wanglab/gogpt-training-data huggingface dataset:
Protein: Intermediate capsid protein VP6 (B2BN53)
Organism: Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A)
Function: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus (By similarity). Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (By similarity). VP6 is required for the transcription activity of the DLP (By similarity).
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:19036817, ECO:0000269|PubMed:21157433}. Note=Component of the intermediate capsid (PubMed:19036817, PubMed:21157433). Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential). {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:19036817, ECO:0000269|PubMed:21157433, ECO:0000305}.
Interaction partners:
Sequence:
MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVQLRRVLTTATITLLPDAERFSFPRVINSADGATTWYFNPVILRPNNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATVGLTLRIESAVCESVLADASKTMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK
Protein: Phosphatase and actin regulator 2 (O75167)
Organism: Homo sapiens (Human)
Subcellular location: [Isoform 2]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Tropomodulin-3
Sequence:
MDNAVDGLDKASIANSDGPTAGSQTPPFKRKGKLSTIGKIFKPWKWRKKKTSDKFRETSAVLERKISTRQSREELIRRGVLKELPDQDGDVTVNFENSNGHMIPIGEESTREENVVKSEEGNGSVSEKTPPLEEQAEDKKENTENHSETPAAPALPPSAPPKPRPKPKPKKSPVPPKGATAGASHKGDEVPPIKKNTKAPGKQAPVPPPKPASRNTTREAAGSSHSKKTTGSKASASPSTSSTSSRPKASKETVSSKAGTVGTTKGKRKTDKQPITSHLSSDTTTSGTSDLKGEPAETRVESFKLEQTVPGAEEQNTGKFKSMVPPPPVAPAPSPLAPPLPLEDQCITASDTPVVLVSVGADLPVSALDPSQLLWAEEPTNRTTLYSGTGLSVNRENAKCFTTKEELGKTVPQLLTPGLMGESSESFSASEDEGHREYQANDSDSDGPILYTDDEDEDEDEDGSGESALASKIRRRDTLAIKLGNRPSKKELEDKNILQRTSEEERQEIRQQIGTKLVRRLSQRPTTEELEQRNILKQKNEEEEQEAKMELKRRLSRKLSLRPTVAELQARRILRFNEYVEVTDSPDYDRRADKPWARLTPADKAAIRKELNEFKSTEMEVHEESRQFTRFHRP
Protein: Guanine nucleotide-binding protein subunit gamma (A0A8I6GAY3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}.
Interaction partners:
Sequence:
PVPAAPQRAAPTQLQARVSSPPTAAVGRGDSVRGPWSEAEGVEETAPPTGPSAPPTREGRSRSGVGRRGRAVPGARRAGLPGGSGSGGEDGGGGDGREFTLPFKTWRHWPTQSLADFRKEESSKMSSKTASTNSTAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTCIIL
Protein: Coatomer subunit beta' (Q586P1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347, ECO:0000256|PIRNR:PIRNR005567}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347, ECO:0000256|PIRNR:PIRNR005567}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347, ECO:0000256|PIRNR:PIRNR005567}. Golgi apparatus membrane {ECO:0000256|PIRNR:PIRNR005567}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR005567}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR005567}. 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:0000256|PIRNR:PIRNR005567}.
Interaction partners:
- Coatomer subunit gamma
- Coatomer subunit epsilon
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit delta
- Coatomer subunit zeta
- ADP-ribosylation factor GTPase activating protein, putative
- ER lumen protein-retaining receptor
- Vesicle tethering protein Uso1/P115-like head domain-containing protein
- SEC7 domain-containing protein
Sequence:
MMSPPETLMVANSDRVKMVDMHPKEPLFLCSLYSGIINLWNFETQALLKSFDTGTGLPVRCVRFIPRLQSFACGTDDMQVRVFNYNTMERTRTFQAHDDYIRGIVAHETLPILLTCSDDMTIRQWDWSRDWALVETYEGHQHYVMGIAMNPKDPSTFATASLDCTVKVWSLNSPVSNFQLEGHEDGVNCVDYYPGGDKPYLLSGADDRTVRLWDYQTKACLQVFSHHTANVTAVLFHPSQPLLFTLAEDMEMKVITTDTHRLVLNLDHSRMNRGWSMTTKKHASALVVGYDGGTVVYKVGDDRPVFTMDSNGKILLVVGNDVRRVDAKGIPADVTDGDVLALPSKEMGTLESRPTAIVYGPSGQFVAALGESDFTILSSLSMRSKAFGKCMSFVWGPDNGSYAVMLSPREVRICKNFKDRGAISLVDSAERLFAGPLLGVCTASSLAFYDWATLSFIRQIDESPKAVQWTENGEFVAIVTDSAFFTLRFNSDDVVDYFDAHDTTPEEGLDFAFEVVEEVMESAKEVLWVSNCVVFINQAHRLCYYVAGEINSIAVVSRDQYLLGYLPKENRVLCIDKDLNITSYLIPLGIIECMTAVARGDLVAVQALVPPLGAREKLLVARFLQSRKYLELALEVTSEDDHRFELALQLGRLTMAEEIAKQSGSVGHWKQLADVALTKGAFQLAKEALCKCGDSNGLLLLYSCVGDMEAISKLGDTCVANGRLNIAFTCFHLTRRYADNVDLLCRTGKLAEAAFYARTHCHGKVDEVVEKWKLGLVRLPRVSEAIANPTAYPNLFPNMRMNAPAAAVVEGSTIKFENDLAATKNGSAVLSASGVGVGVGVGGDDDEWGEQ
Protein: Thyrotropin receptor (Thyroid-stimulating hormone receptor) (TSH-R) (P21463)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase (By similarity). Plays a central role in controlling thyroid cell metabolism.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}. Basolateral cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}.
Interaction partners:
- Thyrotropin subunit beta
- Glycoprotein hormones alpha chain
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- VIP peptides
- Thyroid peroxidase
- Natriuretic peptides A
- Gastric inhibitory polypeptide
Sequence:
MRPGSLLQLTLLLALPRSLWGRGCTSPPCECHQEDDFRVTCKELHQIPSLPPSTQTLKLIETHLKTIPSLAFSSLPNISRIYLSIDATLQRLEPHSFYNLSKMTHIEIRNTRSLTYIDPDALTELPLLKFLGIFNTGLRIFPDLTKIYSTDVFFILEITDNPYMTSVPENAFQGLCNETLTLKLYNNGFTSIQGHAFNGTKLDAVYLNKNKYLTAIDKDAFGGVYSGPTLLDVSSTSVTALPSKGLEHLKELIAKNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSIRNLRQRKSVNVMRGPVYQEYEEGLGDNHVGYKQNSKFQEGPSNSHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTVCGDNEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSPMALLGNVFVLFVLLTSHYKLTVPRFLMCNLAFADFCMGVYLLLIASVDLYTHTEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHAYTIMAGGWVSCFLLALLPMVGISSYAKVSICLPMDTDTPLALAYIALVLLLNVVAFVIVCSCYVKIYITVRNPQYNPRDKDTKIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSGVLLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGLCKHQAQAYQAQRVCPNNNTGIQIQKIPQDTRQSLPNVQDTYEPLGSSHLTPKLQGRISEEYTQTAL
Protein: Nucleoredoxin-like protein 1 (Thioredoxin-like protein 6) (Q96CM4)
Organism: Homo sapiens (Human)
Function: Plays an important role in retinal cone photoreceptor survival. In association with glucose transporter SLC16A1/GLUT1 and BSG, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors. May play a role in cone cell viability, slowing down cone degeneration, does not seem to play a role in degenerating rods (By similarity).
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q8VC33}.
Interaction partners:
- Visual system homeobox 1
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Visual system homeobox 2
- Thioredoxin
- Paired box protein Pax-4
Sequence:
MASLFSGRILIRNNSDQDELDTEAEVSRRLENRLVLLFFGAGACPQCQAFVPILKDFFVRLTDEFYVLRAAQLALVYVSQDSTEEQQDLFLKDMPKKWLFLPFEDDLRRDLGRQFSVERLPAVVVLKPDGDVLTRDGADEIQRLGTACFANWQEAAEVLDRNFQLPEDLEDQEPRSLTECLRRHKYRVEKAARGGRDPGGGGGEEGGAGGLF
Protein: General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) (P78347)
Organism: Homo sapiens (Human)
Function: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10373551}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00484, ECO:0000269|PubMed:10373551}. Note=Colocalizes with BTK in the cytoplasm.
Interaction partners:
- Tyrosine-protein kinase BTK
- Upstream stimulatory factor 1
- cGMP-dependent protein kinase 1
- General transcription factor II-I repeat domain-containing protein 1
- cGMP-dependent protein kinase 2
- Zinc finger MYM-type protein 3
- Histone deacetylase 3
- Histone deacetylase 2
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Zinc finger MYM-type protein 2
Sequence:
MAQVAMSTLPVEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKSTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVVVQGLPEGVAFKHPENYDLATLKWILENKAGISFIIKRPFLEPKKHVGGRVMVTDADRSILSPGGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQAGPSETDDVDEKQPLSKPLQGSHHSSEGNEGTEMEVPAEDSTQHVPSETSEDPEVEVTIEDDDYSPPSKRPKANELPQPPVPEPANAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAHPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVISYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNNNPQTSAVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKINSSPNVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQSESEGPVIQESAEPSQLEVPATEEIKETDGSSQIKQEPDPTW
Protein: Purpurin (Rbp4l) (Retinol binding protein 4, like precursor) (Retinol-binding protein 4,-like) (Q6PC07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Protein MIX23
Sequence:
MGFYKFALLVVFLSYIERCFSASCAVESFTVKDDFDPKRYAGKWYAQQKKDPEGLFLQDNISAEYTIDDDGTMTASSKGRVTLFGFWVVCADMAAQYSVPDPTTPAKMFMNYQGLASYLSSGGDNYWVIDTDYDNYAITYACRTLKDDGSCDDGYSLVFSRNPRGLPPAIQRLVRQKQDEICMAGQFQPVLQSGAC
Protein: TATA-binding protein-associated factor 2N (Q3V452)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSDSGSYSQSGGEQQSYSSYGNQGSQGYGQTPQGYSGYGQTTDSSYGQNYGGYSGYGQNQSGYSQSYGSYENQKQSSYGQQSYNNQGQQNTESSGGQGGRAPSYGQSDYGQQDSYDQQSGYDQHQGSYDEQSNYQQHDSYNQNQQSYHSQRENYSHHTQDDRRDVSRYGEDNRGYGGSQGGGRGRGGYDKDGRGPMTGSR
Protein: Glycolate oxidase 3 (GOX 3) (EC 1.1.3.15) (AtGLO5) (Peroxisomal (S)-2-hydroxy-acid oxidase GLO5) (Short chain alpha-hydroxy acid oxidase GLO5) (O49506)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants.
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
- Glutamate--glyoxylate aminotransferase 2
- Serine--glyoxylate aminotransferase
- Glyoxylate/hydroxypyruvate reductase A HPR2
- Malate synthase
- Glycerate dehydrogenase HPR, peroxisomal
- Isocitrate lyase
- Glutamate--glyoxylate aminotransferase 1
- Phosphoglycolate phosphatase 1A, chloroplastic
- Phosphoglycolate phosphatase 2
- Catalase-2
Sequence:
MEITNVMEYEKIAKEKLPKMVYDYYASGAEDQWTLQENRNAFSRILFRPRILIDVSKIDVSTTVLGFNISMPIMIAPTAMQKMAHPDGELATARATSAAGTIMTLSSWATCSVEEVASTGPGIRFFQLYVYKDRNVVIQLVKRAEEAGFKAIALTVDTPRLGRRESDIKNRFALPRGLTLKNFEGLDLGKIDKTNDSGLASYVAGQVDQSLSWKDIKWLQSITSLPILVKGVITAEDARIAVEYGAAGIIVSNHGARQLDYVPATIVALEEVVKAVEGRIPVFLDGGVRRGTDVFKALALGASGVFVGRPSLFSLAADGEAGVRKMLQMLRDEFELTMALSGCRSLREISRTHIKTDWDTPHYLSAKL
Protein: Two-pore potassium channel 5 (AtTPK5) (Calcium-activated outward-rectifying potassium channel 5, chloroplastic) (AtKCO5) (Q9S6Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable voltage-independent potassium-selective tonoplast ion channel.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16984403, ECO:0000269|PubMed:17764516}; Multi-pass membrane protein {ECO:0000269|PubMed:16984403, ECO:0000269|PubMed:17764516}.
Interaction partners:
- Potassium channel KAT3
- Potassium channel GORK channel)
- Potassium transporter 1
- Potassium channel SKOR
- Potassium transporter 6
Sequence:
MEPLISPQPRFRLQPIPENPSSSSSSASITIPRSISNTSFFHEISQERLLLHHQDLEQSVQDDKEDQDSDSDETNRFLSQTRPLHRSRTAPAMVIIKDLRTKPPETKKPSPVSKSIIRQAIFLLIVYLTLGVSIYSFNRDHYSGIETHPVVDALYFCIVTMCTIGYGDIAPLTPWTKIFAVVFVLFGFGFLDILLSGVVNYVLDLQESMILTGIQTRQHHQHHHHHRFSAKDYIIDFEKGRMRIRMKVCLALCVVVLCIGVGALVLHFVEELGFVDSVYLSVMSVTTVGYGDRAFKTLQGRLFAAVWLLVSTLAVARAFLYLAEARIDRRHRKAVKLALNREITVDDLLKADTYQHGFISKSEYIVLKLKEMGKITQKDIDQVVIQFEKLDPNQIGKITLPDLLGDPL
Protein: Ig mu chain C region (P01875)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
ASASPSPPRLFPLVLCSPSDSVYTVGCAAFDFQPSSIAFTWFDSNNSSVSGMDVIPKVISGPPYRAVSRIQMNQSEGKEKQPFRCRAAHPRGNVEVSVMNPGPIPTPNGIPLFVTMHPPSREDFEGPFRNASILCQTRGRRRPTEVTWYKNGSPVAAAATTATTVGPEVVAESRISVTESEWDTGATFSCVVEGEMRNTSKRMECGLEPVVQQDIAIRVITPSFVDIFISKSATLTCRVSNMVNADGLEVSWWKEKGGKLETALGKRVLQSNGLYTVDGVATVCASEWDGGDGYVCKVNHPDLLFPMEEKMRKTKASNARPPSVYVFPPPTEQLNGNQRLSVTCMAQGFNPPHLFVRWMRNGEPLPQSQSVTSAPMAENPENESYVAYSVLGVGAEEWGAGNVYTCLVGHEALPLQLAQKSVDRASGKASAVNVSLVLADSAAACY
Protein: F-box and leucine rich repeat protein 22 (A0A1W2PQW8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWPLLTMHITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLHFRSLTELQKDNFLLGPALRSLSICWHSSRVQVCSIEDWLKSAFQRSICSRHESLVNDFLLRVCDRCPNLASVTLSGCGHVTDDCLARLLRCCPRLRALRLENCARVTNRTLAAVAADGRALQTLHVDFCRNVSAAGLRRLRAACPRLALRAEHSAAMLPDQPPRPRAPAAALGKLLQR
Protein: At1g63840/T12P18_14 (Putative RING zinc finger protein) (RING/U-box superfamily protein) (Q9CAJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- ACD11 homolog protein
- Putative cell wall protein
- VQ motif-containing protein 10
- Pectinesterase inhibitor 3
- Kunitz trypsin inhibitor 1
Sequence:
MGFPVGYSELLLPKIFFYLLSFLGLIRKLISTMFKIIGLPDFLEPEPVSTSWPDPPPTLTKPDSAAILAGEMLPVVRFSDINRPESECCAVCLYDFENDDEIRRLTNCRHIFHRGCLDRWMMGYNQMTCPLCRTQFIPDHLQLEFNQRLWSQSSAVSSQLLDESSS
Protein: ATP-dependent DNA helicase PIF4 (EC 3.6.4.12) (DNA repair and recombination helicase PIF4) (Q381V6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:19646907}. Note=Localizes predominantly to the kDNA disk.
Interaction partners:
Sequence:
MLLNSTRTLLLTYGRLLFAPGREGRQSRLAKGVSAWTVAAEGEKGGQLSPAPESTSCCGAAEVNEIKERDTKTCRQASSAGHNDLGLQEKEKSSGDESAFSSLGLNEEKRRALTLVLDGAPLFIGGGAGVGKSYMIQSIVTALRAKDLDVVVTASTGIAALNIGGSTFHSTFGVRVTSVGNSETNESCAVSILRYSKSLLAKVDVIVVDEVSLLHARHLEGLDIAARGAPGRIPHLPFGGIQVILCGDFMQLMHSTENCTSQDGGGDAGNKIGYRGDETTENTAGQNRSDVSSTAAVTDQGHIMSAVKNICVGERQRTSSGLIFESPLFLTCLLHLQLCEVKRHGDTAFLNDLNKLRQGVLTRRMMRSALVNPEDPNAIQLYPTRRSVAAFNESKMLELDGEEHLFRSIVESAGLSGPKGHASPNSRGANNVDGCNDVVVLHFLEKMRSSRRWQREVKKFVGQICTRCGISGIATSVVAPPYSSRQPYLKVYVHFCVSKQYDCLYPVAKMKAEWERSYYGTTPESKSARRFFGRVLFEVKHKNSLSTFLRASLKQAYSKVIESDNVLQSKRLKVGCRVILLRNLSNEYVNGSTGTVIGFQPVNKSRHLFPKGIRTQLSRKVYASLSRRPVVSSDSSAGSSENSYGGNGKEQALDVVNYDDVIVPIVRMDADGKDVAIPWLSLPLPDLQDRVFCTARVVTMPLVPAYAFTVHKTQGLTLDHSILLDCKGFFPCNHIIYVAASRVKKFSQLRMINVSPRMVTVHPGALHFSSSLPNVAEAETKWKKWKELQRMVNNGKALSASNPSVLELALYCATWKHHK
Protein: Peptidyl arginine deiminase 1 (Peptidylarginine deiminase type I) (E1C0W6)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSQRQVIQMSTSHASYGVCVLGTEVFLDTHRSTPKGATSFDVHATSAVTVHIIHSPMTKPMLNSRWPLDPDIEVVVTIGVTSKTVNDNKVKISYYGREENEISVAWLYLTCVDISLDVDVSRNGRVRSKGKDKAKWTWGPDGQGAVLLVNCDKDSPSTVGTDSSQVDIHTPADLQDMSVMLLRTQGPSSIFADYQLVLHVSESDADKVRVFHAIRSDSHPRYKPVLGPGMLSCLLDCVRSGENTFYVEGLAFPDAGFSGLVSISVSLLEVPHKYSPGTPVFTDTVVFRVAPWIMTPNTQQPLEVFVCSIKRGINSNEVFLEELQALLRKANCKMTICSEVESRSDRWIQDELEFGYVEAPHKSFPVVFDSPRNRGLKDFAFKKILGPDFGYVTRVPPGCDACSLDSFGNLDVSPPVTVRGKEYPLGRILIGSPLPWASGRRMSKVVRDFLYAQKVQAPVEVYSEWLSVGHVDEFLTFVPAYDRKGFRLLLASPTACFKLFQEKQRQGHGEATQLVGMVGCERRSIDDILADEGLRNDNKHVQRCIDWNRDLLKHELGLSEQDIIDIPQLFILRGSRAEALFPDMVNMLVLGRHLGIPKPFGPLVAGQCCLEERVRALLQPLGLSCTFINDFFSYHVLSGDVHCGTNVRRKPLAVKWWHVVP
Protein: HMG box-containing protein C28F2.11 (Q9USU7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerase I subunit rpa49
- RNA polymerase I-specific transcription initiation factor rrn3
- Zinc finger protein sfp1
- DNA topoisomerase 2
Sequence:
MAQNSTQLEKISGSFTRLAEAFQLALTACREIEESLPSILGEKSEVSKPFKPAVTDPSNAKKEINMAIESPSKKATSPKKATPAAVAPVEATSAVDTSEAVASMTPNKRKARDPAQPKRPPSAYNLFQKNQRSEIKESLGEKSNDVKEVNKAMHEKWGSLSEDDRKTYEEEASKLREAYEEEMAAYNASKENASVADSRVTAEETSTKPSEDLSSPTKKDLIDFSETRPLAQASRATPDIKEQHAKKPKRKHTRSTVPTSNVEPVSQPQPSPDKIVSSPNPPSAKREKKKRRKSSMSSSITTPPTAKVAN
Protein: small monomeric GTPase (EC 3.6.5.2) (Q9VM20)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MNATSPKSSLVKLGLHTNKQKTLKVMVLGQSGVGKTAMVVRFITRRFIGEYDPNLEKIYTCQTTLDKEQIQFDILDATGQLQELDGVSLESNIRWADAFILMYSITDKCSFDECSRLKFLINYNKRRRKLGSASKEYALDIPVILVGNKTDQPGDRMVSLEEGQRRFRELSCSCFHEISVRESVDQVQNVFRDVFRFWRVFSKFPKLKRSTSDVANTDGILTPDSGSCSFYDASSLGVGRHSFLVIGSACLEESNGDHTESTDEITSSSLSSSRSDIDAPFRSRASTDGTLLSRPRRWRYPPPGCLLPHTNRVERRMSISTRGSNASY
Protein: Cytochrome P450 monooxygenase easM (EC 1.-.-.-) (Ergot alkaloid synthesis protein M) (Q4WZ65)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 monooxygenase easK
Sequence:
MDFLQRILGILSSEDVAPALFASSISVLFLILSYQVLYPPSKYSAFPTINGTRWLALSNRRILAEFVTDAQGLMRNGLEKYDIFRIISSIGPMTILHPKYTDEIHNDRQLNFMAVLAKEMFPNYPGFDLFREGTDGSTVLQDAVKFGSSRCLGKSTQLLSDETSTLLQKLWGDEPEWHEVTAKSSVHDIIAHLSALLFYGPELCSHKEWLEVTDEYASVGFLAARQLRLWPPILRPIAQWFLPACRRLRYLASRTRGLIEPVIAARQKEKAICYSHGRQPPVYDDAIEWTERAAKGRPYDAAMSPLLFSINALHTTTDLLTQVILDLSTQPDLIVALRQEILSVKPQQNGWKNASLNQLLLMDSAIKESQRLKPTESILMRRYAMDDLTLADGNKIPKGTVLGIPIFGMRDPKIYVDPDMYDGYRFQKMRDKPGFENKCQLVSTSPWHLGFGHGIHACPGRFLAAVQVKIILCYIVAKYDFKLAGGAPPKVQSVGIELISDTEARLAVRRRQEMVIGLE
Protein: Serine/threonine-protein kinase pakD (EC 2.7.11.1) (Q55DD4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase cnrN
- Guanine nucleotide-binding protein alpha-8 subunit
- Autocrine proliferation repressor protein A
Sequence:
MSRLQPQQQQRGRSSSFKDNFQIQKPLQSLTPSEQQQQQQQQQQQQQQQQQQQQQQQQQNNANNNNNNNNNKFNNQYIQQMKNVENDIKKWIGEKCSSSLSDDFLEKDLMESLCTGTILCVLINMIKQGTIQKIHLQPNYLQRVENIRNYLRACWLFGLHSKYFFPSSYLLSMTIENNDNSNSSKTTTNNNNNNNNNNNNNNNNNNNNNNNNNNRAIITSPNKNGGVNTMIVNLEYKEKIMINLTELCKISLKIKNFGSFLQLSSSSSSTPPPPINNNNNNNNNNNNNNNNNNDLLISNNSSNISSPNSFSDSPMGFSSSINSSSNNSNLNTPNNYNNTNNNNNNNNNNNNNNNNNINNLTPQMIISSPTSTSSTPPLPPCANNINNNNLKKRTKIPKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKIIIKRDCKKVYRKRKSSNCDNDDNGSNSDSDSSDSSDSSDSDSDSLLSSDGTPIILSQSSNPESVSFKSFIKEILHLKNIISKQDKTITSQKQTIETLEKDLEFQKQLTKKLLSSPIDLSNFIETSSDPNGAIPVSIQAFTRQIQQIQTLQQQNLSLETELSKTNEHLSTNIRKNSKLENEVLSIETELLNLRMKYANTLSSSNSNGNNNSNNNSLGCNNSINGSSSGGGGNNSSTSKGTLSRTISQPFPLRKSISHSNIITSPVNSHQQQQQQNQLSQSQTTSPKNTSASYNNGILSKSSIVSNTNTNSTYKFGSSTGILKVSATLQQKQQQQQQQQNQQQQQNQQQQQQNQQQQNQQQQNQQKQNQQQQNQQQQQQQQQQQQQNQQQQQQQQQQQQQQQQQQNQQQQQNNQLSQSQQLQQQQNQQINNLIDSPLIISNSSNQQIESESIESDSDYDKDMVDFGKKIVSALISSSNHVEMSEIYKMNDILTNETSRRQICIVLEEETKINQLKLPMNENSFEVTLYLVNTILQCIHEAPSKDYFSLKLIMESSRILNRKKVNGSCEFIQEFIKDHPTWKDIKFWEEQYWDELIIKHQQFSGSGSSSSSNTGGSIVTTMTTTTTVTSAITSSSSTTSDDFDVDYTELVNTLLISYVYNLASWGLSKSDVKEFTISMSKKSFLKSNELEKLIEQVTSTVELSFTSDHNVCKGPHSFVLKSFRIISECNYCRQYIWGVRGIVAREAFECVGCKYKTHKKCLKEASEKTFCSSPNVGAPFNVKHEMHVGLAIQGLPSGWRTLLLQSGFQDYEIQQHQEDVLDVLEFHHVYNEKQQNSIKLLTNNSNNNNNNNNSNNNLQQQQQQNQQLKQKLNITNNQQNNTIININITSPSISVNNNTYNNNNNNNNNNEINPSSPNNNNNYYDSLLEIEEPSFTLKDLVSLENPIDLYKVREVVGGGSTGKVYVGENSITGEKVAIKKMKVDNNNIKNIINEISTMKNSKHKNVIKYVSSHLVINHIWLIMEYMSYGSLTDLISNCINIQCNGNNQQQQQQQQQQQTYFIESHIAYICQQVLQGMDYIHKGHRTHRDIKSDNILLGKDGSVKIADFGFVANLTRKKLQRNSVVGTPYFMAPELIRGNQYNHKVDIWSLGILARELSEGEPPYAKYPPVRALFLLTLEGVPDFKEPNKWSSDFIEFVNLCLNLDDKRRPDAHYLLRHPFLKKACSSREFADKVEEIYNTRKNQFSDINFNF