wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein C3H8.04 (Q10140)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MPACYCATSTSLENNELLYKNIRNLFSTSRSFPIEQEWMNLKSISQMKDFFSNFPGNSKANNHFLCNSPLKFEIFNNEKSVKPSNGPHLFTRCSCRCNKLLSGDYITQQQPIDASAEHSLNAKGINTYSLKNCFQRSGFIGSYEESLFSGHMPYCSSVPFEFSIEIGVISFCRCKPSLVFPPHLKINFVAYSLVGNVDNVQFPYIGRFRLRSQKSDKVMNKGYPFGYRIPSVGQLQLILRQTNGLVIKVFLVPYNVSSMVDCSKTWIRQKHYLQQLDDKSGKILSHLKFGLQLQIICTSAGHHYLYDSQRIIFVQQSLGGLYGNTKIVNETLLSESCR
Protein: SWI/SNF complex subunit SMARCC1 isoform X1 (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily c, member 1a) (F1Q9K1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1-A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- Brahma protein-like protein 1
- PHD finger protein 10
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Protein polybromo-1
- AT-rich interactive domain 2
- AT-rich interactive domain 1B
- Bromodomain-containing 7
Sequence:
MATAATAAGGTGSGGPSAGQTGAGSSIGRKKDGGPSSKYWESSETVSQLETVRLWIGKHYKKHVQTDSPTSKTLAALVVQLLQFQEDAFGRRVSNPALTKLPAKSFLDFKPGGALCHILGSAYKFKSEQGWRRFDLQNPSRMDRNVEMFMTIEKTLVQNNSLTRPIVYIVSDVEQKQANKLKDIIKRHQGTITEDKSKATHIIYPSPTQMEEEEWLRPVMRKDKQVLVHWGYYPDSYDIWVSTSDVDADVEDPPSSEKPWRVHAKWVIDTDAFNEWMNEEDYEVDENKKPVSFRQRIFPGEDVSSRTPDRKERKSLVAGKKRRRSPSPPSTPVESRKKGKKGNPGSQWRRRGQPIDDEQDEDSTKDLEDPSPVPGMEEVTLPKNVNQKKDSENTPVKGGIHNDLDDQEDDSVTSGGKEDDEQSKAEVNRLIDSEDNVTEQTHHIIIPSYAAWFDYNSIHEIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTSCRRNLTGDVCAVMRVHAFLEQWGLVNYQVDAESRPLPMGPPPTSHFNVLADTPSGLVPLHHRPPQVPPAQQMLNFPEKGKDKPTDLQNFGLRTDIYSKKNLKGKGAAGGRDWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDQYLESSDASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVAAAAAKAALDEFSRVREEVPAELVEAHVKKVQEAARSTGKVDPAFGLESSGIAGTAPEEPEKTEPTETEKMDTDSDSQQPDKAESKDEAEKPSESAEKPAETEKEKIETTEKSEPQEEEESEAGETKTAEKEKEEAMETTEEGKEDEEEQEEGKKKLELDIGEGNIATAAAAALASAATKAKHLAAVEERKIKSLVALLVETQMKKLELKLRHFEELETIMDREKEALELQRQQLLTERQAFHMEQLKYAEMKARQQMEQQAAVQQNAGGHHGPPPHGPPPGMHPGHPGHPGHPGPGFPPMHHPMGPHHTPQTGPMVGPGQPMPGRMMSGPPPQGGIAPMMGPRHPGPPNGMYPGPPPPTAQPDGMPPGPVGPPPSVPATRAAEN
Protein: K27M-like inhibitor of PRC2 (A0A515VFR0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATQSDMEKEQKHQQDEGQGGLNNETALASGDACGTGNQDPAASVTTVSSQASPSGGAALSSSTAGSSAAAATSAAIFITDEASGLPIIAAVLTERHSDRQDCRSPHEVFGCVVPEGGSQAAVGPQKATGHADEHLAQTKSPGNSRRRKQPCRNQAAPAQKPPGRRLFPEPLPPSSPGFRPSSYPCSGASTSSQATQPGPALLSHASEARPATRSRITLVASALRRRASGPGPVIRGCTAQPGPAFPHRATHLDPARLSPESAPGPARRGRASVPGPARRGCDSAPGPARRGRDSAPVSAPRGRDSAPGSARRGRDSAPGPALRVRTARSDAGHRSTSTTPGTGLRSRSTQQRSALLSRRSLSGSADENPSCGTGSERLAFQSRSGSPDPEVPSRASPPVWHAVRMRASSPSPPGRFFLPIPQQWDESSSSSYASNSSSPSRSPGLSPSSPSPEFLGLRSISTPSPESLRYALMPEFYALSPVPPEEQAEIESTAHPATPPEP
Protein: Cytokine-like 1 (Cytokine-like protein C17) (A1E5L0)
Organism: Mus musculus (Mouse)
Interaction partners:
- Golgi-associated PDZ and coiled-coil motif-containing protein
- Membrane cofactor protein
- Receptor tyrosine-protein kinase erbB-4
Sequence:
MSPKTLPLLLLLVVVVIAWPLAVQSAPPTCYSRMLTLSREIMADFQSLQASEPEDSCVRYLPRLYLDIHNYCVLAKLRDFVASPQCWKMAEVDTLKDRVRKLYTIMNSFCRRDLVFLSDDCSALEDPIPEATGPPDWQS
Protein: NEDD8 ultimate buster 1 (Negative regulator of ubiquitin-like proteins 1) (Protein BS4) (P54729)
Organism: Mus musculus (Mouse)
Function: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Predominantly nuclear. {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein NEDD8
- Ubiquitin D
- 26S proteasome non-ATPase regulatory subunit 4
- Aryl-hydrocarbon-interacting protein-like 1
- 26S proteasome regulatory subunit 6B
Sequence:
MAQKKYLQAKLTQFLREDRIQLWKPPYTKENKEVGLAVKDLAKKYSERLECCENEVENIIEEIRRKAIERGTGNEHYRTTGIATIEVFLPPRLRKHDKKSLLETRLHVTGRDLRCQIAETFGFQENYIKIVINKKQLQLGKSLEEQGVTHNVKAMVLELKQSEEDVRKNLQLEEEEQNEAELKERRIQRTKRGLEILAERAEMVVDPETMPYLDIANQTGRSLRIPPAERKALMLAMGYHEKGRAFLKRKEYGIALPCLLDADRYFCECKELLDTVDNYAVLQLDIVWCYFRLEQLECLDDAEKKLNLAQKCFKNCYGENHQRLVHIKGNCGKEKVLFLRLYLLQGIQNYHSGNGEEAREYLNKARQLFKELYIDPSKVHNLLQLGFTAQEARLGLRACDGNVDHAATHISNRREELAQIRKEEKEKRRRRLENVNTLRGMGYSTQAAKQALHQARGNLDDALKVLLSNPHMWWLQDADPENNSRQASPSQESINQLVYMGFDTVVAEAALRVFGGNVQLAAQTLAHHGGSLPPDLQFSGEDSSPTPSTSPSDSAGTSSASTDEDMETEAVNEILEDIPEHEEDYLDSTLEDEEVIIAEYLSYVESISSAAKNN
Protein: Interferon regulatory factor 7 (M9RSF4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPVPERPAAGPDSPRPGTRRAAPRVLFGEWLLGEISSGCYEGLQWLDEARTCFRVPWKHFARKDLSEADARIFKAWAVARGRWPPSSRGGGPPPEAETAERAGWKTNFRCALRSTRRFVMLRDNSGDPADPHKVYALSRELCWREGPGTDQTEAEAPAAVPPPQGGPPGPFLAHTHAGLQAPGPLPAPAGDKGDLLLQAVQQSCLADHLLTASWGADPVPTKAPGEGQEGLPLTGACAGGEAAAPESPHQAEPYLSPSPSACTAVQEPSPGALDVTIMYKGRTVLQKVVGHPSCTFLYGPPDPAVRATDPQQVAFPSPAELPDQKQLRYTEELLRHVAPGLHLELRGPQLWARRMGKCKVYWEVGGPPGSASPSTPACLLPRNCDTPIFDFRVFFQELVEFRARQRRGSPRYTIYLGFGQDLSAGRPKEKSLVLVKLEPWLCRVHLEGTQREGVSSLDSSSLSLCLSSANSLYDDIECFLMELEQPA
Protein: FI16720p1 (Q0E9F9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD35289p
- Epidermal stripes and patches, isoform A
- FI01430p
- Uncharacterized protein, isoform B
- Tartan, isoform B
Sequence:
MGNKIINMPAARIGTQWLVILCVAMAASGTNLDSGICPVAGDSGCRGNPPDQARYDNYRIYNVEFENQEQIELFQKLEEQSDSLTFIGHAREVGQKLSILVAAHRVADIADLLKTYKVKHRVLTYNFQEKIDRNLAEVQPESIDASQLDWQHFFHLKTIYEWLDKMVEKYPNRVTVLDMGSSTQGNAIKGVKLTSNANNKAIFIESGIHAREWISPAAATYIINQLLTSQDPKVQQLAQDYNWIIFPCVNPDGYKYTFEHDRMWRKNRQLFGTCRGVDLNRNYPDHWNSTGSSSDPTRYDFAGPSAGSELETKRLIDFIRANAGKEQIKTYIALHSYSQMLMFPYGYTKERVSNYDDLQEFGKKASAAIKAENGRDYVSGSLFETIYPSSGGSMDWAHSEAGIPIAYTFELRGPPDSQDLFILPAVEIQPTASEAFTAIRAIVEAAAEKGYYK
Protein: Tubulin gamma chain (Q94771)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000256|ARBA:ARBA00004267}.
Interaction partners:
Sequence:
MPREIITLQVGQCGNQVGSEFWRQLCAEHGIRHDGVVESFASGGDDRKDVFFYQADDDHYIPRALLVDLEPRVINAIQRGSMQRLFNPENVYIHSEGGGAGNNWAHGYEMGDTVQETLFDMIEREAENSDSLEGFVLTHSIAGGTGSGMGSYLLENLNDRFPKKLIQTYSVFPNQSRGGDSDVIVQPYNSLLAIKRLTLHADCVVVLDNTALNRIATDNLHISSPTVEQMNGLVSTVMAASTATLRYPGYMNNDLMSMLASLIPTPRCHFVCTGYTPTTLDTSNIQSSVQKTSVHDVMRRLLMPKNMMVSTSMKSGCYISLLNLIQGDVDPAQVHRSLERIRERSPNFIPWGPASIQVILSKKSPYLDTRHRVSGLVMANHTSISSLFQRTLKQFDLLFNRGVFLEQYKRYGPIKDNLDEFKHSRDVVESLVSEYKACESSDYIRNF
Protein: M-phase phosphoprotein 8 (A0A0A0MT47)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKKVKKGEIRDLKTKTREDPKENRKTKKEKFVESQVESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDTRENRKLENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDKETKRNESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSGEFGIILQNFSR
Protein: 7-methylguanosine phosphate-specific 5'-nucleotidase (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase IIIB) (EC 3.1.3.5) (N(7)-methylguanylate 5'-phosphatase) (Q9W197)
Organism: Drosophila melanogaster (Fruit fly)
Function: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. Also able to mediate hydrolysis of diphosphate (m(7)GDP) to 7-methylguanosine and 2 inorganic phosphate with lower activity. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates.
Interaction partners:
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1
- AMP deaminase
- Inosine triphosphate pyrophosphatase
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11
- Adenine phosphoribosyltransferase
- Apyrase
- 5' nucleotidase B, isoform G
- Thymidylate kinase
- 3',5'-cyclic-AMP phosphodiesterase, isoform I
- UMP-CMP kinase
Sequence:
MGFDEKREPTGGRLRLQDIPALTQDHCRMRDPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHPNVKVVSNFLQFRDGLLDGFQQPMIHTFNKNETVLNETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLIEKQHKLNLEAPKQSSL
Protein: Ring finger protein 14 (D6RA38)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEDREAQEDELLALASIYDGDEFRKAESVQGGETRIYLDLPQNFKIFVSGNSNECLQNSGFEYTICFLPPLVLNFELPPDYPSSSPPSFTLSGKWLSPTQLSALCKHLDNLWEEHRGSVVLFAWMQFLKEETLAYLNIVSPFELKIGSQKKVQRRTAQASPNTELDFGGAAGSDVDQEEIVDERAVQDVESLSNLIQEILDFDQAQQIKCFNSKLFLCSICFCEKLGSECMYFLECRHVYCKACLKDYFEIQIRDGQVQCLNCPEPKCPSVATPGQ
Protein: Sphingolipid long chain base-responsive protein LSP1 (Q12230)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16496001}. Note=Localizes at eisosomes, structures which colocalize with sites of protein and lipid endocytosis.
Interaction partners:
- Sphingolipid long chain base-responsive protein PIL1
- Eisosome protein 1
- Non-classical export protein 2
- Eisosome protein SEG1
- Serine/threonine-protein kinase PKH1
- Uncharacterized protein MRP8
- Serine/threonine-protein kinase PKH2
- Protein SUR7
- Uncharacterized protein YGR130C
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Sequence:
MHRTYSLRNQRAPTAAELQAPPPPPSSTKSKFFGKASIASSFRKNAAGNFGPELARKLSQLVKTEKGVLRAMEVVASERREAAKQLSLWGADNDDDVSDVTDKLGVLIYELGELQDQFIDKYDQYRVTLKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPQSTKIPVLEQELVRAEAESLVAEAQLSNITREKLKAAYSYMFDSLRELSEKFALIAGYGKALLELLDDSPVTPGEARPAYDGYEASRQIIMDAESALESWTLDMAAVKPTLSFHQTVDDVYEDEDGEEEEEPEIQNGDIPGQVVEEEEVEWTTEVPVDDEAHEADHHVSQNGHTSGSENI
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q9XYZ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365081}.
Interaction partners:
- FI23980p1
- RNA helicase
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing factor 17
- Kelch-like protein diablo
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase
- RING-type E3 ubiquitin transferase
- ATP-dependent RNA helicase WM6
- Serine/arginine repetitive matrix protein 1
Sequence:
MSVVIETTMGDLTVDLFISERPIACLNFLKLCRLKYYNFNLFHTVQQGFIAQTGDPSGAGDGGSSIWGVVEGPQKRFFEAEFLPKINHSSAGMLSLVSAGKNLVGSQFFLTLGENLTSLDGNHCVIGEVVEGHEVLRKLNDAIVDDSFRPYQDIRITHTVVLEDPFPNPRGLQAPSRSPSPSAERLKNGRIAADEDIDDTDGMTAEEMQEMLAEREAKARATILEIVGDLPDADMAPPENVLFVCKLNPVTTDDDLEIIFSSFGVLKGCEVIRDRKTGDSLQYAFVEFEDQKSCEAAYFKMDNVLIDDRRIHVDFSQSVSKVTWRGKGRGIEGDYRKLDFNNLRDDKDHRKPNNGRSRTEDHKERNRTEDFRNRMSSAERRKAREQRHQEQSERDVRKNLQRRTRSKEKDEKSVYRSKKSQNESVRENSNRERNRNEKRSSRSRDATHRRYSRSRDREERRPSRPRDQLGRRSRSRDQKERRRSRPREQNERRRSRSRDQTGKRPTQNRDRNDSRRFHSPQEGRRNDERSHRETSRNQRRSPERRQQSRNREDHRMDTHSSPNKSHEKKRKLSVEKSKKQAKKSKRAASSSSDSSESSSESESDSTSSDSSEDSSSSSSSSDDRSKRKKSTKSKQKKSKSKSSHKSKKKHNRN
Protein: CUB-like domain-containing protein (O45667)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
Sequence:
MLQKLFICLAFATAISAAGNGCTLGKSVNKPVIDGTPVYWPAAWNETQPAPQLDNGQSCSWIVTVPRGYYAKLIISGKTTDKDSRFQTVDAAGNLIRTTQENMEPYYFAAPKFTLTVANEGSATFAFKVVWWPLPTVDFEYSTGPTGWIINATNAVYAHEYSEGGGITLMVFPENETSYSSLRSALVYEGRSLSSANYVSNLNLLCQTKKQWASTQNAIFVVNLEASLSKDILLVQANRYLTGIDEMVELRPQLNSIYNGTVHGGTQMSSLVSVANINMQMIDAQMINESNLTVYRGSPAAYTFKQNYTGAQLKSALPLSFSGTFVQFVVSSGQAVFTFKS
Protein: Mrr restriction system protein (P95025)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTIPDAQTLMRPILAYLADGQAKSAKDVIAAMSDEFGLSDDERAQMLPSGRQRTMYDRVHWSLTHMSQAGLLDRPTRGHVQVTDTGRQVLKAHPERVDMAVLREFPSYIAFRERTKAKQPVDATAKRPSGDDVQVSPEDLIDAALAENRAAVEGEILKKALTLSPTGFEDLVIRLLEAMGYGRAGAVERTSASGDAGIDGIISQDPLGLDRIYVQAKRYAVDQTIGRPKIHEFAGALLGKQGDRGVYITTSSFSRGAREEAERINARIELIDGARLAELLVRYRVGVQAVQTVELLRLDEDFFDGL
Protein: Transcription termination factor, mitochondrial (Mitochondrial transcription termination factor) (mTTF) (Q9V3F3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription termination factor. Binds promoter DNA and regulates mitochondrial replication and transcription. Transcription termination activity may be polarized with highest termination activity occurring when its DNA-binding site is positioned in the reverse orientation with respect to the incoming RNA polymerase. Required for normal topology and maintenance of mitochondrial DNA (mtDNA) levels. Regulates mtDNA replication by promoting replication pausing, possibly by acting as a natural barrier to replication fork progression. Its function in replication pausing prevents unregulated replication that may occur for example by collisions between the machineries of DNA replication and transcription during mtDNA synthesis. This ensures the incorporation of RNA transcripts into replication intermediates at the replication fork and allow for proper fork progression. Shares mtDNA binding sites with the mitochondrial termination factor mTerf5 and thereby may antagonize mTerf5 function during replication to regulate pausing. Likely to function downstream of Dref which activates genes involved in mtDNA replication and maintenance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16648357, ECO:0000269|PubMed:24068965}.
Interaction partners:
- Transcription termination factor 5, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial dimethyltransferase 2)
- RE18748p
- Transcription termination factor 3, mitochondrial
Sequence:
MIRSLLRSFETALKLHAGLNMHPMHCSRRLLFSQYENRASPSRLTSSGTLGSNEAENDYVPYRQDRETGTKTRVLLEALRERFRFTDAELQKIISDELVHRCYRGRSLTLVMDTLQLEGVSRRSFVEYPWLLSLDNKRLELKMQLLKSMDFKDINHFVPFLRLTVPRLRKLVGALNSERDAMPQRNRVYYISEKLDVSPDIVSKYLSKRLFILEMPFEMFEKNLQHMIDYNVSPINVLKDLWAFRYTPKSVQLRLERAKRAKKDKIMPWMVRCPEPILQRSLKLSLDELKVLGEFSSVVEYLAHRLGFSTSEAKAIMDKHPQVHTVRVTKIKEVLDYLLDEAQFTRFEVAQNPRILCHSLKTTKERMEELKSHGCRPSSLVILCRSRREYDKFLQNWISHERNPQSVSEG
Protein: Glycolipid 2-alpha-mannosyltransferase 2 (EC 2.4.1.-) (Alpha-1,2-mannosyltransferase 2) (P46592)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in O-glycosylation of cell wall and secreted proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Mainly responsible for the addition of the third mannose residue in an O-linked mannose pentamer. Can also substitute for MNT1 by adding the second mannose residue. Important for adherence to host surfaces and for virulence.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glycolipid 2-alpha-mannosyltransferase 1
- Probable mannosyltransferase MNT3
- Mnn4p
Sequence:
MKPSIFYSSRQPYLKYLAIILTTITIYVLTHSSYSADPNINDVTTKPISETVPQPPPQSPSSPEQQQQQPANQDQIVKVPEELKNKPQDLVVDNNKDQKPAVSGVPKSSSSSPQQQEKQDTKKESENSSSSKDPVKPEKVKATFVTLARNSELYDLIKSIRNVEDRFNRKFNYDWVFLNDDDFTQEFKDLTTALVSGKTKYGKIPKEHWSYPDWIDLKRAEETRKNMKLQKIIYGDSESYRHMCRFESGFFWRHPLLDDYDWYWRVEPSIDIHCDLNYDLFKYMEDNNKVYGFTISIHEFRATIPTLWDTTKKFIKENPQYLAENNFMDFISDDKGETYNLCHFWSNFEIANLNFWRGEAYRKYFDYLDQTGGFFYERWGDAPIHSIAAALFLPKDKIHYFDDVGYKHSVYTQCPLNPQFRYEHKCHCNPDNDFTFRGYSCGKKYFEKMGLQKPKEWEKYQ
Protein: HTH-type transcriptional regulator (Q88GK5)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Interaction partners:
- Muconolactone Delta-isomerase
- Muconate cycloisomerase 1
- catechol 1,2-dioxygenase
- catechol 1,2-dioxygenase
- BenABC operon transcriptional activator
- Transcription regulatory protein
- Transcriptional regulator
- Benzoate 1,2-dioxygenase subunit beta
- Benzoate 1,2-dioxygenase electron transfer component
- 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
Sequence:
MELRHLRYFKVLAETLNFTRAAELLHIAQPPLSRQISQLEDQLGTLLVVRERPLRLTEAGRFFYEQTCTVLQQLQNISDNTRRIGQGQRQWLGIGFAPSTLYTVLPELIRELRQDSELELGLNEMTTLQQVEALKSGRIDIGFGRIRIDDPVIHQQVLCEDPLVAVLPKGHPLAGSPLSLAQLAGEAFILYPANPRPSYADHVLALFAHHGMSIRVSQWANELQTAIGLVAVGVGVTLVPASVQQQHRPDIEYVGLLDSGAVSPIILSRRKGDVSPIVQRCLALIEQQAI
Protein: SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-conjugating enzyme UbcE2A) (Ubiquitin-protein ligase I) (P63281)
Organism: Rattus norvegicus (Rat)
Function: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451 (By similarity). Can catalyze the formation of poly-SUMO chains (By similarity). Essential for nuclear architecture and chromosome segregation (By similarity). Necessary for sumoylation of FOXL2 and KAT5 (By similarity). Sumoylates p53/TP53 at 'Lys-386' (By similarity). Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9013644}. Cytoplasm {ECO:0000269|PubMed:9013644}. Note=Mainly nuclear (By similarity). In spermatocytes, localizes in synaptonemal complexes (By similarity). Recruited by BCL11A into the nuclear body (By similarity). {ECO:0000250|UniProtKB:P63279, ECO:0000250|UniProtKB:P63280}.
Interaction partners:
- Ran GTPase-activating protein 1
- E3 SUMO-protein ligase RanBP2
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 3
- Small ubiquitin-related modifier 2
- SUMO-activating enzyme subunit 2
- SUMO-activating enzyme subunit 1
- Protein PML
- E3 SUMO-protein ligase NSE2
Sequence:
MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
Protein: Excitatory amino acid transporter 5 (Retinal glutamate transporter) (Solute carrier family 1 member 7) (O00341)
Organism: Homo sapiens (Human)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Acts primarily as an inhibitory glutamate-gated chloride channel being a major inhibitory presynaptic receptor at mammalian rod bipolar cell axon terminals. Glutamate binding gates a large Cl(-) conductance that mediates inhibition, affecting visual processing in the retina (By similarity).
Subcellular location: Photoreceptor inner segment membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Note=Located in both cone and rod photoreceptor terminals and in axon terminals of rod bipolar cells. {ECO:0000250|UniProtKB:Q8JZR4}.
Interaction partners:
Sequence:
MVPHAILARGRDVCRRNGLLILSVLSVIVGCLLGFFLRTRRLSPQEISYFQFPGELLMRMLKMMILPLVVSSLMSGLASLDAKTSSRLGVLTVAYYLWTTFMAVIVGIFMVSIIHPGSAAQKETTEQSGKPIMSSADALLDLIRNMFPANLVEATFKQYRTKTTPVVKSPKVAPEEAPPRRILIYGVQEENGSHVQNFALDLTPPPEVVYKSEPGTSDGMNVLGIVFFSATMGIMLGRMGDSGAPLVSFCQCLNESVMKIVAVAVWYFPFGIVFLIAGKILEMDDPRAVGKKLGFYSVTVVCGLVLHGLFILPLLYFFITKKNPIVFIRGILQALLIALATSSSSATLPITFKCLLENNHIDRRIARFVLPVGATINMDGTALYEAVAAIFIAQVNNYELDFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWALDRFRTMINVLGDALAAGIMAHICRKDFARDTGTEKLLPCETKPVSLQEIVAAQQNGCVKSVAEASELTLGPTCPHHVPVQVEQDEELPAASLNHCTIQISELETNV
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (A0A060X747)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
- C2H2-type domain-containing protein
- Uncharacterized protein
- Mediator of RNA polymerase II transcription subunit 1
- Transcription factor Jun
- Transcription factor Jun
- Protein c-Fos
- Protein c-Fos
- Nuclear receptor interacting protein 1b
- Nuclear receptor-interacting protein 1 repression domain-containing protein
- Nuclear receptor domain-containing protein
Sequence:
MYPEETRGGGGAAAFNYLDGGYDYTAPAQGPAPLYYSTTPQDAHGPPSDGSMQSLGSSPTGPLVFVSSSPQLSPQLSPFLHPPSHHGLPSQSYYLETSSTPLYRSSVVTNQLSASEEKLCIASDRQQSYSAAGSGVRVFEMANETRYCAVCSDFASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTMDRNRRKSCQACRLRKCYEVGMVKGGLRKDRGGRVLRKDKRYCGPAGDREKPYGDLEHRTAPPQDGGRNSSSSLNGGGGWRGPRITMPPEQVLFLLQGAEPPALCSRQKVARPYTEVTMMTLLTSMADKELVHMIAWAKKITCFQELSLHDQVQLLESSWLEVLMIGLIWRSIHCPGKLIFAQDLILDRSEGDCVEGMAEIFDMLLATVSRFRMLKLKPEEFVCLKAIILLNSGAFSFCSNSVESLHNSSAVESMLDNITDALIHHISHSGASVQQQPRRQAQLLLLLSHIRHMSNKGMEHLYSIKCKNKVPLYDLLLEMLDGHRLQSPGKVAQAGEQTEGPSTTTTTSTGSSIGPMRGSQDTHIRSPGSGVLQYGSPSSDQMPIP
Protein: Activating transcription factor 6 (Cyclic AMP-dependent transcription factor ATF-6 alpha) (Q5RH85)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- X-box-binding protein 1
- DNA damage-inducible transcript 3 protein
- Wolfram syndrome 1a
- Wolframin
- Immunoglobulin binding protein
- Cyclic AMP-dependent transcription factor ATF-4
- Eukaryotic translation initiation factor 2-alpha kinase 3
- Membrane-bound transcription factor peptidase, site 2.
- Membrane-bound transcription factor site-1 protease
- Eukaryotic translation initiation factor 2-alpha kinase 2.
Sequence:
MSSNLMLDLMNPSMSSKEVGDISIDQDGEWDISLFDELEDLGDADELLEALVKSVGYDTSVPDLNFGTEQPAWSSDGWRETSSPRSDGDVTVDSLSPNHTFSSVSSPASVEPQSPYSTHDEALSPDSWRSHPSPLSVCSDSSGFTEAPNEKKPSKRTNQTKAKPLQPAKRPIQVCPKVSIQPKPIITAVPISRPAAPLQTKIIIQPLQATVLPVVKPPPVTIQPAPPTGQLMQLPQPTQVLQLQTPQSMPTRVVTMPALAQDRPISLVAPVTTSPVVTMTLQNSTPDDDSNASRRQQRMIKNRESASLSRKKKKEYLMTLETRLKLALTENEKLKNENGTLKRQVEGLMSENSVLKATAPKRRAVCLMVVLVFLVVNLGPMSLLGGDRGSAFPATPVFNGRHLLGFSPESERNLDKPQTDPSNTVDRLEEGVSEQKALMVVKDPLYFRTPPPCQPPVNRTKCIKIAHELRGWVHRHEVERTKTRRMSNTQHRGRTFMKASSKQADVPQIMSQIQYTDSSEKNPGSELQVYYAPHRTYNDFFDELNRRGDTFYVISFRRDHLLLPATNHNKGSRPKMSVVLPAMNYNESIIKDKDYEVMMQIDCEVMDTKILHIKSSSIPPILRVNQTETSSFYHATPSNNQPAAPVGVLVGSS
Protein: PNPLA domain-containing protein (O05770)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPIPFADGMLSRLGRRGAALDLIEEFEDESGEPPASLSPADLLAAEPALLLQKMENRLVRHHLANPDVLSGEQLRKLRYILNFARLADFEPGAAGPGGSRGRGDISVGGQVAPWRSRVVDALYAPLREEPDPVTALEGAKDVLATLVDDQDDQRRVLIERHGSDFSATELDAEVGYKKLVTVLGGGGGAGFVYIGGMQRLLAAGQVPDYMIGSSFGSIIGSLVARELPVPIDEYAEWAKTVSYRAILGPERRRSRHGLAGMFTLRFDQFAHTLLSRADGERMRMSDLAIPFDVVVAGVRRQPYAALPSRFRHRERSTLTLRSLPFLPIGIGPWVAARMWQVAAFIDLRVVKPIVISADGATRDVNVVDAASFSSAIPGVLHHETSDPRMLPILDELCADQDVAAMVDGGAASNVPVELAWERVRDGRLGTRNACYLAFDCFHPHWDPRHLWLVPITQAVQLQMVRNLPYADHLVRFEPTLSPVNLAPSAAAIDRACRWGRDSVEPAIAVTSALLEPTWWEGDRPPAAEPKERTKSAASSMSAVMAAIQAPTGRFRRWRSRHLT