wanglab/gogpt-training-data huggingface dataset:
Protein: Soluble secreted antigen MPT53 (P9WG65)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Disulfide oxidoreductase that catalyzes the oxidation of reduced, unfolded secreted proteins to form disulfide bonds. Despite a weak homology to thioredoxin this cannot serve as a substrate for thioredoxin reductase.
Subcellular location: Secreted.
Interaction partners:
- Probable conserved integral membrane protein
- Alkyl hydroperoxide reductase C
- Peptide methionine sulfoxide reductase MsrA
- TIGR03085 family protein
- Dihydrolipoyl dehydrogenase
- Probable oxidoreductase
- Probable soluble pyridine nucleotide transhydrogenase
- Mycothione reductase
- NAD
- Nudix hydrolase domain-containing protein
Sequence:
MSLRLVSPIKAFADGIVAVAIAVVLMFGLANTPRAVAADERLQFTATTLSGAPFDGASLQGKPAVLWFWTPWCPFCNAEAPSLSQVAAANPAVTFVGIATRADVGAMQSFVSKYNLNFTNLNDADGVIWARYNVPWQPAFVFYRADGTSTFVNNPTAAMSQDELSGRVAALTS
Protein: Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP) (P53619)
Organism: Bos taurus (Bovine)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit beta'
- Coatomer subunit epsilon
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- ADP-ribosylation factor GTPase-activating protein 3
- Transmembrane emp24 domain-containing protein 10
- Coatomer subunit zeta
Sequence:
MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSTVSGGSTTSMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGENIISSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPNDFFPVQVSFISKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL
Protein: Thiol-specific monooxygenase (EC 1.14.13.-) (Flavin-dependent monooxygenase) (Q9HFE4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins (By similarity).
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein coq9
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Atypical kinase COQ8, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
Sequence:
MCLPTIRKIAIIGAGPSGLVTAKALLAEKAFDQVTLFERRGSPGGVWNYTSTLSNKLPVPSTNPILTTEPIVGPAALPVYPSPLYRDLQTNTPIELMGYCDQSFKPQTLQFPHRHTIQEYQRIYAQPLLPFIKLATDVLDIEKKDGSWVVTYKGTKAGSPISKDIFDAVSICNGHYEVPYIPNIKGLDEYAKAVPGSVLHSSLFREPELFVGESVLVVGGASSANDLVRHLTPVAKHPIYQSLLGGGDIQNESLQQVPEITKFDPTTREIYLKGGKVLSNIDRVIYCTGYLYSVPFPSLAKLKSPETKLIDDGSHVHNVYQHIFYIPDPTLAFVGLALHVVPFPTSQAQAAFLARVWSGRLKLPSKEEQLKWQDELMFSLSGANNMYHSLDYPKDATYINKLHDWCKQATPVLEEEFPSPYWGEKERSIRENMWSIRAKFFGIEPPK
Protein: Small ribosomal subunit protein mS29 (Q9W253)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS16m
- LD06441p
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS6m
- GH07821p
Sequence:
MKMIRNRFGSLSRVSAQLQRHVQQMSTNAAASPAEGATISEFRTAVSNPGEHSAMQVAKFYTIPAEQKKQIFTGGGLPKQYEQQIKTFTEACLMVRNPALELLQYIKDGDLTKPVVRYVLYGENGTGKTLTMAHVLHYGALNDFLLVHVPWAPNWMKRPKEASNAAGQEGMIDLPFDAAAWLVHFKTQNGPLLQRLQLKTSKEYVWSKRESTPAGSSLIELVEHGIARIKYASETTAALIAELKQLSTAGQCKVMVAIDGFNAFFHPVTRIFSDNKQLVTPDRVTLTQPFLDITNYDWTNGVCILSVDKIAMTEGHMDSYMPRYLLGKEGFEHLDPFVPIHVENYTDKEFHSYISYYLDRHWINKTPQGFEEQLKFMSNKNPYSLMQLVKAL
Protein: Calpastatin (Calpain inhibitor) (P27321)
Organism: Rattus norvegicus (Rat)
Function: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Interaction partners:
- Calpain-2 catalytic subunit
- Calpain small subunit 1
- Calpain-1 catalytic subunit
- Calpain-3
Sequence:
MSRPGPKPAASSRPRRGAAASHTQEHVNEKNIGSSSKPAEKKGSDEVTASSAATGTSPRMSTTGAKAVKIESEKSQSSEPPVIHEKKPKGKPKEGSEPQTLPKHASDTGSKHAHKEKALSRSNEQIVSEKSSESKTKFQDAPSADGESVAGGVTVATASDKVVVKKKEKKSLTPTLPMESTLNKLSDKSGVNAALDDLIDTLGECEDTNKDDPPYTGPVVLDPMDSTYLEALGIKEGTIPPEYRKLLEKNEAITGPLPDSPKPMGIDHAIDALSSDFTCSSPTGKQTEKEKSTGESSKAQSAGVTRSAVPPQEKKRKVEEEVMNDQALQALSDSLGTRQPDPQSHLRQAKQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKCLSESELIGELSADFVQPTYQEKPSMPAAKIKKGVVPDDAVETLARSLGTRKEDPEDEKSLVDKVKEKAKEEDHEKLGEKEETIPPDYRLEIVKDKDGKPLLPKEAEEQLPPLSDDFLLDALSQDFSSPANILSLGFEDAKLSAAVSETVSQVPAPSNHTAAPPPGTERRDKELDDALDELSDSLGQRQPDPDENKPLDDKVKEKIKAEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPLTKNTEKLGQDQDPIDALSEDLDSCPPTTETSQNTTKEKGKKTSSSKASKNEEKTKDSSKKTEEVPKPKVDEDAT
Protein: RE23625p (RE52196p) (Uncharacterized protein, isoform B) (Q8IQW5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Hsc70Cb, isoform G
- Heat shock 70 kDa protein cognate 4
- MAP kinase-activated protein kinase 2
- IP07647p
- Heat shock protein 27
- Eukaryotic translation initiation factor 4G1, isoform B
- Protein lethal
- TAR DNA-binding protein 43
- E3 ubiquitin-protein ligase CHIP
- DnaJ-like-2, isoform A
Sequence:
MAEANKRNIPIKLGDFSVIDTEFSNIRERFDSEMRKMEEEMAKFRHELMNREANFFESTSSTKKTTTTSSTTNSALPSRIPKQQNYVSDISSPLIQDEGDNKVLKLRFDVSQYAPEEIVVKTVDQKLLVHAKHEEKSDTKSVYREYNREFLLPKGVNPESIRSSLSKDGVLTVDAPLPALTAGETLIPIAHK
Protein: Hepatocyte nuclear factor 1-beta (Transcription factor 2) (A0A0C4DGS8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHSLNPLLSHGSPHHQPSSSPPNKLSGVRYSQQGNNEITSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHNLLSPDGKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQMSSTSLVMPTHHLLRAQQQGPCFPHHHPLGSCHGKAQ
Protein: Small proline-rich protein 2A3 (Q4KL71)
Organism: Mus musculus (Mouse)
Function: Gut bactericidal protein that selectively kills Gram-positive bacteria by binding to negatively charged lipids on bacterial membranes, leading to bacterial membrane permeabilization and disruption. Specifically binds lipids bearing negatively charged headgroups, such as phosphatidic acid, phosphatidylserine (PS), cardiolipin (CL), and phosphatidylinositol phosphates, but not to zwitterionic or neutral lipids (By similarity). Induced by type-2 cytokines in response to helminth infection and is required to protect against helminth-induced bacterial invasion of intestinal tissue. May also be involved in the development of the cornified envelope of squamous epithelia; however, additional evidences are required to confirm this result in vivo (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:34735226}. Secreted, extracellular space {ECO:0000269|PubMed:34735226}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:34735226}. Note=Present in intestinal secretory epithelial cells and is secreted into the intestinal lumen. {ECO:0000269|PubMed:34735226}.
Interaction partners:
- Small proline-rich protein 3
Sequence:
MSYYQQQCNQPCRPPPVCPPPKCPEPCPPQVWPGPCRPVMCFEPCLPSVWPGPCRPVVCYEQCPPQPWQSTCPPVQFPPCQQK
Protein: BRCA1 associated RING domain 1 (A0A087X2H0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLRNLLHDNELSDLKEDKPRKSLFNDAGNKKNSIKMWFSPRSKKVRYVVSKASVQTQPAIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKKKTLAEINQKWNLEAEKEDGEFDSKEESKQKLVSFCSQPSVISSPQINGEIDLLASGSLTESECFGSLTEVSLPLAEQIESPDTKSRNEVVTPEKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTGQRRDGPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHPERVRQGKVWKAPSSWFIDCVMSFELLPLDS
Protein: Amino acid transporter, putative (Q57V86)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTSIKTKSPTSVTYPRNDHGSAEVVNPNPEAPLSQNELKNSGGCFARVSLFMATIIPPGGIAASAFNIAASSVGAGIIGLPSAANSSGLVMAMIYLIIITAMSVFTMHNLAVVADKTNVYTYEGVARVLLGRWGKYYVAVVRAFHGFSACVAYVISVGDILSATLKGTNAPDFLKQKSGNRLLTIGMWLCFMLPLVIPRRIDSLRYVSTFAVSFMVYLVIAIVVHSCMNGLPENIKNVSVGKDDNAEIILFNSGNRAIEGLGVIMFAYVCQVVALEVYENMTNRSVGRFVIASAIALGICFTLYVMTSFFGYMDFGRAVTGSVLLMYDPVNEPAIMVGFVGVLVKLCVSYAILAMACRNALYDVVGWDADKVAFWKHCIAVVTLSVVMLLCGLFIPKINTVLGFAGSISGGSLGFILPSLLVMYSGGFTWQKVGPFYYLTTYAVLLTGVIAIVFGTGCAIWGTFTG
Protein: Leukocyte surface antigen CD47 (Integrin-associated protein) (IAP) (CD antigen CD47) (Q61735)
Organism: Mus musculus (Mouse)
Function: Adhesive protein that mediates cell-to-cell interactions (By similarity). Acts as receptor for thrombospondin THBS1 and as modulator of integrin signaling through the activation of heterotrimeric G proteins (By similarity). Involved in signal transduction, cardiovascular homeostasis, inflammation, apoptosis, angiogenesis, cellular self-renewal, and immunoregulation. Plays a role in modulating pulmonary endothelin EDN1 signaling. Modulates nitrous oxide (NO) signaling, in response to THBS1, hence playing a role as a pressor agent, supporting blood pressure. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells (By similarity). Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation (By similarity). Positively modulates FAS-dependent apoptosis in T-cells, perhaps by enhancing FAS clustering. Plays a role in suppressing angiogenesis and may be involved in metabolic dysregulation during normal aging. In response to THBS1, negatively modulates wound healing. Inhibits stem cell self-renewal, in response to THBS1, probably by regulation of the stem cell transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4. May play a role in membrane transport and/or integrin dependent signal transduction (By similarity). May prevent premature elimination of red blood cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7691831}; Multi-pass membrane protein {ECO:0000269|PubMed:7691831}.
Interaction partners:
- Thrombospondin-1
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Scavenger receptor class B member 1
- Platelet glycoprotein 4
- Cell surface glycoprotein CD200 receptor 1
- Receptor-type tyrosine-protein phosphatase C
- Thrombospondin-2
- Vascular endothelial growth factor receptor 2
- Thrombospondin-4
- Cartilage oligomeric matrix protein
Sequence:
MWPLAAALLLGSCCCGSAQLLFSNVNSIEFTSCNETVVIPCIVRNVEAQSTEEMFVKWKLNKSYIFIYDGNKNSTTTDQNFTSAKISVSDLINGIASLKMDKRDAMVGNYTCEVTELSREGKTVIELKNRTVSWFSPNEKILIVIFPILAILLFWGKFGILTLKYKSSHTNKRIILLLVAGLVLTVIVVVGAILLIPGEKPVKNASGLGLIVISTGILILLQYNVFMTAFGMTSFTIAILITQVLGYVLALVGLCLCIMACEPVHGPLLISGLGIIALAELLGLVYMKFVASNQRTIQPPRNR
Protein: Serine/threonine transporter SstT (Na(+)/serine-threonine symporter) (Q5F5G9)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Function: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01582}.
Interaction partners:
Sequence:
MAFGKSLFHAIGRVSLVRQIAAGLALGIVIGSVSPQLGLAAGLFGSLFVGALKAVAPVLVFILVAATIAQHQKGNKAHIRPIIVLYLIGTFSAALTAVIAGMVFPTHIVLAGAGDVSAAPPSGIVEVLKSLLMNLVANPINAIANANYIGILAWALVLGAALRNHGSDVTRQVVADLAEAVSTVVKWIIRFAPLGIFGLVSSTIAETGFGALAGYAKLLAVLLGCMAFIALAVNPAIVWWKIRRNPYPLVFTCLRESGVYAFFTRSSAANIPVNMALAKKLGLHEDTYSISIPLGATVNMGGAAITITVLAMAAAHTQGIQVDFATALLLSLVATVSACGASGVAGGSLLLIPLACSLFGISNDVAMQVVAVGFIIGVIQDSAETALNSSTDVLFTAAADLGRQRNRAE
Protein: Signal transducer and activator of transcription (Q8AW20)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MSQWKQVQQLDIKFLEQVDYFYDDNFPMELRQVLANWIESQDWETASNHESMATVLFNNFLIQLERQCSQEQNFLHRHNLKRIFHQIQVKYKANPLQMAAVICNCLREERRILSTASMQEQGPLEKSMQNSAALEKQKVLDNKVAVIRSSVQMLDQAVKYLEDMQDDFDFRYKTLQLRDPLERNSSSMKQEVTTLQEILNRLDFKRKANVIKEIDALISSQLNPELKEWKRRQQIACIGGPVLIGLDQLQNWFTLTAQSLFQIKRQLDKLGELILKVTYESDPIPLQRPQMEEQVKYLIYHLIKSSFVVEKQPCMPTHLQKPLIIKTQVQFTTKVRLLVKLPEVDYQLKVKTTFDKNRQFFILTNNTKVMDVEESTGCLSVEFRHLQLKERKCPTGGKGNEGPLSVTEELHSLNFEAMLMLQGLDIDLETCSLPLVVISNVSQLPGGWASVMWYNLLTDDPKNLAFFSNPLRASWSQLSEVLSWQFSSFAGRGLNKEQLNMLGDKLLGQHGSYNDCQVSWSKFCKEVIPGKSFSFWMWLDSILDLIKKHLLPVWIDGCIMGFVSKEMERALLKEKEPGTFLLRFSESHLGGITFTWVEQDENGDPKFISVEPYTKNRLNALPIADIIRDYKVIADGVVPENPLNFLYPDIPKDEAFGKHYNSQQNKG
Protein: Very long chain fatty acid elongase 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Elongation of very long chain fatty acids protein 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (Q9JLJ4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Essential for the formation of C24:5(n-6) up to C30:5(n-6) PUFAs in testis, these fatty acids being indispensable for normal spermatogenesis and fertility.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}.
Interaction partners:
- Acyl-CoA
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very long chain fatty acid elongase 5
- Acyl-CoA 6-desaturase
Sequence:
MEQLKAFDNEVNAFLDNMFGPRDSRVRGWFLLDSYLPTFILTITYLLSIWLGNKYMKNRPALSLRGILTLYNLAITLLSAYMLVELILSSWEGGYNLQCQNLDSAGEGDVRVAKVLWWYYFSKLVEFLDTIFFVLRKKTNQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHKYLWWKKYLTQAQLVQFVLTITHTLSAVVKPCGFPFGCLIFQSSYMMTLVILFLNFYIQTYRKKPVKKELQEKEVKNGFPKAHLIVANGMTDKKAQ
Protein: B3 domain-containing protein At3g18960 (Q84R27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Uncharacterized protein T20N10_120
- Zinc-finger homeodomain protein 1
- B3 domain-containing protein REM7
- B3 domain-containing protein REM19
- Hapless protein
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS21z
Sequence:
MVTTQNTKARVTSVSHRRSQQDPESPVKKFFKLVLPSTMKDKMMKIPPRFVKLQGSKLSEVVTLETPAGFKRSIKLKRIGEEIWFHEGWSEFAEAHSIEEGHFLLFEYKENSSFRVIIFNVSACETKYPLDAVHIIDSDDDIIDITGKEFVGTQGTRKNNQSVNGGDTEHKSKKRSRDIELDKILHDLDVMNPMHVLKEEEEDKRVFRG
Protein: Sortilin 1 (E1BKZ9)
Organism: Bos taurus (Bovine)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGAERPGSAYPRSAGLRLGGVARRLRGWAGAPGCRCPRRRHSAAMERPGGAADSLSRWPHGLGLLLFLLQLLPPATLGQDRLDAPPPPAAPLSRWSGPVGVSWGLRAAAPGGPAPRGGRWRRSAPGEDEDCGGVQDFVSRLANNTHQHVFDDLSGSVSLSWVGDSTGIILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITNLINNTFIRTEFGMAIGPENSGKVILTAEVSGGSHGGRIFRSSDFAKNFVQTNLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGGKWEEIHKAVCLAKWGSENIIFFTTYVNGSCKADLGALELRRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYMTSVLSEDNSIQTMITFDQGGRWKHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWMKMLEGPHYYTILDSGGIIVAIEHSSHPINVIKFSTDEGQCWQTYTFTKEPIYFTGLASEPGARSMNISIWGFTESFLARQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPGDYGDGCILGYKEQYLRLRKSSVCQNGRNYVVTKQPSVCPCSLEDFLCDFGYFRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPGDKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILATVGLMLVTVIAGVLIVKKYVCGGRFLVHRYSVLQQHAEANGVDGVDALDTASHTHKSGYHDDSDEDLLE
Protein: Iron-sulfur assembly protein 1 (Q07821)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the assembly of mitochondrial and cytoplasmic iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Iron-sulfur assembly protein 2
- NifU-like protein
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- Cysteine desulfurase, mitochondrial
- Adrenodoxin homolog, mitochondrial
- Iron sulfur cluster assembly protein 2, mitochondrial
- J-type co-chaperone JAC1, mitochondrial
- Monothiol glutaredoxin-5
- Frataxin homolog, mitochondrial
Sequence:
MINTGRSRNSVLLAHRFLSTGGFWRGGTNGTMSRTINNVNPFKLKFIPKTVPAAADSVSPDSQRPGKKPFKFIVSNQSKSSKASKSPKWSSYAFPSRETIKSHEEAIKKQNKAIDEQIAAAVSKNDCSCTEPPKKRKRKLRPRKALITLSPKAIKHLRALLAQPEPKLIRVSARNRGCSGLTYDLQYITEPGKFDEVVEQDGVKIVIDSKALFSIIGSEMDWIDDKLASKFVFKNPNSKGTCGCGESFMV
Protein: Krueppel-like factor 13 (Basic transcription element-binding protein 3) (BTE-binding protein 3) (Novel Sp1-like zinc finger transcription factor 1) (RANTES factor of late activated T-lymphocytes 1) (RFLAT-1) (Transcription factor BTEB3) (Transcription factor NSLP1) (Q9Y2Y9)
Organism: Homo sapiens (Human)
Function: Represses transcription by binding to the BTE site, a GC-rich DNA element, in competition with the activator SP1. It also represses transcription by interacting with the corepressor Sin3A and HDAC1. Activates RANTES expression in T-cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:17513757}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Myotubularin-related protein 10
Sequence:
MAAAAYVDHFAAECLVSMSSRAVVHGPREGPESRPEGAAVAATPTLPRVEERRDGKDSASLFVVARILADLNQQAPAPAPAERREGAAARKARTPCRLPPPAPEPTSPGAEGAAAAPPSPAWSEPEPEAGLEPEREPGPAGSGEPGLRQRVRRGRSRADLESPQRKHKCHYAGCEKVYGKSSHLKAHLRTHTGERPFACSWQDCNKKFARSDELARHYRTHTGEKKFSCPICEKRFMRSDHLTKHARRHANFHPGMLQRRGGGSRTGSLSDYSRSDASSPTISPASSP
Protein: Rifin (O96109)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MMLNYTNILLFYLSLNILSSSSEVYNQRNHYITRTPKATTRTLCECELYAPSNYDNDPEMQKVMENYNRQTSQRFEEYNERVIKNRQKCKEQCDKEIQKIILKDKLEKELMNKFATLQTDIQSDAIPTCVCEKSVADKVEKTCLKCGGVLGSGIAPSVGLLGTVAIDQWTNAALLDAAQKGIQAGIDTVVAELEYVAERFDDIGINIVGMINKETYRCPQALIESIYAAKQKVCDNVGNPAPTCHRVGQDGTSIWFRPEVLKATQDGIDAAETVEKAEIVLINEESAHLYSAIGYSVLAILIIVLVMLIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Decapping and exoribonuclease protein (DXO) (EC 3.6.1.-) (5'-3' exoribonuclease DXO) (EC 3.1.13.-) (Dom-3 homolog Z) (NAD-capped RNA hydrolase DXO) (DeNADding enzyme DXO) (EC 3.6.1.-) (O70348)
Organism: Mus musculus (Mouse)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to environmental stress (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA. Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates. Exhibits decapping activity towards FAD-capped RNAs. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O77932}.
Interaction partners:
- 5'-3' exoribonuclease 2
- Exosome complex exonuclease RRP42
- Regulation of nuclear pre-mRNA domain-containing protein 1A
- Fas-binding factor 1
- Regulation of nuclear pre-mRNA domain-containing protein 1B
- RNA/RNP complex-1-interacting phosphatase
- m7GpppN-mRNA hydrolase
- 5'-3' exoribonuclease 1
Sequence:
MEPRGTKRKAEKTEVEKPLNKLPRAVPSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPINGPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQLEGGPGWLAGATVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPLLRELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLFSGEVDCLNPQAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPHVVAGFRNPEGFVCSLKTFPTMEMFENVRNDREGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHRDAPYAFLPSWYVETMTQDLPPLSKTPSPKD
Protein: Catabolite repression control protein (Exodeoxyribonuclease (EC 3.1.11.2)) (Q51380)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MRIISVNVNGIQAAAERGLLSWLQAQNADVICLQDTRASAFDLDDPSFQLDGYFLYACDAELPEQGGVALYSRLQPKAVISGLGFETADRYGRYLQADFDKVSIATLLLPSGQSGDESLNQKFKFMDDFTHYLSKQRRKRREYIYCGSLYVAHQKMDVKNWRECQQMPGFLAPERAWLDEVFGNLGYADALREVSREGDQFSWWPDSEQAEMLNLGWRFDYQVLTPGLRRFVRNAKLPRQPRFSQHAPLIVDYDWQLSI