wanglab/gogpt-training-data huggingface dataset:
Protein: Protein translocase subunit SecA (EC 7.4.2.8) (Q7WWK0)
Organism: Streptococcus parasanguinis
Subcellular location: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Note=Distribution is 50-50. {ECO:0000256|HAMAP-Rule:MF_01382}.
Interaction partners:
Sequence:
MANLLKTIIENDRGEIKRLEKMADKVFSYEEQMAALTDDELKAKTVEFKQRYQDGESLDDLLYEAFAVVREGAKRVLGLFPYKVQVMGGIVLHHGDVPEMRTGEGKTLTATMPVYLNALSGKGVHVVTVNEYLTERDATEMGELYSWLGLSVGINLAAKSPAEKKEAYLCDITYSTNSEIGFDYLRDNMVVRAENMVQRPLNYALVDEVDSILIDEARTPLIVSGQTASDTSQLYHMADAYVKTLTEDDYIIDVPSKTIGLSDSGIDKAESYFNLENLYDIENVALTHFIDNALRANYIMILDIDYVVSEDQEILIVDQFTGRTMEGRRYSDGLHQAIEAKEGVPVQEETKTSASITYQNLFRMYKKLSGMTGTGKTEEEEFREIYNIRVIPIPTNRPIARIDHPDLLYPSLKSKFKAVVEDVKSRHEKGQPVLVGTVAVETSDYLSQLLVQAGVPHEVLNAKNHYKEAQIIMNAGQRGAVTIATNMAGRGTDIKLGEGVRELGGLCVIGTERHESRRIDNQLRGRSGRQGDPGESQFYLSLEDELMRRFGSERIKAVLDRFKLSEEESVIRSNMFTRQVEGAQKRVEGNNYDTRKQVLQYDDVMREQREIIYAERYDVITANRDLAPEIKAMIKRTIKRIVEGASHSSKEERIEAILNFAKYNLVPEDTISESDIEGKSDKEVIDYLYARAEEIYASQVAKLRDEESVQEFQKVLILRVVDSKWTDHIDALDQLRNAVGLRGYAQNNPVVEYQSESFRMFNDMIGSIEFDVTRLMMKAQIHEQERPRTEHSISTTATRNIAAQQDIPSGIDLSQVKRNDLCPCGSGKKFKNCHGRKF
Protein: NF-kappa-B inhibitor zeta (I-kappa-B-zeta) (IkB-zeta) (IkappaBzeta) (IL-1 inducible nuclear ankyrin-repeat protein) (INAP) (Molecule possessing ankyrin repeats induced by lipopolysaccharide) (MAIL) (Q9EST8)
Organism: Mus musculus (Mouse)
Function: Involved in regulation of NF-kappa-B transcription factor complexes. Inhibits NF-kappa-B activity without affecting its nuclear translocation upon stimulation. Inhibits DNA-binding of RELA and NFKB1/p50, and of the NF-kappa-B p65-p50 heterodimer and the NF-kappa-B p50-p50 homodimer. Seems also to activate NF-kappa-B-mediated transcription. In vitro, upon association with NFKB1/p50 has transcriptional activation activity and, together with NFKB1/p50 and RELA, is recruited to LCN2 promoters (By similarity). Promotes transcription of LCN2 and DEFB4 (By similarity). Is recruited to IL-6 promoters and activates IL-6 but decreases TNF-alpha production in response to LPS. Seems to be involved in the induction of inflammatory genes activated through TLR/IL-1 receptor signaling. Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR).
Subcellular location: Nucleus {ECO:0000269|PubMed:11086164, ECO:0000269|PubMed:11278262, ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:15618216}.
Interaction partners:
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Akirin-2
- Proto-oncogene c-Rel
- Tumor necrosis factor alpha-induced protein 3
- Endoribonuclease ZC3H12A
- Transcription factor RelB
- NF-kappa-B inhibitor alpha
- Phospholipase A and acyltransferase 5
- Growth-regulated alpha protein
Sequence:
MIVDKLLDDSRGGEGLLDAAGDCGLMTSPLNLAYFYGASPPSAPGAGDTGYLSAVPSAPGSPGSDSSDFSSTSSVSSCGAVESRPRGGARAERPQVEPHMGVGRQQRGPFQGVRVKNSVKELLLHIRSNKQKASGQPVDEFKTQSVNIEQLTDLKSAVSAVGKRKGPDPLSDGPVCKRPALLPSHFVTSPQTPTPGESMEDVRHSESKLDSSAALLQNIINIKNECNPVSLNTVQVSWMSPTVPQNSPRDQCQDFHGGQAFSPPQKYQPFQVSGSPQMMDQASMYQYSPQTQNMQQPPPLPPQQQHQQNYPHNSPLQFSPYSRMSQSPKYDSNLFDTHEPQFCTGQSFVSLLTGPGEPESLAVPVPAPTSIPPQTETQLQTFSLMPSNACEAVVGVHDVGSHSLGTSLSLQNIMGSPMNTTQLGKSFFQWQVEQEESKLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGAVRSNQFVDLEATNYDGLTPLHCAVVAHNAVVHELQRNRQSHSPEVQDLLLRNKSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSCLSFVNAKAYNGNTALHVAASLQYRVTQLDAVRLLMRKGADPSTRNLENEQPVHLVPDGPVGEQIRRILKGKSIQQRAPPY
Protein: Carboxysome shell protein CcmK2 (Carbon dioxide-concentrating mechanism protein CcmK2) (P72761)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. The central pore probably regulates metabolite flux. Hexamers make sheets that form the facets of the polyhedral carboxysome (Probable).
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000305|PubMed:16081736, ECO:0000305|PubMed:17993516, ECO:0000305|PubMed:19177356, ECO:0000305|PubMed:19844993}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305|PubMed:17993516}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome assembly protein CcmM
- Carboxysome assembly protein CcmN
- Ribulose bisphosphate carboxylase large chain
- Ribulose bisphosphate carboxylase small subunit
- Carboxysome shell protein CcmK1
Sequence:
MSIAVGMIETRGFPAVVEAADSMVKAARVTLVGYEKIGSGRVTVIVRGDVSEVQASVSAGIEAANRVNGGEVLSTHIIARPHENLEYVLPIRYTEEVEQFRTY
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (D6XFK8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar protein, putative
- Ribosome biogenesis protein BOP1 homolog
- RNA-binding protein, putative
- Pescadillo homolog
- Nop14-like protein
- Sas10 C-terminal domain-containing protein
- Nucleolar complex protein 2
- RNA helicase
- U3 small nucleolar RNA-associated protein 14
- BING4 C-terminal domain-containing protein
Sequence:
MQRNVIQSNSGRGLRSILDQYEDFKLIMQLRKNGRGNYYRYQQKLWPSAEALERDMTERLYSSTERTPLALLPQPKRAPSPRTCVLEGCGAAALLEGAENAVQISEDLNDNQKEVNEPLDLTDSTETMFAELYGTDQSINNKIITDNDLQGTVLEAAQQRARTLIFNDLRVNELATSPAVASTNSRRTTTILSAKDKGSMAWEALGLCPTLSKQVIAKYSAAPTRLQCRLLPALLHEDHNDVLFNGVTGSGKTSALLLALLQAVRNESAGLNVFVASNAITAMRARDQLQALCGELGGAMVDRPRDDFTWLFMGIFSGEYEAYYRTLRRSLNSDHGPVRIFITTADTFCQLLFEKKMEFEAFGYLRRVYVDDVGVQLPMVPPHAPVHEMRERLRNPLPCELLLGTLHQLPGPHIRSILQLGLVSADMETALKDHLKSLCVKLERHTIVLSAVRIPSTIHCLFSFHLAHEDVYEYVVQLIWNARATIPGRAVIYVRYEDNILQVRTKLRQLGMDVKLFSEVYHDGVFRDSWKFLLLHESEAFGVDLPLVSHVFITFCPHSTCSFQHMCGRTGRLGNVGWVYTITDKREAKAVREVVTQLEVDFCSHVVDSNLAQVPPSDMDRLTKEFELYGLDPQYAVRQHYVVQSENPDMAYRSREFFSKPAEKQFQMEDYTPTPVLHRRFVNAKKLAKDVERDPSVALTLQKEGLLNSKLAPTKKMRNLLNNKSRSFNAALYGMKSNK
Protein: Integrin alpha L (Q3T1L6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MSFRIPGPRLLLLGLQLFVNAWSYNLDTRHAQSFLTQAGRHFGYQVLQFGDGVVVGAPGEGNSTGNLYHCHPSSGSCQPVHLGSNHTSKYLGMTMVTDAAKGSLLACDPGLSRTCDQNPYLSGLCYLFSQSLGKPILQNRPAYQECMKGNVDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSNTSYQFAAVQFSTECKTEFTFLDYIKLNKNPDVLLGNVTPMFLLTNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDAAQDITRYIIGIGKHFSTTQKQEKLHIFASKPVEEFVKILDTFEKLKDLFTDLQRKIYAIEGTSKQDLASFNMELSSSGISADLSKGHAVVGAVGAKDWAGGFLDLHEDLEGATFVGQEPLTSDERGGYLGYTVAWLTSRSSRPLLAAGAPRYQHVGQVLLFQAPEAGGHWNQTQKIEGTQIGSYFGGELCSVDLHQDGETDLLLIGAPLFYGEQRGGRVSVYQRRRSLFEMVSELQGDPGYPLGRFGAAISALTDINGDGLTDVAVGAPLEEQGAVYIFNGKPGGFSSQSSQRIPGTQVSPGVRWFGRSIHGVKDLGGDRLADVVVGAEGQVIVLSSRPVVDIVTELSFSPDEIPVHEVECSYSASQEQKEGVKLKVCFQIRPLTSQFQGRLLANLSYTLQLDGHRTRSRGLFPGGSRELGGNTFVTPDRSCMDFHFHFPICIQDLISPINVSLNFSLLEEEGSPRDQKGGRDMQPILRPSIHAVTKEIPFEKNCGEDKKCEADLALSPPARSGVLRLMSSASLAVEWTLRNLGEDAYWVRLDLDFPRGLSFRKVEMLQPHSQIPVSCEELTEESSLLTKTLKCNVSSPIFKAGKQMTLQVMFNTLLNSSWGDFVELNGTVHCENENSSLGKDNSATTRIPVLYPVNILTEDQENSTLYISFTPKGPKTQQVQHIYKVRIQPSAYDHNMPALEALVEVPQPHSEGPIAHTWTVHTDPLVTCHCEDLKKPTREAEPCLPGVQFRCPIVFRQETFIRVAGTVELSEKIKASSTLSLCSSLSVSFNSSKHFHLYGSKASKAQVLMKVDMIYEKEMLHLYVLSGIGGLLLLSLIFLALYKVGFFKRKLKEKMEADGGVPNGSPGEDADPLAVPGEETKDMGCLEPLRESDKD
Protein: Transmembrane protein 9 (B1ALM7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSM
Protein: Serglycin (Hematopoietic proteoglycan core protein) (Platelet proteoglycan core protein) (P.PG) (Secretory granule proteoglycan core protein) (P10124)
Organism: Homo sapiens (Human)
Function: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:11154222}. Cytolytic granule {ECO:0000269|PubMed:11154222}. Secreted, extracellular space {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:16870619}. Golgi apparatus {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T lymphocytes from where it is secreted upon cell activation (By similarity). Secreted constitutively by endothelial cells and macrophages (PubMed:11154222). Located to Golgi apparatus during neutrophil differentiation (PubMed:15136585). {ECO:0000250|UniProtKB:P13609, ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}.
Interaction partners:
- CD44 antigen
- Granzyme B
- Perforin-1
- Lysosomal-associated transmembrane protein 5
- Mast cell carboxypeptidase A
Sequence:
MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFML
Protein: T-cell leukemia translocation-altered gene protein (T-cell leukemia translocation-associated gene protein) (P57738)
Organism: Homo sapiens (Human)
Function: May be required for cellular fusion during osteoclastogenesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAESWSGQALQALPATVLGALGSEFLREWEAQDMRVTLFKLLLLWLVLSLLGIQLAWGFYGNTVTGLYHRPGLGGQNGSTPDGSTHFPSWEMAANEPLKTHRE
Protein: Gamma-tubulin complex component 3 (GCP-3) (hGCP3) (Gamma-ring complex protein 104 kDa) (h104p) (hGrip104) (Spindle pole body protein Spc98 homolog) (hSpc98) (Q96CW5)
Organism: Homo sapiens (Human)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Interaction partners:
- Mitotic-spindle organizing protein 1
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
- Gamma-tubulin complex component 6
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 2
- Tubulin gamma-2 chain
- Mitotic spindle organizing protein 2B
- Protein NEDD1
- Actin, cytoplasmic 1
Sequence:
MATPDQKSPNVLLQNLCCRILGRSEADVAQQFQYAVRVIGSNFAPTVERDEFLVAEKIKKELIRQRREADAALFSELHRKLHSQGVLKNKWSILYLLLSLSEDPRRQPSKVSSYATLFAQALPRDAHSTPYYYARPQTLPLSYQDRSAQSAQSSGSVGSSGISSIGLCALSGPAPAPQSLLPGQSNQAPGVGDCLRQQLGSRLAWTLTANQPSSQATTSKGVPSAVSRNMTRSRREGDTGGTMEITEAALVRDILYVFQGIDGKNIKMNNTENCYKVEGKANLSRSLRDTAVRLSELGWLHNKIRRYTDQRSLDRSFGLVGQSFCAALHQELREYYRLLSVLHSQLQLEDDQGVNLGLESSLTLRRLLVWTYDPKIRLKTLAALVDHCQGRKGGELASAVHAYTKTGDPYMRSLVQHILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPTVKTDRLWHDKYTLRKSMIPSFMTMDQSRKVLLIGKSINFLHQVCHDQTPTTKMIAVTKSAESPQDAADLFTDLENAFQGKIDAAYFETSKYLLDVLNKKYSLLDHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNLTGILETAVRATNAQFDSPEILRRLDVRLLEVSPGDTGWDVFSLDYHVDGPIATVFTRECMSHYLRVFNFLWRAKRMEYILTDIRKGHMCNAKLLRNMPEFSGVLHQCHILASEMVHFIHQMQYYITFEVLECSWDELWNKVQQAQDLDHIIAAHEVFLDTIISRCLLDSDSRALLNQLRAVFDQIIELQNAQDAIYRAALEELQRRLQFEEKKKQREIEGQWGVTAAEEEEENKRIGEFKESIPKMCSQLRILTHFYQGIVQQFLVLLTTSSDESLRFLSFRLDFNEHYKAREPRLRVSLGTRGRRSSHT
Protein: Procollagen C-endopeptidase enhancer 1 (P14) (Procollagen COOH-terminal proteinase enhancer 1) (PCPE-1) (Procollagen C-proteinase enhancer 1) (Type 1 procollagen C-proteinase enhancer protein) (Type I procollagen COOH-terminal proteinase enhancer) (Q61398)
Organism: Mus musculus (Mouse)
Function: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity.
Subcellular location: Secreted.
Interaction partners:
- Collagen alpha-1
- Tolloid-like protein 2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
Sequence:
MLPAALTSFLGPFLLAWVLPLARGQTPNYTRPVFLCGGDVTGESGYVASEGFPNLYPPNKKCIWTITVPEGQTVSLSFRVFDMELHPSCRYDALEVFAGSGTSGQRLGRFCGTFRPAPVVAPGNQVTLRMTTDEGTGGRGFLLWYSGRATSGTEHQFCGGRMEKAQGTLTTPNWPESDYPPGISCSWHIIAPSNQVIMLTFGKFDVEPDTYCRYDSVSVFNGAVSDDSKRLGKFCGDKAPSPISSEGNELLVQFVSDLSVTADGFSASYRTLPRDAVEKESALSPGEDVQRGPQSRSDPKTGTGPKVKPPTKPKSQPAETPEASPATQATPVAPAAPSITCPKQYKRSGTLQSNFCSSSLVVTGTVKTMVRGPGEGLTVTVSLLGVYKTGGLDLPSPPSGTSLKLYVPCRQMPPMKKGASYLLMGQVEENRGPILPPESFVVLYRSNQDQILNNLSKRKCPSQPRTAA
Protein: Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin) (Rotamase A) (P9WHW3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Mycoketide-CoA synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycocerosic acid synthase-like polyketide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Phthioceranic/hydroxyphthioceranic acid synthase
- Chaperone protein HtpG
- RNA helicase
- Large ribosomal subunit protein uL14
- ATP-dependent RNA helicase DeaD
- Small ribosomal subunit protein uS12
Sequence:
MADCDSVTNSPLATATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGTKDYSTQNASGGPSGPFYDGAVFHRVIQGFMIQGGDPTGTGRGGPGYKFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGKTPHLNRRHTIFGEVIDAESQRVVEAISKTATDGNDRPTDPVVIESITIS
Protein: Zinc finger protein 628 (Zinc finger protein expressed in embryonal cells and certain adult organs) (Q8CJ78)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3'. Plays a role in spermiogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15556296}.
Interaction partners:
- Zinc finger protein 341
Sequence:
MAGSHVDMAPASTTEGTGEKPGPTAPAPTPAAQYECGECGKSFRWSSRLLHHQRTHTGERPYKCPDCPKAFKGSSALLYHQRGHTGERPYQCPDCPKAFKRSSLLQIHRSVHTGLRAFTCGQCGLAFKWSSHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRRHRHVHTGERPYTCGICGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHHRTHGPAPGPAPAPAPPGETSRADTKVLVSDAYLQPRSPPEPPAPPPQPPPVVPELFLAAAETTVELVYRCDGCEQGFSSEELLLEHQPCPGPPVATQSQDVPAELPQADSALPQPPPATPGPPNFACLPCGKSFRTVAGLSRHQHSHGAASGQAFRCGSCDGAFPQLASLLAHQQCHVEEAAAGRPPPQAEVAEVTCPQEPVAPATPAPPPPPPPAPVVSAERPYKCAECGKAFKGSSGLRYHLRDHTGERPYQCGECGKAFKRSSLLAIHQRVHTGLRAFTCGQCGLTFKWSSHYQYHLRLHSGERPYACTECGKAFRNTSCLRRHRHVHTGERPHSCSVCGKSFAQTSNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHSAERPFACPICGRGFVMAAYLQRHLRTHTPATTTSGTTGSAVASQPPAPLAAAPTPLAAQDVHVLPNLQATLSLEVAGGTAQPTPPGPAAPSSQTFLLVQTAQGLQLIPSSVQSPTPPPPPPPPKVILLPPASAGGPGSGAARPGPRSVGKAGQGTGVVWFPGPGGLGLQGGANAGASGGGQSLIVLQNVGSGETGPQEVSGVQLQPAQEVATVQLQPAQEVTTVQLQPAQEVTTVQLQPLTGQVSNSNGGAGTTEAPNLLLVQSGATEELLTGPGPGEVGDSEAGAGVVQDVLFETLQTDEGLQSVLVLSGADGEQTRLCVQEVETLSPGLAEPAATGPSGQKLLIIRSAPATDLLENSSVAGGTTTLQLLAPSAPGPVSAPVGVPVAPPSQMVQVVPAVAGPGVMAPQNLPSIQIVQTLPAVQLVHTF
Protein: PAN2-PAN3 deadenylation complex catalytic subunit pan2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) (P0C581)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pabp-1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by rgb-30/xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit pan3
- Polyadenylate-binding protein, cytoplasmic and nuclear
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
Sequence:
MDSRDWTQLGCVAYPSPIHPDYHAGPASTIAFDNQDELLWIGTQKGFAGSFIGRELKRFTAFRIHPETDGPLRQFLFVDKGVIFLGSRSVYMAARSGVPIWSIRHESMQDLRAMSFTSKGTSEILVAGWQNKMLVIDVNKGEVVKELPTQDQYSFLKMSRYICAATNKGTVNILDPITFTIKKQWQAHGAFINDLDTSNDFIVTCGGSHRQTHNTPAILDPYVKVFDLKNMSAMNPVPFAPLAAHVRMHPRMLTTAIVVNQAGQIHVTDLLNPSNSQVCYTQPQGVVLHFDVSRTGEGKALADNKHNTYVWGSPNKIQFTEIGIPPRLPDPPQPSLLPPDPDMLEELPLSRIGLPYYREQLFSALPPDIISDVGAPPQQIDPNILSTLTKTDWGYIGPNKTGLQRNQYMDTRSTMKTSNTIRAPKFLSEKARESQTGSEDNTLATNETAMMTPNNDHWSLRPEAPPEYRICEIKYSKFGVDDFDFGFFNNTPYPGLENNITNSYANSLLQVMHYTPLLRNMALQHAATACLADPCLLCELGYVFDMLQKGEGPSCHATNMLRALNHTSNASVSGVLEDIAKDKNPSTLVKNLTMFLFDKISQDYKGTPPISTELERTLFKLNQPPNPLDLVKRLLETDARYQIKCMHCQHVSPRTATTFVNKLCYPAAKPNIRGMKAQRITFSQVLKAGLENEAVNKGYCTKCQRYQNLDQRKIIFNIPAVLALCTEITTAEHRKLWSTPGWLPEEIGIIVDQGHVYCYEGDDLKLHLNRGIHNITVYSLVGTVVNVETKSPQKSHLVATVNVGRAEPESKDQDRWHLFNDFSVRGISKVEALTFNAAWKMPVVVMFQVKAANHRFNMDWKTRLDTSVLFRDNNPHALKTYELLDRETEIPGPDTVIAIDTEFIRLKEREIHIDEDGKSKTIRPISHAIARASVVRGQGSREGVAFIDDYIHIKETIVDYLTEWSGITPTDLDPINSQRNLVSPKTAYKKLWVLVNLGCKFLGHGLSQDFRVINIQVPRNQVIDTSIIFMKPPSQRKISLAFLAWYLLKEDIQQNTHDSIEDAQTALKLYRKYEEFMANGSFHDVLEALYKKGKTLNFKPPRISTGAAKDAGFGAVHRVGTPPVPAPGTTEGSFEISNSSTATTGGSALSATGGMGSASASSSMPSTPVRKPIGLGGPFTVAGVVKPSPATSLDNFGAGAVGTGITTAAATMGGGYGGYGTDGAYWGGPNDMAPTSMIGGSAFIPAKFPPGPPETRGFIPYRPQVLLAEREAAAAAAAAAAAAAANNDVGGRGGVACGNGGAGGEQGKQE
Protein: Phytochrome-interacting ankyrin-repeat protein 2 [Cleaved into: Protein ANKYRIN REPEAT 6, mitochondrial] (Q9FNP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes anthocyanin accumulation through interaction with PHYA, especially in response to far-red light, high light and sucrose treatment, probably by triggering A3G2XYLT/UF3GT expression. Required for gametophytes development as well as male-female gamete recognition during fertilization, possibly by regulating mitochondrial gene expression. Represses PHYA-mediated PIF3 phosphorylation.
Subcellular location: [Phytochrome-interacting ankyrin-repeat protein 2]: Cytoplasm {ECO:0000269|PubMed:21395597}. Nucleus {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:21395597}.; SUBCELLULAR LOCATION: [Protein ANKYRIN REPEAT 6, mitochondrial]: Mitochondrion {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:29312411}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Ankyrin
- Ankyrin repeat-containing protein BDA1
- Ankyrin repeat domain-containing protein, chloroplastic
- RNA polymerase sigma factor sigE, chloroplastic/mitochondrial
- AT3G13950 protein
Sequence:
MLQEPSAAFSLRRNSFRRRSPRSNVDDRGWNPLHIKARKGDLKSVKQLLDQGMDVNALAWGPKSKGVSALHLAAEGGHIEVMDLLLERGANIDAKTWGSCGWTPLHAAAKERKREAVKFLVENGAFLADDITDTRFNPPVHYCHGLEWAYEEMKKLNSESSSSSGGDTSSSSDN
Protein: Interferon lambda-2 (IFN-lambda-2) (Cytokine Zcyto20) (Interleukin-28A) (IL-28A) (Q8IZJ0)
Organism: Homo sapiens (Human)
Function: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression.
Subcellular location: Secreted {ECO:0000269|PubMed:12483210}.
Interaction partners:
- Interferon lambda receptor 1
- Interferon lambda-3
- Interleukin-10 receptor subunit beta
- Interferon lambda-1
- Interferon alpha/beta receptor 1
- Tyrosine-protein kinase JAK1
- Interleukin-22
- Interferon alpha/beta receptor 2
- Interleukin-20 receptor subunit alpha
- Interleukin-22 receptor subunit alpha-2
Sequence:
MKLDMTGDCTPVLVLMAAVLTVTGAVPVARLHGALPDARGCHIAQFKSLSPQELQAFKRAKDALEESLLLKDCRCHSRLFPRTWDLRQLQVRERPMALEAELALTLKVLEATADTDPALVDVLDQPLHTLHHILSQFRACIQPQPTAGPRTRGRLHHWLYRLQEAPKKESPGCLEASVTFNLFRLLTRDLNCVASGDLCV
Protein: RNA-editing complex protein MP18 (Q95W12)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLALTSRRLLLQQTFMRCCKSVNSVTLVGVVHDIQSGFVYEDAVTQFTLTTTSIDTTHPTQEVVVEKDHHAIRCFGELFSAEVKQKVKEGNVVCVNGRLRLSPQLEPSCNKHFYFPYIQVQPPHGQVAVIHGDRRTVPAAVNPAVEDIKSEKEGSGGDQSGVPS
Protein: Histone H2A type 1-A (H2A-clustered histone 1) (Histone H2A/r) (Q96QV6)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2B type 1-A
- Histone H2B type 2-E
- Histone H4
- Histone H2B type 1-C/E/F/G/I
- Histone H3.1
- Histone H1.1
- Histone deacetylase 1
- Histone deacetylase 3
- Histone deacetylase 2
- Histone H2B type 1-B
Sequence:
MSGRGKQGGKARAKSKSRSSRAGLQFPVGRIHRLLRKGNYAERIGAGAPVYLAAVLEYLTAEILELAGNASRDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHHHKAQSK