wanglab/gogpt-training-data huggingface dataset:
Protein: Formyltransferase/hydrolase complex Fhc subunit A (Ftr complex) (EC 3.5.1.-) (C5B137)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR). May be catalyze the hydrolysis of formylmethanofuran (formyl-MFR) to yield formate and MFR.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Formyltransferase/hydrolase complex Fhc subunit C
- Formyltransferase/hydrolase complex subunit D
- Formyltransferase/hydrolase complex Fhc subunit B
- Methenyltetrahydromethanopterin cyclohydrolase
- NAD
- 5,6,7,8-tetrahydromethanopterin hydro-lyase
- Bifunctional protein MdtA
- 
- Tetrahydromethanopterin synthesis protein
- Glutamate synthase large chain
Sequence:
MLTRIHGGRVVDPTAGRDAVGDVWIEDGRVVAPSERAPDQTIDATGCVVMAGGVEVHSHIAGGNVVMSRLLLPDLYVSESAPNGHPFAHAGGSGSWIGANYARMGYTTAVEPALPPSNALATHLELADIPLLDRGGLAVLGNDDHLLQLLRDGEGKQAVRDLVQQTLAHSRGLGVKCINAGGASAFKDGVLKLSLDDEIPCYGLSTRKIMSALLDAVEEIGVPHPLHVHCNNLGLPGADDSLVATLEAAEGRRIHFAHAQFYAYGVVDPENPMTGGFRSAAERINAAMEAHPNATYDVGQVVFGQTVTISLDILRQFGGRKGAKPKKWVISAGDAEGGGVVPFLYRPRGPVSSLQWAIGLELMLLSSNPERTILTTDHPNGGVFTEYPRIIHLLMDAEERAKEIATLPAIVGERSGLPKIEREYSFSEIAQLTRSGPAKLLGLTDRGHLREGAKADVAIYRDDKDRTAMFSRAKLVLKDGQPIVEDGEVVAWFSGKTLSLDVEADAGMEKRAESYLQDRFGAGLDTFAVPDAAFPENTGTFEDVACRA
Protein: Lactase/phlorizin hydrolase (Lactase/glycosylceramidase) [Includes: Lactase (EC 3.2.1.108); Glycosylceramidase (EC 3.2.1.62) (Phlorizin hydrolase)] (P09848)
Organism: Homo sapiens (Human)
Function: Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:9593732}; Single-pass type I membrane protein {ECO:0000305|PubMed:9593732}. Note=Brush border. {ECO:0000250|UniProtKB:P09849}.
Interaction partners:
- Beta-galactosidase
- Galactose mutarotase
- Alpha-galactosidase A
- Alpha-lactalbumin
- Glucose-6-phosphatase catalytic subunit 1
- Hexokinase HKDC1
- Aldo-keto reductase family 1 member B1
- Aldo-keto reductase family 1 member B10
- Hexokinase-2
- Hexokinase-4
Sequence:
MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKDMYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKALKTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIKELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQDTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSLFEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQRIWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTTEGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKLIDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTFHEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIVLNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPVAQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQTSSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYINEVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTSIIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYHGTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLDADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFHWDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFPPGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDVEAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRATADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWIKEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMDNFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEGFIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQNLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTLQDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRPGTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRYVQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGFNHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEYNDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEWATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTISPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQELSPVSSF
Protein: Aqp8a protein (Aquaporin 8) (Aquaporin 8a, tandem duplicate 1) (Aquaporin-8a.1) (Q66I64)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin
- Aquaporin 7
- Aquaporin
- Aquaporin-10b
- Uncharacterized protein.
- Inactive rhomboid protein 1
- Leucine carboxyl methyltransferase 1
- Inactive rhomboid protein
- Aquaporin-3
- Aquaporin 9b
Sequence:
MTSAESKSELFTVATGDGGDNHQNQPKKLPFFEHYIQPCLAEVVGSFLFMFVGCVSVMGNVGISGSIQPALAHGLALAIAIAIFGEISGGHFNPAVSVCVYLIGGMEVILLVPYIISQMLGGVIAASLAKAVTTNDAFSNATGAAFNAIPSSDGIGAATMAEMIMTLFLTIVVSMGAVNGRTKSQLAPFCIGLTVTANILAGGGISGACMNPARAFGPAVVSGHWTHHWIYWVGPLTGALVTVSIVRLVMGDKKVRVIFK
Protein: GTPase, IMAP family member 2, isoform CRA_c (Immunity associated protein 2) (A0A090N8H4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDQNEHSHWGPHAKGQCASRSELRIILVGKTGTGKSAAGNSILRKQAFESKLGSQTLTKTCSKSQGSWGNREIVIIDTPDMFSWKDHCEALYKEVQRCYLLSAPGPHVLLLVTQLGRYTSQDQQAAQRVKEIFGEDAMGHTIVLFTHKEDLNGGSLMDYMHDSDNKALSKLVAACGGRICAFNNRAEGSNQDDQVKELMDCIEDLLMEKNGDHYTNGLYSLIQRSKCGPVGSDERVKEFKQSLIKYMETQRSYTALAEANCLKGALIKTQLCVLFCIQLFLRLIILWLCILHSMCNLFCCLLFSMCNLFCSLLFIIPKKLMIFLRTVIRLERKTPRL
Protein: Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha-1,4-N-acetylglucosaminyltransferase) (Alpha-1,4-galactosyltransferase) (Alpha4Gal-T1) (CD77 synthase) (Globotriaosylceramide synthase) (Gb3 synthase) (P1/Pk synthase) (UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase) (Q9NPC4)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of galactose from UDP-alpha-D-galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside Gb3Cer (d18:1(4E)). Also able to transfer galactose to galactosylceramide/beta-D-Gal-(1<->1')-Cer. Globoside Gb3Cer is a glycosphingolipid of the globo serie, one of the major types of neutral root structures of glycosphingolipids, that constitute a significant portion of mammalian cell membranes (Probable). Globotriaosylceramide/globoside Gb3Cer in blood and tissue cell membranes is the antigen Pk of blood histogroup P.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
- Alpha-galactosidase A
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 6
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
- Beta-1,3-galactosyltransferase 4
Sequence:
MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIPCPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGGNASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRIALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDHYNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDINPEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL
Protein: Protein LRATD1 (LRAT domain-containing 1) (Neurologic sensory protein 1) (NSE1) (Protein FAM84A) (Q96KN4)
Organism: Homo sapiens (Human)
Function: May play a role in cell morphology and motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16820875}.
Interaction partners:
Sequence:
MGNQLDRITHLNYSELPTGDPSGIEKDELRVGVAYFFSDDEEDLDERGQPDKFGVKAPPGCTPCPESPSRHHHHLLHQLVLNETQFSAFRGQECIFSKVSGGPQGADLSVYAVTALPALCEPGDLLELLWLQPAPEPPAPAPHWAVYVGGGQIIHLHQGEIRQDSLYEAGAANVGRVVNSWYRYRPLVAELVVQNACGHLGLKSEEICWTNSESFAAWCRFGKREFKAGGEVPAGTQPPQQQYYLKVHLGENKVHTARFHSLEDLIREKRRIDASGRLRVLQELADLVDDKE
Protein: RNA editing complex protein MP46 (Q386L2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- REH2-associated factor 2
- RNA-editing ligase 1, mitochondrial
- RNA editing associated helicase 2
- RNA editing complex protein MP63
- RNA editing complex protein
- MP18 RNA editing complex protein
- REH2-associated factor 1
- RNA editing 3' exouridylylase MP99
- RNA editing complex protein MP67
- RNA editing complex protein MP61
Sequence:
MLRVENLRRSMTRLARHSLIRAVPFSPLSVGSSTDQTFGAPTRTPFRSHTCLLCDVSYESWGDHAESTTHIARHAICRTFVSPERHNAVMQQLWKHIRLDFGYVDEVTHKKEDRRRMRLASTMRHLQEKGVLHHSLPRVTVDAQSEVSLTVESDSFVNYMFLGESFARQETLDRVARLMPRAEALELSSIISFVLSKRRLAHFFDILDMRKMVLNGDSSDDKASADGGVPPTIPRLQQDGKAVILFSCLGELQMFSRRDRSHSVATRSAAEQLVLNVLGTHVMENIIGELVHEALQTVVEEGTAVWREHCGELKHKLFEGTKAVSPPIATTPNPVSNSGGPEVTADVNDQMWVDLCRLYVLDKNGSVPQLQPTVKRHSWHDVARALTLELTVPNPVNKSAVFAAAAPRLATKKK
Protein: Vacuolar protein sorting-associated protein 52 (Suppressor of actin mutation protein 2) (P39904)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. May also be involved in the actin cytoskeleton organization.
Subcellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Interaction partners:
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 51
- GTP-binding protein YPT6
- t-SNARE affecting a late Golgi compartment protein 1
- t-SNARE affecting a late Golgi compartment protein 2
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 4
Sequence:
MDVLKEVLSLDQDKFDQLKETSRDKTNETDDPFENYLKDCKFKAPSNKDQSPFAKLKSLQETHSNNEAAINIIIPQLIDYLTEFTNRLSNYTQDLDFIKKKSNELQSLLEYNSTKLAHISPMVNDLMIPPELIDDIIKGKINESWQDNITFIADKEEIYNKYRSNNLDQDNKDAENSAMLAPKDFDKLCQLLDILKNVILERSKRLIISKIKTLRSHNPVPSQRIQNKLLKVQKIFPFIRDNNLSLALELRQAYCYTMKWYYREYFSRYIRSLTILQFQQIDSQFALGNGLSTTSVSGFNNSPSLFFSNYLTTSASNAFYNKLPVTDEKIDKYFQIKKRLNILTQEDNTVMVSQIAENNTTKNYIEIGFKNLNLAILDNCTVEYHFLKDFFAMNGDNFEEINGLLEQIFQPTFDEATTYTQQLIQYNYDIFGVLISIRVANQLQFESERRGIPSMFDSFLNGQLIQLWPRFQQLVDFQCESLRKAAITTNVAKYAGNSSTSNSSPLTSPHELTVQFGKFLSSFLTLAITHKQSIDERSEPLYNSIIRLRNDFETVMTKCSKKTKSPERFLATNYMYLYNNLQQLHLHLNINDSDAQNYNFDSAENVGTKVANDDDNDSSVPLIIRETENHFKTLVEAFTRN
Protein: Dehydrin DHN1 (M3) (RAB-17 protein) (P12950)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MEYGQQGQRGHGRTGHVDQYGNPVGGVEHGTGGMRHGTGTTGGMGQLGEHGGAGMGGGQFQPAREEHKTGGILHRSGSSSSSSSEDDGMGGRRKKGIKEKIKEKLPGGHKDDQHATATTGGAYGQQGHTGSAYGQQGHTGGAYATGTEGTGEKKGIMDKIKEKLPGQH
Protein: Forkhead box protein P3 (Scurfin) [Cleaved into: Forkhead box protein P3, C-terminally processed; Forkhead box protein P3 41 kDa form] (Q9BZS1)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2. Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7. Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1. Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development. Inhibits the transcriptional activator activity of RORA. Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:22678915, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:32644293}. Cytoplasm {ECO:0000269|PubMed:22678915}. Note=Predominantly expressed in the cytoplasm in activated conventional T-cells whereas predominantly expressed in the nucleus in regulatory T-cells (Treg). The 41 kDa form derived by proteolytic processing is found exclusively in the chromatin fraction of activated Treg cells (By similarity). {ECO:0000250|UniProtKB:Q99JB6, ECO:0000269|PubMed:22678915}.
Interaction partners:
- Runt-related transcription factor 1
- Nuclear factor of activated T-cells, cytoplasmic 2
- Histone acetyltransferase KAT5
- Interleukin-2
- Hypoxia-inducible factor 1-alpha
- Nuclear receptor ROR-gamma
- Signal transducer and activator of transcription 3
- Interferon gamma
- T-cell surface glycoprotein CD4
- Cytotoxic T-lymphocyte protein 4
Sequence:
MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGPVVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP
Protein: Small ribosomal subunit protein eS26x (40S ribosomal protein S26-3) (Q9LYK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS10y
- Small ribosomal subunit protein uS4z
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS1z
Sequence:
MTFKRRNGGRNKHNRGHVKPIRCSNCGKCCPKDKAIKRFIVRNIVEQAAIRDVQEASVYEGYTLPKLYAKTQYCVSCAIHSHVVRVRSRTNRRVRTPPPRFARRKEDTPKPAQPGQAPRPAGGAPAAPRA
Protein: UPF0656 protein C926.02 (Q9UUG6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone transcription regulator slm9
- Histone promoter control protein 2
- Protein hir1
- Histone transcription regulator 3 homolog
Sequence:
MSFSRNQVLKGLKTKKAKPKKNPTVDELFEIAIDLEESGDRWRLEPAKCLRFYQKSLETYDRYLLQCPNDFDARFNKARLLLNMATNCDMLYKDSQVCLQKSIEMHKHALLLQEAPDIWFNLAQVHLNLAEIWVDLDREDLAYPEIQQALQSISHSIDLQERERIEWENTIQTSSQQKYEEIPDIQARRLYFIEADKEASTLVTEIASLACSCKLLEESDFEKLCQIMLPITEKLDILKLMDWYLAKTKRLVLGGKENEVAWIDLLQVFDHQLSQLPQLNLQNPLDPNSSVKPLHIQLLCDKADAYIDFAETLLDSCVSTEESASIEIMTRAWNMLGVAAKSLKMANTYNPNHVRILISRADLEIQRAAIPIMVAQNSKLVLYKNAKVLYEKAFRDYSTKKTTRTFAEIVLKHYQLQKLTNPETIKMLDSLTEVAQEDILNTI
Protein: Anaphase-promoting complex subunit 11 (APC11) (Cyclosome subunit 11) (Hepatocellular carcinoma-associated RING finger protein) (Q9NYG5)
Organism: Homo sapiens (Human)
Function: Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11573242}. Nucleus {ECO:0000269|PubMed:11573242}.
Interaction partners:
- Anaphase-promoting complex subunit 5
- Ubiquitin-conjugating enzyme E2 C
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 20 homolog
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
- Ubiquitin-conjugating enzyme E2 S
- Cell division cycle protein 23 homolog
- Cell division cycle protein 27 homolog
Sequence:
MKVKIKCWNGVATWLWVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE
Protein: Glutamate-1-semialdehyde 2,1-aminomutase (GSA) (EC 5.4.3.8) (Glutamate-1-semialdehyde aminotransferase) (GSA-AT) (Q725I1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
Interaction partners:
- Glutamyl-tRNA reductase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- Spore coat polysaccharide biosynthesis protein spsF
- uroporphyrinogen-III C-methyltransferase
- precorrin-2 dehydrogenase
- Malonyl CoA-acyl carrier protein transacylase
- Aromatic amino acid decarboxylase, putative
Sequence:
MSQRSSELFERAQQLIPGGVNSPVRACLGVDSEPLFIARAAGSRLHTVDGETFIDFVESWGPMLLGHTHPEVTAAVHAAVDRGTSYGAPCEDEVVLAAKVVDALPGVDMVRMVNSGTEATMSALRLARGYTGRTKLVKFVGCYHGHADPFLASAGSGVATLSIPGTPGVPESTVRDTLLAPYNDLAAVKDLFALHGKDIAAIIVEAVAGNMGLVPPKAGFLEGLRELCDQHGALLIFDEVITGFRVSFGGAQQRFGITPDLTTLGKIIGGGLPVGAYGGKREIMQRIAPCGEVYQAGTLSGNPLAMAAGIATLDVLSRSDYAGLEARVAAFVKELEAILKGKGVPVRINTLASMFTVFFTNDPVTDFASAKTADGALYTSFYKQMRAQGIYLAPSPFEAAMVSFAHTDDDLAAMLDAARKVTF
Protein: Thiocyanate methyltransferase 1 (EC 2.1.1.n4) (Q93V78)
Organism: Brassica oleracea (Wild cabbage)
Function: S-adenosyl-L-methionine-dependent methyltransferase. Probably involved in glucosinolate metabolism and defense against phytopathogens. Highly reactive to thiocyanate (NCS(-)) derived from myrosinase-mediated hydrolysis of glucosinolates upon tissue damage. Also accepts halid ions as substrates with a lower affinity.
Interaction partners:
Sequence:
MAEEQQKAGHSNGENIIPPEEVAKFLPETVEEGGWEKCWEDGITPWDQGRATPLVVHLVDSSSLPLGRALVPGCGGGHDVVAMASPERFVVGLDISESALEKAAETYGSSPKAKYFTFVKEDFFTWRPNELFDLIFDYVVFCAIEPEMRPAWAKSMYELLKPDGELITLMYPITDHDGGPPYKVAVSTYEDVLVPVGFKAVSIEENPYSIATRKGKEKLGRWKKIN
Protein: Portal protein (Connector protein) (Gene product 10) (gp10) (Gene product 19) (gp19) (Head-to-tail connector) (Probable portal protein) (Protein p10) (Upper collar protein) (P04332)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the 6 packaging RNA molecules (pRNA) forming a double-ring structure which in turn binds to the ATPase gp16 hexamer, forming the active DNA-translocating motor. This complex is essential for the specificity of packaging from the left DNA end.
Subcellular location: Virion {ECO:0000269|PubMed:11562162}. Note=Present in 12 copies in the virion. {ECO:0000269|PubMed:11562162, ECO:0000269|PubMed:11812138}.
Interaction partners:
Sequence:
MARKRSNTYRSINEIQRQKRNRWFIHYLNYLQSLAYQLFEWENLPPTINPSFLEKSIHQFGYVGFYKDPVISYIACNGALSGQRDVYNQATVFRAASPVYQKEFKLYNYRDMKEEDMGVVIYNNDMAFPTTPTLELFAAELAELKEIISVNQNAQKTPVLIRANDNNQLSLKQVYNQYEGNAPVIFAHEALDSDSIEVFKTDAPYVVDKLNAQKNAVWNEMMTFLGIKNANLEKKERMVTDEVSSNDEQIESSGTVFLKSREEACEKINELYGLNVKVKFRYDIVEQMRRELQQIENVSRGTSDGETNE
Protein: Myosin-2 essential light chain (Myosin II essential light chain) (Non-muscle myosin essential light chain) (P54357)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myosin regulatory light chain sqh
- Myosin heavy chain, non-muscle
- Dilute class unconventional myosin, isoform C
- Myosin regulatory light chain 2
- MIP03207p
- Myosin heavy chain 95F
- Myosin-VIIa
- Myosin heavy chain, muscle
- Myosin heavy chain-like, isoform B
- Myosin light chain alkali
Sequence:
MAAYTEDQLAEFQEAFNLFDNRGDGKIQLSQVGECLRALGQNPTESDVKKCTHQLKPDERISFEVFLPIYQAISKARSGDTADDFIEGLRHFDKDASGYISSAELRHLLTTLGEKLTDEEVEQLLANMEDQQGNINYEEFVRMVMSG
Protein: Glycoprotein 3-alpha-L-fucosyltransferase A (EC 2.4.1.214) (Core alpha-(1,3)-fucosyltransferase) (Fuc-T C3) (FucT1) (FucTA) (Fucosyltransferase 11) (AtFUT11) (Q9LJK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cell wall synthesis (Probable). Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the first GlcNAc residue next to the peptide chains in N-glycans.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Beta-1,2-xylosyltransferase
- Beta-1,3-galactosyltransferase GALT1
- Beta-hexosaminidase 3
- Beta-hexosaminidase 1
- Beta-hexosaminidase 2
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-mannosidase 2
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Putative fucosyltransferase-like protein
- Dol-P-Man:Man
Sequence:
MGVFSNLRGPKIGLTHEELPVVANGSTSSSSSPSSFKRKVSTFLPICVALVVIIEIGFLCRLDNASLVDTLTHFFTKSSSDLKVGSGIEKCQEWLERVDSVTYSRDFTKDPIFISGSNKDFKSCSVDCVMGFTSDKKPDAAFGLSHQPGTLSIIRSMESAQYYQENNLAQARRKGYDIVMTTSLSSDVPVGYFSWAEYDIMAPVQPKTEKALAAAFISNCAARNFRLQALEALMKTNVKIDSYGGCHRNRDGSVEKVEALKHYKFSLAFENTNEEDYVTEKFFQSLVAGSVPVVVGAPNIEEFAPSPDSFLHIKQMDDVKAVAKKMKYLADNPDAYNQTLRWKHEGPSDSFKALIDMAAVHSSCRLCIFVATRIREQEEKSPEFKRRPCKCTRGSETVYHLYVRERGRFDMESIFLKDGNLTLEALESAVLAKFMSLRYEPIWKKERPASLRGDGKLRVHGIYPIGLTQRQALYNFKFEGNSSLSTHIQRNPCPKFEVVFV
Protein: Aldehyde dehydrogenase (Q583M9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acetyl-coenzyme A synthetase
- Enoyl-CoA hydratase/Enoyl-CoA isomerase/3-hydroxyacyl-CoA dehydrogenase, putative
- Acylphosphatase
- glutamine synthetase
- NAD-specific glutamate dehydrogenase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Serine/threonine-protein phosphatase 2A activator
- Multifunctional fusion protein
- AAA+ ATPase domain-containing protein
- Peroxin 19
Sequence:
MPAGVPENTSLENIPTIVSKCREAFNNDANRDLKKRKQVLRSLLNLVEENTDEFCKAIHRDRRRHRDETVVMEILPLRNEVWHLIEHMDEYVKPVKPTMEGAAALDDCELQYEPLGVVLVIGTWNYPLLLILQPLLGALAAGNTAVIKPSELAPATAELLTKLLPKYVSSDVVGIVNGGVSETTAVLKERFDHILYTGSARVAEIVMAAAAKHLTPVTLELGGKSPVVVDDSCADNMKVVAERIMWGKIINAGQTCIAPDYVVVEKSMESVLVDALAEARKAMLGDKFLKVLKGELLVKQKQQFLEESDYPRIVNASHFHRLMEFMKGGKVAVGGEADEATLTIAPTILTDIDPTHPVMQEEIFGPILPVLTYENEKDILKIINSREKPLALYVFSNNKRFIRGVESRTSSGAVVVNDVVVHAGADGLPFGGVGRSGMGAYHGRYSFETFSHRRPVMRRGFFFSSIDTVRFPPYTTAKSRVLNSLLKPSAEVAGAVGRSVWGVAALARVVEVGYHYMRFLMAGETTPAPSSSEPFSKGPRSNE