wanglab/gogpt-training-data huggingface dataset:
Protein: Pancreatic secretory granule membrane major glycoprotein GP2 (Glycoprotein 80) (gp80) (Pancreatic zymogen granule membrane protein GP-2) (P19218)
Organism: Rattus norvegicus (Rat)
Function: Functions as an intestinal M-cell transcytotic receptor specific of type-I-piliated bacteria that participates in the mucosal immune response toward these bacteria. At the apical membrane of M-cells it binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to elicit a mucosal immune response.
Subcellular location: Zymogen granule membrane {ECO:0000269|PubMed:1999417, ECO:0000269|PubMed:6479170}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}. Secreted {ECO:0000305|PubMed:6479170}. Cell membrane {ECO:0000269|PubMed:1999417, ECO:0000269|PubMed:6479170}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}. Apical cell membrane {ECO:0000250|UniProtKB:Q9D733}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}. Membrane raft {ECO:0000269|PubMed:11853552}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}. Endosome {ECO:0000250|UniProtKB:Q9D733}. Note=Secreted, after cleavage, in the pancreatic juice. {ECO:0000305|PubMed:6479170}.
Interaction partners:
- GTP-binding protein 1
- Platelet glycoprotein V
- Scavenger receptor cysteine-rich type 1 protein M130
- NPC intracellular cholesterol transporter 1
- Glycoprotein VI
- Synaptic vesicle glycoprotein 2A
- Chymotrypsin like elastase 3B
- Synaptic vesicle glycoprotein 2C
- Pancreatic polypeptide prohormone
Sequence:
MVACDLLWLAAASCLLTLVFPSTTHQGYGNPRNTSNVDLDCGAPGSSSAGICFDPCQNHTVLNDPSRSTENTVSSEECDSHLRGWYRFVGDGGVKMPETCVNVYRCHTYAPMWLSGSHPILGDGIVNRTACANWNENCCFWSSEVQVKACLGESGEYHVYKLQGTPECSLRYCTDPSTAPKKCEIACRPEEECVFQNNSWTCVCRQDLNVSDTLSLQPLLDCGANEIKVKLDKCLLGGLGFKEDIITYLNDRNCRGTMKDEPNNWVSTTSPVVANDCGNILENNGTQAIYRNTLSLATDFIIRDFLVNVNFQCAYPLDMNVSLQTALQPIVSSLNVDVGGAGEFTVTMALFQDQSYTHPYEGSKVLLPVENILYVGALLNRGDTSRFKLLLTNCYATPSGDRNDIVKYFIIRNRCPNQRDSTINVEENGVSSESRFSVQMFMFAGNYDLVFLHCEVYLCDSTTEQCQPSCSTSRLRSSEPAIDLTRVLDIGPITKKSVQNPDTSNGTPRNTGFLLAWPTFFLPVFLAWLF
Protein: Nucleolar protein, putative (Q583H8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar complex protein 2
- Ribosome biogenesis protein BOP1 homolog
- Nucleolar GTP-binding protein 1
- RNA-binding protein, putative
- Ribosome assembly factor mrt4
- NLE domain-containing protein
- CCAAT-binding factor domain-containing protein
- rRNA processing protein, putative
- Pescadillo homolog
Sequence:
MSGNGGISGNYAPYEENEEVEYNDEEFGSYEEEESDYFSDGEEVEDDDDFEAKAIKFRQQMDKLHSEAAAEQEGDIRSRTAKPTLFGDAEEQEEDGEQVQLLGQQHTVEELRDRIGETVHVLSHFKEEREEGRTREDYMQLLRADIMELYGYNEFLTDSILLLFSPTEAVEFFEAMEKPRPTTIRVNTIKAKRRDLVQALVKRGMNVEPLEKWSKVGLQVFESNVPISGTVEYLAGHYMLQSAVSFLPVMALAPQINERVLDMAAAPGGKTTYIAQLMKNTGVIFANDVSEPRTKSLNANLQRLGVTNTVVTNYDGVGFEKVMKNFDRILLDAPCTGSGIISRDKSIKTSKQYEDVQRASQLQRSLLLSAIDAVRVGGYIVYSTCSFLVEENEAVVDFVLHRRDVAIVETGLPFGRPGLTKYRHHRFHDKLQNARRLFPHVHNMDGFFVCKLKKLSNNAGGPSTNGLKKEESNVAKSENVKTMKGTNKRQREDDSKAKGELKTKNNRISVPPATKKSPKSKGKSG
Protein: SPbeta prophage-derived bacteriocin sublancin-168 (P68577)
Organism: Bacillus subtilis (strain 168)
Function: Bacteriocin active against Gram-positive bacteria. Inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells. Inhibits B.subtilis strain ATCC 6633.
Subcellular location: Secreted {ECO:0000269|PubMed:21196935}. Note=Extracellular region.
Interaction partners:
- SPbeta prophage-derived sublancin-168-processing and transport ATP-binding protein SunT
- SPbeta prophage-derived glycosyltransferase SunS
- SPbeta prophage-derived disulfide bond formation protein A
- SPbeta prophage-derived disulfide bond formation protein B
Sequence:
MEKLFKEVKLEELENQKGSGLGKAQCAALWLQCASGGTIGCGGGAVACQNYRQFCR
Protein: FAD synthase (EC 2.7.7.2) (FAD pyrophosphorylase) (FMN adenylyltransferase) (Q384S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- riboflavin kinase
- Cystathionine beta-synthase, putative
- Riboflavin transporter RibJ
Sequence:
MGEEVVRLDGHGVTDGTVAGLCDHRNIRRVELTNCTRITDISPLANIFTLEEVVIRNCQSVRYVGTLGQSQPSLRRIEFTGTPLTGEQLQLLRSAQAQLILRDGDFPVQLKQPGQLLVKESIDVVKGIVSQFKPEEIGIAFNGGKDSVVMMDILYCVMGAEFISQCCVFHLNTINDKEFHEVVEFRKAFAAARKLSIVQSDQMLSMKDGLEQVKKTMGIRVAFMGTRKADGCHQMTGVERTTAGWPDLLRACPLFCWEYEDVWGYIRTYDLPFCELYEKGYTSLGGANSTIPNSHLSREDGTFRPAWELANGRSERCGRLST
Protein: LETM1 domain-containing protein 1 (Cervical cancer receptor) (MCC-32) (Q924L1)
Organism: Mus musculus (Mouse)
Function: Plays an essential role for mitochondrial structure and function, as well as thermogenesis of brown adipocytes. In brown adipose tissue also localizes in the nucleus where it interacts with the chromatin remodeler SMARCA4 to regulate thermogenic genes expression, such as UCP1. May regulate phagocytosis and inflammatory responses to lipopolysaccharide in macrophages (By similarity). Involved in tumorigenesis and may function as a negative regulator of the p53/TP53.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q6P1Q0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6P1Q0}. Nucleus {ECO:0000269|PubMed:34910916}. Mitochondrion inner membrane {ECO:0000269|PubMed:36334589}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALSRVCWARAALWGSTVAPGPFVTRRLQLGRSGPAWRAPRSSKLHLSPKADVKNLISYVVTKTRAINGSYHRFLGRHFPRFYALYTTFMKGIQMLWADGKKARRIKADMWKQNLKFHQLSYREMEHLRQFRRDITKCLFVGLISIPPFANYLVFLLMYLFPRQLLVKHFWTPKQQIDFLDVYHGLRRRSHSEVITHLRRASTFVSHEKLRRQLTDLCTKVQSGTHPAAQDVLALRDCFSTYPLGFSQLQASQMRALSQAMLLTPYLPPPLLRQRLKSHTTVIHQLDRALAKLGIGQLTAQEVKSACYLRGLNSTHIADDRCRAWLGEWLHISCSLKEPELSLLLHNVVLLSTNYLETRR
Protein: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC 2.5.1.58) (EC 2.5.1.59) (CAAX farnesyltransferase subunit alpha) (FTase-alpha) (Ras proteins prenyltransferase subunit alpha) (Type I protein geranyl-geranyltransferase subunit alpha) (GGTase-I-alpha) (Q9LX33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Interaction partners:
- Geranylgeranyl transferase type-1 subunit beta
- Protein farnesyltransferase subunit beta
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Dehydrodolichyl diphosphate synthase 6
- Dehydrodolichyl diphosphate synthase 7
- Dehydrodolichyl diphosphate synthase 8
- Dehydrodolichyl diphosphate synthase 4
- Dehydrodolichyl diphosphate synthase 2
- Alkyl transferase
Sequence:
MNFDETVPLSQRLEWSDVVPLTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRALRLTEETLLLNSGNYTVWHFRRLVLEALNHDLFEELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVAGRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWEDELDYCHELLEADVFNNSAWNQRYYVITQSPLLGGLEAMRESEVSYTIKAILTNPANESSWRYLKALYKDDKESWISDPSVSSVCLNVLSRTDCFHGFALSTLLDLLCDGLRPTNEHKDSVRALANEEPETNLANLVCTILGRVDPVRANYWAWRKSKITVAAI
Protein: CCT-theta (Q5AB74)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- CCT-beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit delta
- Gim5p
- Heat shock protein homolog SSE1
- Heat shock protein 60, mitochondrial
Sequence:
MSLKLPQAPNSGLFKQGYSSFSNADGAIIRNVEAVREIASILLTSMGPSGRNKIIVNKLGKKFITNDAATMLNELEIVHPVVKILIQASKQQEFEMGDNTNLVIILAGEFLNVAEKLLTLGLNVSEIIQGFNLANKFVMKTLDELVVEKVESFETDLLKAVKPVIAAKQYGVEDTIAKLVVDAVALVMKNGSFNVDNIRVVKVMGASLSQSQVVKGMVFPREPEGTVKNAAKSKVVVFTNPIDISTTETKGTVLLHNAQEMLDFTKGEEQQLDQLCKEIHDSGVKVVVAGSSVGELALHYLNKYGILVLRVPSKFDLRRICQVCGATPLPRLGAPTPDEMGEIDIIETKEIGGDRVTIFRQDESSSRTATIVVRGATQNNLDDIERAIDDGVNSIKGLIKDNRLLPGAGAVEIELMKRITAYGESTPGLLQLAIKSFAKAFEVIPRVLAETSGHDSSEILSKLHAAHAEDTGLRAGIDIDSGEVADTAVLDILATKKSAIDLAVDATNTILSIDQIIMAKRAGGPVMPQQPRPGNWDQDD
Protein: Cathepsin L (Q5T8F0)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEAGVKNGAWVAT
Protein: 2'-5'-oligoadenylate synthase-like protein (2'-5'-OAS-related protein) (2'-5'-OAS-RP) (59 kDa 2'-5'-oligoadenylate synthase-like protein) (Thyroid receptor-interacting protein 14) (TR-interacting protein 14) (TRIP-14) (p59 OASL) (p59OASL) (Q15646)
Organism: Homo sapiens (Human)
Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L.
Subcellular location: [Isoform p56]: Nucleus, nucleolus. Cytoplasm.; SUBCELLULAR LOCATION: [Isoform p30]: Cytoplasm.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- Ubiquitin-like protein ISG15
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon-induced protein with tetratricopeptide repeats 2
- Interferon-induced GTP-binding protein Mx1
- Interferon-induced protein 44-like
- Interferon-induced protein 44
- E3 ISG15--protein ligase HERC5
Sequence:
MALMQELYSTPASRLDSFVAQWLQPHREWKEEVLDAVRTVEEFLRQEHFQGKRGLDQDVRVLKVVKVGSFGNGTVLRSTREVELVAFLSCFHSFQEAAKHHKDVLRLIWKTMWQSQDLLDLGLEDLRMEQRVPDALVFTIQTRGTAEPITVTIVPAYRALGPSLPNSQPPPEVYVSLIKACGGPGNFCPSFSELQRNFVKHRPTKLKSLLRLVKHWYQQYVKARSPRANLPPLYALELLTIYAWEMGTEEDENFMLDEGFTTVMDLLLEYEVICIYWTKYYTLHNAIIEDCVRKQLKKERPIILDPADPTLNVAEGYRWDIVAQRASQCLKQDCCYDNRENPISSWNVKRARDIHLTVEQRGYPDFNLIVNPYEPIRKVKEKIRRTRGYSGLQRLSFQVPGSERQLLSSRCSLAKYGIFSHTHIYLLETIPSEIQVFVKNPDGGSYAYAINPNSFILGLKQQIEDQQGLPKKQQQLEFQGQVLQDWLGLGIYGIQDSDTLILSKKKGEALFPAS
Protein: Serine protease PepD (EC 3.4.21.107) (HtrA-like serine protease) (O53896)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for virulence. Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone. Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks. May utilize its PDZ domain to recognize and process misfolded proteins at the cell membrane, leading to activation of the MprAB and SigE signaling pathways and subsequent establishment of a positive feedback loop that facilitates bacterial adaptation. Interacts with and potentially cleaves several proteins, including the 35 kDa antigen PspA. Proteolytic cleavage of PspA may help to maintain cell envelope homeostasis in Mycobacterium and regulate specific stress response pathways during periods of extracytoplasmic stress. In vitro, exhibits proteolytic activity against the artificial substrate beta-casein.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:21445360}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:21445360}. Secreted {ECO:0000269|PubMed:21445360}. Note=Traffics from the cytoplasm through the cell membrane to the cell wall where it is autoprocessed and eventually secreted into the culture filtrate protein. {ECO:0000269|PubMed:21445360}.
Interaction partners:
- MoaB/Mog domain-containing protein
- Signal transduction histidine-protein kinase/phosphatase MprB
- Putative envelope-preserving system protein Rv2743c
- Putative envelope-preserving system protein Rv2742c
- Proteasome-associated ATPase
- Protease HtpX homolog
- Serine protease Rv3671c
- Response regulator MprA
- RNA polymerase sigma factor SigB
- Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Sequence:
MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGALVNMNAQLVGVNSAIATLGADSADAQSGSIGLGFAIPVDQAKRIADELISTGKASHASLGVQVTNDKDTLGAKIVEVVAGGAAANAGVPKGVVVTKVDDRPINSADALVAAVRSKAPGATVALTFQDPSGGSRTVQVTLGKAEQ
Protein: Bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic (AtRIBA1) [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)] (P47924)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in riboflavin biosynthesis. Catalyzes both the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate and the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. RIBA2 and RIBA3 together are not able to complement the loss of function of RIBA1.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23203051}.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase, chloroplastic
- Riboflavin biosynthesis protein PYRD
- Riboflavin synthase
- Riboflavin biosynthesis protein PYRR
- GTP cyclohydrolase 1
- Monofunctional riboflavin biosynthesis protein RIBA 3
- Monofunctional riboflavin biosynthesis protein RIBA 2
- GTP 3',8-cyclase, mitochondrial
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial
Sequence:
MSSINLSSSSPSTISLSRSRLSQSSTTLLHGLHRVTLPSNHPLSTFSIKTNTGKVKAAVISREDDLLSFTNGNTPLSNGSLIDDRTEEPLEADSVSLGTLAADSAPAPANGFVAEDDDFELDLPTPGFSSIPEAIEDIRQGKLVVVVDDEDRENEGDLVMAAQLATPEAMAFIVRHGTGIVCVSMKEDDLERLHLPLMVNQKENEEKLSTAFTVTVDAKHGTTTGVSARDRATTILSLASRDSKPEDFNRPGHIFPLKYREGGVLKRAGHTEASVDLTVLAGLDPVGVLCEIVDDDGSMARLPKLREFAAENNLKVVSIADLIRYRRKRDKLVERASAARIPTMWGPFTAYCYRSILDGIEHIAMVKGEIGDGQDILVRVHSECLTGDIFGSARCDCGNQLALSMQQIEATGRGVLVYLRGHEGRGIGLGHKLRAYNLQDAGRDTVEANEELGLPVDSREYGIGAQIIRDLGVRTMKLMTNNPAKYVGLKGYGLAIVGRVPLLSLITKENKRYLETKRTKMGHMYGLKFKGDVVEKIESESES
Protein: BCL-WAV (BCL2-like 16) (D2Y5Q2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Calcium uniporter protein
- Zona pellucida protein C.
Sequence:
MGRSDDAVIGRGLNSPDPLVREAFLMAYDYISYVTAKPGVPLCPAPSRASAALRHAGDELLIRFPIFFRRWPRVFQDVTEHTACPTLLSILDEHFAPTRRRDLAWSAVLSVFVLAGQLALHCQDRGMEDITPQIQECVGSYVERVICPEIRDKGGWSGFISRFGEKQNLEDHVVKVCCWSLLLLCVGILSYFIWTRRKT
Protein: U2 small nuclear RNA auxiliary factor 1 (Q7Z780)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQEHYDEFFEEVFTEMEEKYREVEEMNVCDNLGDHLVGNVYVKFRREEDAEKAVIDLNNRWFNGQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPISRELRRELYGRRRKKHRSRSRSRERRSRSRDRGRGGGGGGGGGGGGRERDRRRSRDRERSGRF
Protein: Ubiquitin thioesterase OTU1 (EC 3.4.19.12) (Q55BI3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}.
Interaction partners:
- Phospholipase A-2-activating protein
- Ubiquitin fusion degradation protein 1 homolog
- Cell division cycle protein 48
- NSFL1 cofactor p47 homolog
- Nuclear protein localization protein 4 homolog
- Ubiquitin conjugation factor E4 B
- RING-type E3 ubiquitin transferase
- Ubiquitin domain-containing protein
- PARP catalytic domain-containing protein
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MSLISIRIRSKTGVENIKLESQLKLKELQNIIEEKTKISTDTQKILYGFPPKALDLSNQDAVISGFLANGDTITIENVSSISSNPGVDSVTNDKVTSSTNSFDRNIKSQPFISQEEEEDGGYATRRVTDDDNSCLFSAVAYVLEDKNRLKGYSLRALIAQNVKSDPFEYNEAVLGKSNEGYCNWIQNPKNWGGAIELSILSNHYKVEIAAFDISTQLMYCYGEDRKYTERVYLIYDGIHYDALSICLTKNGPEDFDITRFSVDDKDSLAKMKVLIEKEFKAGKFTDTAKFSLICLNCNKTLKGEKEAAIHASTTGHGNFTEYKKR
Protein: Chromatin remodeling factor mit1 (EC 3.6.4.-) (Mi2-like interacting with clr3 protein 1) (Snf2/Hdac-containing repressor complex protein mit1) (SHREC protein mit1) (Q9P793)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).
Subcellular location: Nucleus. Chromosome, centromere. Chromosome, telomere. Note=Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.
Interaction partners:
- Cryptic loci regulator protein 1
- Histone deacetylase clr3
- Cryptic loci regulator 2
- Chromo domain-containing protein 2
- Histone deacetylase clr6
- Chromatin-associated protein swi6
- RbAp48-related WD40 repeat-containing protein prw1
- Histone acetyltransferase type B subunit 2
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Histone deacetylase phd1
Sequence:
MPKEDDSLCKIVVRREPLDVLLPYYDASETTVQKILHENDSTLSVKFLAGVEALIKKDELDKYKNGKACLRVWLKHKSRKRYHGYMTSTDKDEEEKNDYLLKSNGSKVLRDSTRTKKFKFGKEFHCALNPSFVSDETASDSATSSSSDTNKKVNRKEHNELSLSHLSFNDTSDFGSSDLSSSEIESTENDNKAPYFSLLYSDGFDFIKFLHVCVCVKCHGREHRSSGKNFVYCDHCSNVYHYDCSPLPSLNKETRNYSQQNGFICPLCSKNSKDVLCNTGFVSGVSSGQDLVIPPSLADRESLSILVNYCKSIRFRCFRCRRVEYFFYLDSNPLSIQRTITHFIKKLVCNECSMHPCDIEEIIAWRTLNSLYPSKATLSNNFVSTSDLSFWSREYFVRSKGKSYLHCFWCSASWLAGISLAKKKNFDGLENASYDATKPIIPVSYTIIDKVWDVQYRSGKNARTAKYKTKKHQLKAISEVTFAFVSWRGLTYYMSNWEPPPKETDRNRWKAWLKGYSDLLECLWIEKAPTASINIDLPFTNLEWHSQPSFIKGGTLMPYQLKGLNWLYLRWYTHHPCILADEMGLGKTVQVISFISVLFYRHKCFPVLVIVPHATVANWERELKKWAPFLQINVLVGSEKNRSLVRDYRLINQKDPKHVSTHVLVISASNVEREISLLRKFQWKVLIVDEGQRLKNDQSSLFYYLSSVKSDFKLLLTGTPLQNNVRELFNLLQFLNPMKINAAELEKRYSIIDTEKVTELHQILKPFFLRRVKSEVLDNFPTKVEVIIPLSMTPVQKGLYKSILSKNLSLLRNITGYANTSSSGGQRTTSLNNILMQLRKTLAHPYIYSPDIEDRNLPYELAMRSLEEASCKFLILRLLVPKLITRGHRILLFSQFIQQLDILEDWFEYKNIAYARFDGASSEMERQSAIDSFNAPNSELSCFLLSTRAGGVGINLASADTVIILDPDFNPHQDMQAIARAHRYGQKKKVLVFVLTTRDSVEEKIIQNAQKKLVLDHLIVESLDQNHNSEKDLESILRHGARALFEEAGDEPSIKYNEYSVELLISEAEKQEDTSTDESDIKSNKFGFFRVWDNKHISSNHYEVKENVLVDEEDVWSVILKQREKDAMLEKTDETTSNRRLRAHHKIHYGEDLNIYDNSDDTDYTVNDRSSPGSPFPIETETISSITDTLSDKQKLKYDSSVNIENLNDESDSQKSADVHFDSILAKSLLATTPKEDEFNKTLSTINLEVANKLTSSEYINDSEMQLIDDPVFYPPYEIIEKNHQLVGRSLSKAVLDNFFLLSSLSDNVRCRCCGIKHLPAHCPLSIVPLEICFLCGTPHFSGRDTCPMLRNKEAIYRLKDSLSKSREPFHIKKQAMARLNSFLQKKEEPTVSSSAKTNELSSKVIIKESIINEAKTL
Protein: Small ribosomal subunit protein uS8 (40S ribosomal protein S15a) (Q6Q420)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Structural component of the ribosome (By similarity). Required for erythropoiesis during embryonic development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62244}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62244}.
Interaction partners:
- Ribosomal protein S3
- Small ribosomal subunit protein eS7
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- Small ribosomal subunit protein eS4
- 40S ribosomal protein S15
- 40S ribosomal protein S6
- 40S ribosomal protein S24
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein uL29
Sequence:
MVRMNVLADALKSINNAEKRGKRQVLLRPCSKVIVRFLTVMMKHGYIGEFEIIDDHRAGKIVVNLTGRLNKCGVISPRFDVQLKDLEKWQNNLLPSRQFGFIVLTTSAGIMDHEEARRKHTGGKILGFFF
Protein: Meiotic nuclear division protein 1 homolog (Q9BWT6)
Organism: Homo sapiens (Human)
Function: Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis (By similarity). Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homologous-pairing protein 2 homolog
- DNA repair protein RAD51 homolog 1
- Exonuclease 1
- Breast cancer type 2 susceptibility protein
- Serine/threonine-protein kinase Chk1
- RAD51-associated protein 1
- Breast cancer type 1 susceptibility protein
- Mitotic spindle assembly checkpoint protein MAD2A
- Kinetochore protein Nuf2
- Mitotic checkpoint serine/threonine-protein kinase BUB1
Sequence:
MSKKKGLSAEEKRTRMMEIFSETKDVFQLKDLEKIAPKEKGITAMSVKEVLQSLVDDGMVDCERIGTSNYYWAFPSKALHARKHKLEVLESQLSEGSQKHASLQKSIEKAKIGRCETEERTRLAKELSSLRDQREQLKAEVEKYKDCDPQVVEEIRQANKVAKEAANRWTDNIFAIKSWAKRKFGFEENKIDRTFGIPEDFDYID
Protein: Proteasome subunit alpha type (A0A1D8PQW1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome regulatory particle lid subunit
- Proteasome subunit beta
- 26S proteasome regulatory subunit RPN1
- Proteasome regulatory particle lid subunit
- Proteasome subunit alpha type
- 26S proteasome regulatory subunit 6A
Sequence:
MTSIGTGYDLSNSVFSPDGRNFQVEYAMKAVENGGTSIGIKCKDGIVLAVEKIIQSKLLIPKKNKRIQTVDRNIGVVYSGLLPDGRHFVNRCRDECQSFKSIFKTMMPISNLMDRMGIYVQNYTCYNSVRPFGIVSIIGGVDNEDGEPYLYMIEPSGSYWGYNGAATGKGRQIAKSELEKLNYEELTCLEAINHAARIIHLSHEDNKDKDYELEISWCSKEHTGGKHQFISDDLLEQARKLAEEEEEEEDDDEEEEAGADDEEMAP
Protein: Sal-like 1 (Drosophila) (Spalt like transcription factor 1) (Q6P5E3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQAKPQHFQSDPEVASLPRRDGDTEKGQPSRPTKSKDAHVCGRCCAEFFELSDLLLHKKSCTKNQLVLIVNESPASPAKAFPPGPSLNDPDDQMKDAANKADQEDCSDLSEPKGLDREESMEVEVPVATTTTTTTGGSGGSGGSTLSGVTNITTPSCHSGSSTGTSAITTSLPQLGDLTTLGNFSVINSNVIIENLQSTKVAVAQFSQEARCGGASGGKLLISTLMEQLLALQQQQIHQLQLIEQIRHQILLLASQSADLPAAPSIPSQGTLRTSANPLTTLSSHLSQQLAVAAGLAQSLASQSANISGVKQLPHVQLPQSSSGTSIVPPSGGTSPNMSIVTAAVPTPSSEKVASNAGASHVSSPAVSASSSPAFAISSLLSPASNPLLPQPTPANAVFPTPLPNIATTAEDLNSLSALAQQRKSKPPNVTAFEAKSTSDEAFFKHKCRFCAKVFGSDSALQIHLRSHTGERPFKCNICGNRFSTKGNLKVHFQRHKEKYPHIQMNPYPVPEHLDNVPTSTGIPYGMSIPPEKPVTSWLDTKPVLPTLTTSVGLPLPPTLPSLTPFIKTEEPAPIPISHSAASPQGSVKSDSGAPDLATRNPSGVPEEVEGSAVPPFGGKGEESNMASSAVPTAGNSTLNSPVADGGPGGTTFTNPLLPLMSEQFKAKFPFGGLLDSAQASETSKLQQLVENIDKKATDPNECIICHRVLSCQSALKMHYRTHTGERPFKCKICGRAFTTKGNLKTHYSVHRAMPPLRVQHSCPICQKKFTNAVVLQQHIRMHMGGQIPNTPVPDNYPESMESDTGSFDEKNFDDLDNFSDENMEECPEGSIPDTPKSADASQDSLSSSPLPLEMSSIAALENQMKMINAGLAEQLQASLKSVENGSMEGDVLTNDSSSVGGDMESQSAGSPAISESTSSMQALSPSNSTQEFHKSPGMEEKPQRVGPGEFANGLSPTPVNGGALDLTSSHAEKIIKEDSLGILFPFRDRGKFKNTACDICGKTFACQSALDIHYRSHTKERPFICTVCNRGFSTKGNLKQHMLTHQMRDLPSQLFEPSSNLGPNQNSAVIPANSLSSLIKTEVNGFVHVSPQDSKDAPTSHVPQGPLSSSATSPVLLPALPRRTPKQHYCNTCGKTFSSSSALQIHERTHTGEKPFACTICGRAFTTKGNLKVHMGTHMWNSTPARRGRRLSVDGPMTFLGGNPVKFPEMFQKDLAARSGSGDPSSFWNQYTAALSNGLAMKANEISVIQNGGIPPIPGSLGSGSSSPISGLTGNVEKLGNSEPSAPLAGLEKMASSENGTNFRFTRFVEDSKEIVTS