVPDKYVCYICRNPQRGRDSMRFKHDQDWLFEGKLPVAAYHTANPQATKQFELLKRSHTLTGNLLDAKRSMHSLLVKINIARNRCHPKLYLWAKKWDEDNLDSTALTPVKRAKLEAPDLPNVPQPEAAIDPEECQYRLIEHIKVQQSLVLDRLNDIEAEMDELEKEDTLDDLKDADISTTKEALATFIKELETMKRLAKLNQVANMKQTLRDSATSK
Protein: Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269) (Copper homeostasis protein CutE) (P23930)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA) or cardiolipin (CL). PE is the most efficient acyl donor.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:15513925, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2032623, ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:15513925, ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614}.
Interaction partners:
- Lipoprotein signal peptidase
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- Magnesium and cobalt efflux protein CorC
- PhoH-like protein
- Lipoprotein-releasing system transmembrane protein LolC
- Outer-membrane lipoprotein carrier protein
- Outer-membrane lipoprotein LolB
- Lipoprotein-releasing system transmembrane protein LolE
- Major outer membrane lipoprotein Lpp
- Signal peptidase I
Sequence:
MAFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSFSRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTGNWPLWVLTALFGFAAVLMSLRQRRK
Protein: Small ribosomal subunit protein uS11c (30S ribosomal protein S11, chloroplastic) (P56802)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS8c
- Small ribosomal subunit protein uS4c
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS7cz/uS7cy
- At1g64880
- Small ribosomal subunit protein bS18c
- Small ribosomal subunit protein uS3c
- Small ribosomal subunit protein uS17c
Sequence:
MAKPILRIGSRKNTRSGSRKNVRRIPKGVIHVQASFNNTIVTVTDVRGRVISWSSAGTCGFRGTRRGTPFAAQTAAGNAIRAVVDQGMQRAEVRIKGPGLGRDAALRAIRRSGILLSFVRDVTPMPHNGCRPPKKRRV
Protein: Uroporphyrinogen-III synthase (UROIIIS) (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) (P10746)
Organism: Homo sapiens (Human)
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P51163}.
Interaction partners:
- Porphobilinogen deaminase
- Uroporphyrinogen decarboxylase
- Delta-aminolevulinic acid dehydratase
- BRCA2 and CDKN1A-interacting protein
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Ferrochelatase, mitochondrial
- Protoporphyrinogen oxidase
- Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32
- Endonuclease V
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLIFTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCGNAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNLNSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVSCTAESPTPQALATGIRKALQPHGCC
Protein: Large ribosomal subunit protein uL18 (50S ribosomal protein L18) (P0C018)
Organism: Escherichia coli (strain K12)
Function: This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Interaction partners:
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL29
- Protein translocase subunit SecY
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS19
Sequence:
MDKKSARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAIAEQLKYTGNKDAAAAVGKAVAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF