wanglab/gogpt-training-data huggingface dataset:
Protein: Retroviral-like aspartic protease 1 (EC 3.4.23.-) (Skin-specific retroviral-like aspartic protease) (SASPase) (Skin aspartic protease) (TPA-inducible aspartic proteinase-like protein) (TAPS) (Q53RT3)
Organism: Homo sapiens (Human)
Function: Protease responsible for filaggrin processing, essential for the maintenance of a proper epidermis organization.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSPGASLGIKKALQSEQATALPASAPAVSQPTAPAPSCLPKAGQVIPTLLREAPFSSVIAPTLLCGFLFLAWVAAEVPEESSRMAGSGARSEEGRRQHAFVPEPFDGANVVPNLWLHSFEVINDLNHWDHITKLRFLKESLRGEALGVYNRLSPQDQGDYGTVKEALLKAFGVPGAAPSHLPKEIVFANSMGKGYYLKGKIGKVPVRFLVDSGAQVSVVHPNLWEEVTDGDLDTLQPFENVVKVANGAEMKILGVWDTAVSLGKLKLKAQFLVANASAEEAIIGTDVLQDHNAILDFEHRTCTLKGKKFRLLPVGGSLEDEFDLELIEEDPSSEEGRQELSH
Protein: Oxysterol-binding protein homolog 6 (Lipid-transfer protein Osh6) (LTP) (Oxysterol-binding phosphatidylserine transferase) (Oxysterol-binding protein-related protein 6) (ORP 6) (OSBP-related protein 6) (Q02201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis. Catalyzes the lipid countertransport between the endoplasmic reticulum (ER) and the plasma membrane (PM). Specifically exchanges phosphatidylserine (PS) with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Also binds phosphatidic acid (PA).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16096648, ECO:0000269|PubMed:16156791}. Cell membrane {ECO:0000269|PubMed:16156791, ECO:0000269|PubMed:20008566}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:23934110}. Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites. {ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:23934110}.
Interaction partners:
- Oxysterol-binding protein homolog 7
- Increased sodium tolerance protein 2
- Vacuolar protein sorting-associated protein 4
- Vesicle-associated membrane protein-associated protein SCS2
- Phosphatidylinositol-3-phosphatase SAC1
- Vesicle-associated membrane protein-associated protein SCS22
- Tricalbin-3
- SEC14 cytosolic factor
- Phosphatidylinositol 4-kinase STT4
- Phosphatidylinositol 4-kinase PIK1
Sequence:
MGSKKLTVGSDSHRLSKSSFSSNKSSHSATKDQPIDTDDIDEDDESGHNIILNIISQLRPGCDLTRITLPTFILEKKSMLERVTNQLQFPEFLLQAHSEKDPLKRFLYVMKWYLAGWHIAPKAVKKPLNPVLGEYFTAYWDLPNKQQAYYISEQTSHHPPECAYFYMIPESSIRVDGVVIPKSRFLGNSSAAMMDGSTVLQFLDIKDGNGKPEKYVLTQPNVYVRGILFGKMRIELGDHMIIKSPNFQADIEFKTKGYVFGTYDAIEGTVKDYDGNAYYEISGKWNDVMYLKDLKQPRSSPKVFLDTHKESPLRPKVRPLSEQGEYESRKLWKKVTDALAVRNHPVATEEKFQIEDHQRQLAKKRIEDGVEFHPKLFRRSKPGEDLDYCIYKNIPVDEDPEKQIRSILQIAPILPGQQFTDKFFIPAFEKIKSQKKMIENEKQNPAKQ
Protein: Large ribosomal subunit protein uL13 (50S ribosomal protein L13) (P9WHE1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Interaction partners:
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein bL25
- Large ribosomal subunit protein bL33B
- Large ribosomal subunit protein bL31
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL4
Sequence:
MPTYAPKAGDTTRSWYVIDATDVVLGRLAVAAANLLRGKHKPTFAPNVDGGDFVIVINADKVAISGDKLQHKMVYRHSGYPGGLHKRTIGELMQRHPDRVVEKAILGMLPKNRLSRQIQRKLRVYAGPEHPHSAQQPVPYELKQVAQ
Protein: UDP-glycosyltransferase 74D1 (EC 2.4.1.-) (Jasmonate glucosyltransferase 1) (AtJGT1) (Q9SKC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glucosyltransferase that glucosylates jasmonate (JA) and JA derivatives. Also active on indole-3-acetic acid (IAA), 4-coumrate, cinnamate and caffeate.
Interaction partners:
- Indole-3-acetate O-methyltransferase 1 acetate carboxylmethyltransferase 1)
- Pentatricopeptide repeat-containing protein At1g05670
Sequence:
MGEKAKANVLVFSFPIQGHINPLLQFSKRLLSKNVNVTFLTTSSTHNSILRRAITGGATALPLSFVPIDDGFEEDHPSTDTSPDYFAKFQENVSRSLSELISSMDPKPNAVVYDSCLPYVLDVCRKHPGVAAASFFTQSSTVNATYIHFLRGEFKEFQNDVVLPAMPPLKGNDLPVFLYDNNLCRPLFELISSQFVNVDDIDFFLVNSFDELEVEVLQWMKNQWPVKNIGPMIPSMYLDKRLAGDKDYGINLFNAQVNECLDWLDSKPPGSVIYVSFGSLAVLKDDQMIEVAAGLKQTGHNFLWVVRETETKKLPSNYIEDICDKGLIVNWSPQLQVLAHKSIGCFMTHCGWNSTLEALSLGVALIGMPAYSDQPTNAKFIEDVWKVGVRVKADQNGFVPKEEIVRCVGEVMEDMSEKGKEIRKNARRLMEFAREALSDGGNSDKNIDEFVAKIVR
Protein: Nuclear envelope phosphatase-regulatory subunit 1 (NEP1-R1) (Transmembrane protein 188) (Q8N9A8)
Organism: Homo sapiens (Human)
Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:22134922}; Multi-pass membrane protein {ECO:0000269|PubMed:22134922}. Cytoplasm {ECO:0000269|PubMed:22134922}. Note=Filamentous pattern in the cytoplasm.
Interaction partners:
- CTD nuclear envelope phosphatase 1
- Phosphatidate phosphatase LPIN1
Sequence:
MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGLFFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
Protein: Mortality factor related protein 1 (A7DTF0)
Organism: Caenorhabditis elegans
Function: Protein involved in the remodeling of chromatin thereby regulating various processes including transcription, chromosome synapsis and genome integrity. Mainly binds genomic loci carrying trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4' (H3K4me3), and acetylated histone H3 'Lys-9' (H3K9ac), 'Lys-27' (H3K27ac). During meiosis, required for the presynaptic pairing of homologous chromosomal regions outside of the pairing center and for the progression of chromosome synapsis. Essential maternal factor required in postembryonic germline development and in maintaining germ cell identity. Plays an important role in maintaining genomic integrity in primordial germ cells (PGCs) during meiosis by regulating DNA double-strand break (DSB) repair and synapsis. Also, required for chromatin-based transcriptional silencing in PGCs and for silencing of X-linked genes in the maternal germ line. By retaining histone acetyltransferase, cbp-1, in euchromatin, promotes the anchoring of heterochromatin at the inner nuclear membrane in intestinal and hypodermal cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:22172672}. Chromosome {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}. Note=Concentrated on euchromatic regions marked by H3K36me2/me3 and probably enriched on autosomes. {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}.
Interaction partners:
- DNA methyltransferase 1-associated protein 1
- Uncharacterized protein
- Enhancer of polycomb-like protein
- Probable histone-binding protein lin-53
- Chromatin modification-related protein MEAF6
- YEATS domain-containing protein
- Actin-related protein 4
- Histone acetyltransferase
- Histone H2A.V
- Paired amphipathic helix protein sin-3
Sequence:
MSSKKNFEVGENVACIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGEEKDRIFKGTASEYAEKHNAELPTTALKPKKKSLAAEAPRDDRDDTPGTSKGKKAKSVTIAPVMTADDMKVELPKPLRKILIDDYDLVCRYFINIVPHEYSVDQIIEDYIKTIPVSNEQMRTVDDLLIEYEEADIKITNLALICTARGLVDYFNVTLGSSYQLLYKFERPQYNDLVKKRAMEKGIDITNPTALQDSGFRPSQEYGIVHFLRMLAKLPDYLKLTQWNDHVINRIMIGVHDLIVFLNKNHGKYYRGSSDYQGASNDYYRRSLAADDGVGANQ
Protein: Forkhead box protein R1 (Forkhead box protein N5) (Q3UTB7)
Organism: Mus musculus (Mouse)
Function: Transcription factor which acts as both an activator and a repressor (By similarity). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (By similarity). Required for normal brain development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6PIV2}. Cytoplasm {ECO:0000269|PubMed:25609838}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25609838}. Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838). {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}.
Interaction partners:
Sequence:
MGNECFLTFTTTHLSEAEQKLALYRLQLVEPPKLPLEKKTNPDKDGPDIKPNLWMWVNPNMVYPPGKLEVAVKEEDQSALSAFQPALKEEEDSCSEASEVQQPLPPCRQKRKQRRSTVPLPLAPGRRAPLENPWRLPQAISPEGRLWSRPPLHYFHLIALALRNSPPCGLSVQQIYSFTREHFPFFRTAPEAWKNTVRHNLSFRDSFEKVPASRQGGASTGPRSCLWKLTEEGHRRFSKEARTLASTQLQSIQQCMSQPGVKPFLFDL
Protein: POC1 centriolar protein homolog (Q229Z6)
Organism: Tetrahymena thermophila (strain SB210)
Function: Required for structural maintenance of centrioles, ciliogenesis, and cilia-based motility.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20008567}.
Interaction partners:
- Endo-1,4-beta-xylanase xylA
- Nucleoporin, putative
Sequence:
MKKTTIASSAVASQKQTQSKLGNTSSKITEQQTTHDPALSRSFRGHEDIITCADFDPKMRQVASCSKDSIVYVWNFKPQQRPFKFVGHKGAVYCVKYSPDGETIASCGQDRQIRLWQNTVQSKCSIIKAHCGAIRSMSFSADGGYLLSSSDDKTLKLWRLQDKKFMCSFAGHKNWVRSGVISPDMRLVASGSDDKTVMLWDLNFQKIVSKYSTLDDNVKISQINSYSDHMDTVSQVLFHPDGTCLISSSFDHKIKITDIRSNKLIQHYNAHDAQVNSISIHPTGYFLASAGSDSKIKIWDLRQGRQIYTLYSNDKDITTVQFNQSGDYFATGGSQNLCMVWKTNFDQNIQNIEQVQRSTVRQNDVEYSSGGLYAQTLFKTNKTASLSPSKKTISIIPPQQLQDTFNNRGDDELNNGRVHENKQSNSPTFSQQQQQQQLNLSENQYPGLEIVGNQFNLQQSTLSNNNNQNNLIKSQNDSIVSNKNAIPFHPSSEFQQSAVQQQFSQQPKLVVNNGTATYPSNFVPKVEEENIMTEAIAASMQQIYSRLDTMFQYMTNLENRVVQSEQLQKSFVSQNHQNTLDPKQQTMNFGYSNIQDHSLSASLNDRNVVNIFQAGALANTGSIEASLINKQQEE
Protein: G1-specific transcription factors activator MSA1 (MBF and SBF-associated protein 1) (Q08471)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activator of G1-specific transcription factors, MBF and SBF. Promotes both the timing of G1-specific gene transcription and cell cycle initiation. Associates with SBF- and MBF-regulated target promoters and this binding is maximal during the G1 phase, prior to maximum budding. Affects cell cycle initiation by advancing the timing of transcription of G1-specific genes. Overexpression advances the timing of SBF-dependent transcription and budding. Depletion delays both indicators of cell cycle initiation.
Interaction partners:
- Putative transcriptional activator MSA2
- Regulatory protein SWI4
- Cyclin-dependent kinase 1
- Transcription factor MBP1
- G1-specific transcriptional repressor WHI5
- Regulatory protein SWI6
- Protein STB1
Sequence:
MDKSMIKKRGRPPITKDYPNPLQSPMAHSSMQVQKQGPHSFAKPLMKVGQSSPSPNKRRLSIDHHHNLAATTRKGRYRGVLLSTPTKKSSTNGSTPISTPSSNDSYNNTVFSETRKTFLQSSPPIMTSSPAFQKKNDYMFPSQEQFKLSLTITESGKAVIAGSLPFSPSSKSSHLMNNNNKKIMQNEKIHKGSKKNAPKFEKRRILSLLKQMKNEKYCDTDTLPEAPPAKPSRSDIIDTELPTIIETSASPIGSARNNNILLSQPPQSPPSSAQLKPPSTPKSSLQFRMGFTPNVALNSVSLSDTISKSTNAVGASNNNNQNGNSISNIADANTLLTLTNSPGVFLSPRNKMLPKSTTASNEQQQEFVFKFSSGDPLLLTDDADGNWPEMLFNVSNTPRRQKCFNTPPSWINFGSPGLFSPPRSSNVMVNGTTVATASDSGNVHRQLQAQLEAQVQVQSQSNSPTQRQQQQRQFQIPPPHINMNSSPPQINIASPPHQSMSRVSSIYFNKEKTTTGVANMLGNTKSENLQPPANLFTAAHGPSTPRNQEFQLPTLIECTPLIQQTMNGSLGTKYIPGTSISNSATPNLHGFPVGTGKAPSSFDDSLKQNPYSNKQDDARTALKRLIDDQ
Protein: NAC domain-containing protein 20 (ONAC020) (OsNAC20) (Q9FTY0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor that acts redundantly with NAC26 to regulate the expression of genes involved in the biosynthesis of starch and storage proteins in grain. Directly binds to the promoters of starch synthase 1 (SS1), pullulanase (PUL), glutelin A1 (GLUA1), glutelins B4 and B5 (GLUB4 and GLUB5), alpha-globulin and 16 kDa prolamin, and activates their expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:32989010}. Endoplasmic reticulum {ECO:0000269|PubMed:27872632}.
Interaction partners:
Sequence:
MGEQQQQVERQPDLPPGFRFHPTDEEIITFYLAPKVVDSRGFCVAAIGEVDLNKCEPWDLPGKAKMNGEKEWYFYCQKDRKYPTGMRTNRATEAGYWKATGKDKEIFRDHHMLIGMKKTLVFYKGRAPKGDKTNWVMHEYRLADASPPPPPSSAEPPRQDDWAVCRIFHKSSGIKKPVPVAPHQVPAAANYQQQQQMAMASAGIIQVPMQMQMPSMSDQLQMLDDFSTTASLSLMAPPSYSTLPAGFPLQINSGAHPQQFVGNPSMYYHQQQQMDMAGGGFVVSEPSSLVVSPQDAADQNNNAADISSMACNMDAAIWKY
Protein: Glycosylphosphatidylinositol anchor attachment 1 protein (GPI anchor attachment protein 1) (GAA1 protein homolog) (mGAA1) (Q9WTK3)
Organism: Mus musculus (Mouse)
Function: Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase component PIGU
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase, stabilizing subunit
- GPI alpha-1,6-mannosyltransferase 2
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
Sequence:
MGLLSDPVRRRALARIVLRLNTPLCVLSYVAGIAWFLALAFPPLTQRTYMSENAMGSTMVEEQFVGGDRARSFARDFAAHRKKPGALPVAWLERSMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRSASTESLVLTVPCGPDATNSQAVGLLLALAAHFRGQIYWAKDIIFLVTDHDLLGTEAWLEAYHDINVTGIQSSPLQGRAGAIQAAVALELSSDVVTSLDVTVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPQDWTSLEGPLQGLQTLLLMVLRQASGRPHGPHGLFLRYGVEALTLRGINSFRQYKYDLATVGKALEGMFRKLNHLLERLHQSFFFYLLPALSRFVSIGLYMPATGFLLLVLGLKALELWMQLHQAGVNPEEAGKAPSPGTPLLPTQGVGLASLTAPLLISQAMGLALYFLPVLGQHLATQHFPVAEAEAVVLTLLAIYVAGLALPHNTHRVVNSQVPDRGWMALKLVALIYLALQLGCIALLNFSLGFLLAATMVPAAALAKPHGPRTLYAALLVVTSPAVTLFGSLFLWRELLEVPLSLAEGWQLFLTALAQGVLEHYTYGALLFPILALGLYPCWLLFWNVLFWK
Protein: Phosphatidylserine synthase 2 (PSS-2) (PtdSer synthase 2) (EC 2.7.8.29) (Serine-exchange enzyme II) (Q9BVG9)
Organism: Homo sapiens (Human)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine. Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein {ECO:0000255}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Choline/ethanolaminephosphotransferase 1
- Phosphatidylethanolamine N-methyltransferase
- Ethanolaminephosphotransferase 1
- Phosphatidylserine synthase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase D1
- Phospholipase A1 member A
- Phospholipase D2
- Membrane-bound glycerophospholipid O-acyltransferase 1
Sequence:
MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPDNETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGSVLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEGEGAPTPN
Protein: Histone-lysine N-methyltransferase (A4LBC3)
Organism: Caenorhabditis elegans
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQTRRKTAAAVQDGGAVKENKAKPPAPQTPTKRAKRGRPPKIKTDANTLNTPSTSSNLVDDKLLIESESQDSILTNEADSFLEKEVEEIEDSSDILPDKINSPEKPSVLVKRRSSTRLKVKTDEDEKDVPVNIEVAVLEEKSIQIEPTSPAHPEDPQPSTSSLPLVEPIEDIVEPNEPTSSADPPVSNIKDEDIKEEEPLIKKPASDESESMDIANSESGNDSDSSEADPRTIPSFSIPLPDTPPPNFAKRGEIHVDVDQKNSKQSGESQSPWERAREKSASNPLSSPTMSRPRIHFLHPAYQSFTNDSVSPLPPPPPEPAPAREKVENGGPTTFKMTFKKAANIPILKTSAFEQPSSPPPSSSVSSSISLSEVNSSTSIASESSPAKRSSNFDLTASNELPPPQMVELPKLSFFNMPPAVRSAEDDSAMTSEEPILLLRSPNSATPDDDALFLTTPPPPKMTESEIQALKVATEKVNQVIARREDSEKDVRHREDRDDYDRRRDDRDRRSRKTDSERNDQRGRQREDDERRAREREREVTKRHDREREEMRLQKQKDEERRKKDEEERIQKENDEKKQKEDEAKMEEEKKKIKEEEMKIPEFELISESKYLTRNANKKKTESLTCECHRTGGNCSDNTCVNRAMLTECPSSCQVKCKNQRFAKKKYAAVEAFHTGTAKGCGLRAVKDIKKGRFIIEYIGEVVERDDYEKRKTKYAADKKHKHHYLCDTGVYTIDATVYGNPSRFVNHSCDPNAICEKWSVPRTPGDVNRVGFFSKRFIKAGEEITFDYQFVNYGRDAQQCFCGSASCSGWIGQKPEEFSSDEDDDIVTTRHINMDEEEEEKLEGLDHLGNHERNEVIKDMLDDLVIRNKKHARKVITIASAMTDYSQRVDVIQEIFSSDTSVTVQKFYAKEGMATLMAEWLSEDDYSLDNLKLVQAILKALHTELFDSCAKNDRLLRDSTSRWVNAKMDEYVDIQVIADSLIACVEDPVQEYKDVCKVIEKGLVENFTRAKEMAYRLNQYWFNRSVSFKIPKKIRDPVPKDVPVRQEDATTSSQSHDNSSRTVSPNHRHHSSSYSNSCYQEREPSHIRFFNNGNDVHQYRFGGYHGNNYNDNYFSRRPNKDSYRDRRRFNGRRSRSRSRSVSPQNYKRRKLDEHDNNHRQRSPIRDRHTSPGGEKTPSSNNSGERNYKRLDIRGARIKTIKEDLEAAAAAAAAAAVPSEVQAYPHEHTAVHQSVYQMPGYESYGVYDPVNGVYMYPHPGAGYYPPAYPQQPIMLTMDTLPPNDRLGELYEKASIEQLAQRDAIVRQELELIRIQIERKTAQKEAIKAACRRANEEEAKRQEALAKTKYVWAIAKSEAGETYYYNKITKETQWTAPTPVQGLLEPACGASPDTTVVIADEITEEEQQAEVLEKPRVVKEEVIEPGSQSETQKESPEKVRVVVPKVEVERSPSPKSSRDREKDREKSREKDRERDRDRREGSKHRDSYHGHRNGSSSVSERRMREFKHELERSTRSAVRSRLQHQRDASSDKTTWLIKLIYREIFKRESAQSGFDYRFSENTDKKVKNYVKSYIDRKLESNDLWKEYSRP
Protein: Nudix hydrolase 7 (AtNUDT7) (EC 3.6.1.-) (ADP-ribose pyrophosphatase) (EC 3.6.1.13) (NADH pyrophosphatase) (EC 3.6.1.22) (Protein GROWTH FACTOR GENE 1) (Q9SU14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use both NADH and ADP-ribose as substrates, but not 8-oxo-dGTP, cyclic ADP-ribose, GDP-manose, UDP-glucose, ATP, or GTP. Exerts negative control of EDS1 signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:22068106}. Cytoplasm {ECO:0000269|PubMed:22068106}. Cell membrane {ECO:0000269|PubMed:22068106}. Note=Localized at the plasma membrane when in complex with GG2, but present in the cytoplasm when associated with GG1. Detected in the cytoplasm and nucleus when interacting with RACK1A.
Interaction partners:
- Nudix hydrolase 1
- Protein EDS1
- Nudix hydrolase 25
- Nudix hydrolase 19, chloroplastic
- Calmodulin-binding protein 60 G
- Probable flavin-containing monooxygenase 1
- Nudix hydrolase 24, chloroplastic
- BON1-associated protein 1
- Probable inactive nicotinamidase At3g16190
- Lipase-like PAD4
Sequence:
MGTRAQQIPLLEGETDNYDGVTVTMVEPMDSEVFTESLRASLSHWREEGKKGIWIKLPLGLANLVEAAVSEGFRYHHAEPEYLMLVSWISETPDTIPANASHVVGAGALVINKNTKEVLVVQERSGFFKDKNVWKLPTGVINEGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILKKKTDMFFLCVLSPRSYDITEQKSEILQAKWMPIQEYVDQPWNKKNEMFKFMANICQKKCEEEYLGFAIVPTTTSSGKESFIYCNADHAKRLKVSRDQASASL
Protein: Protein BRANCHLESS TRICHOME (F4I878)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a key regulator of trichome branching. Could participate with STI in the same pathway. Also plays a role in integrating endoreplication levels with cell shape.
Interaction partners:
- Homeobox-leucine zipper protein HDG2
- Actin-related protein 2/3 complex subunit 5B
- Protein STICHEL
- Actin-related protein 2/3 complex subunit 5A
- Protein ABIL3
- Protein ABIL1
- At2g38901/At2g38901
- Filament-like plant protein 4
Sequence:
MKDMKMQSSPETMMTRIPTPDPHSTGVREDAMDSVCKPWKLYENPYYCSSQSQQHQHQRKAFIWDLNFIKVFMESELGKAQDEIKELKAELDYERKARRRAELMIKKLAKDVEEERMAREAEEMQNKRLFKELSSEKSEMVRMKRDLEEERQMHRLAEVLREERVQMKLMDARLFLEEKLSELEEANRQGERERNRMMKPKILERACSSPARRRCENPQIKRGINPFPRVMRAIRSKSEKWGSKLECQKVQLKILLRQKTTPRCTPLLSSPPP
Protein: FGD5 protein (FYVE, RhoGEF and PH domain containing 5) (B7ZM68)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGQDAEDTSEEPPEKEELAGVQEAETATDCPEVLEEGCEEATGVTGGEQVDLSEPPDHEKKTNQEVAAATLEDHAQDESAEESCQIVPFENDCMEDFVTSLTGSPYEFFPTESTSFCSESCSPLSESAKGLESEQAPKLGLRAEENPMVGALCGQCGSLQGGAAEGPAAPDVVVVLEEEALDDALANPYVMGVGLPGQAAPGEGGQAASDALGGYGSKEELNCEAEGGLVPADRKNTSTRVRPHSGKVAGYVPETVPEETGPEAGSSAPGIGGAAEEVGKTLLSLEGKPLEASRALPAKPRAFTLYPRSFSVEGREIPVSVYQEPEGSGLDDHRIKRKEDNLSLSCVIGSSGSFSQRNHLPSSGTSTPSSMVDIPPPFDLACITKKPITKSSPSLLIESDSPDKYKKKKSSFKRFLALTFKKKTENKLHVDVNVSSSRSSSESSYHGPSRILEVDRRSLSNSPQLKSRTGKLRASESPSSLIFYRDGKRKGVPFSRTVSRVESFEDRSRPPFLPLPLTKPRSISFPSADTSDYENIPAMNSDYENIQIPPRRPARAGAFTKLFEDQSRALSTANENDGYVDMSSFNAFESKQQSADQDAESAYTEPYKVCPISSAAPKEDLTSDEEQRSSEEEDSASRDPSVTHKVEGQSRALVIAQELLSSEKAYVEMLQHLNLDFHGAVMRALDDMDHEGRDTLAREELRQGLSELPAIHDLHQGILEELEERLSNWESQQKVADVFLAREQGFDHHATHILQFDRYLGLLSENCLHSPRLAAAVREFEQSVQGGSQTAKHRLLRVVQRLFQYQVLLTDYLNNLCPDSAEYDNTQGALSLISKVTDRANDSMEQGENLQKLVHIEHSVRGQGDLLQPGREFLKEGTLMKVTGKNRRPRHLFLMNDVLLYTYPQKDGKYRLKNTLAVANMKVSRPVMEKVPYALKIETSESCLMLSASSCAERDEWYGCLSRALPEDYKAQALAAFHHSVEIRERLGVSLGERPPTLVPVTHVMMCMNCGCDFSLTLRRHHCHACGKIVCRNCSRNKYPLKYLKDRMAKVCDGCFGELKKRGRAVPGLMRERPVSMSFPLSSPRFSGSAFSSVFQSINPSTFKKQKKVPSALTEDKVALESMPLLGFTIAPEKEEGSSEVGPIFHLYHKKTLFYSFKAEDTNSAQRWIEAMEDASVL
Protein: Rifin (Q8IK35)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHCSKILLFLLPLNILVTSLSNVHNNNKLYNTPHHIPTTTSRMLSECDLYIPKYDNDADMKSVKENFDRQTSQRFEEYDERMKGKRQKRKEQRDKNIQEIIEKDKMDKSLAEKVEKGCLRCGCGLGGVAASVGLFGGLGIYVSKSAALATAIAEGAETAKAAGEAARIPAAIDAVIKGITKVFGVSTLDGKELGTYITATNYTNFKTIALAINEQYNPLSCIIPDPGADKSICPWVMRNFFAAKDSPRNVVSAYNSIEVAVKSIVLEAQSVTERAAKKATEDVIKSSIAAVDAKYVICQNAIIASVVALLIIVLVMIIIYLVLRYRRKKKMNKKQQYTKLLNQ
Protein: CD55 molecule (Cromer blood group) (A0A8I5XWT0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIRTRAPGTRAPPPPPLLLSLSLLLLLLSPTVSGDCGPPPDIPNATPNSGKHTKFAHQSQVTYSCNKGFKQIPDKPNTVVCLENDQWSNYETFCNKTCSAPLRLNYASLKKEYRNMNFFPIGTTVEFECRPGFQKVTSRTGKSTCLEELVWSPVVEFCKKRACPNPRELKNGHINIPTDILFGSEIIFSCDKGYKLVGVTSTFCSITGNAVDWDDVFPVCTTIFCPDPPKINNGRIREESDSYAYRQSVTYSCDQGFILVGNSSVHCTLNGEVGEWSSAPPKCIERHKVPTKTPPEVDIPSTMPHESTLINFPSTRAPLSHKPTTVKVPGTRVKPTSHKPTEVKVPGTRVPPTSQKHTTVNVPSTRVPATSQKPSMVHVSDTRVSPKPQKPTKANNPSTEIPPTPQKANTADVPSTESPPTPQKANTAVVPATEIPPAPQKTNTAVAPATEIPPTPQKTNTADVPSTESPPTPQKANTADVPATEIPPALQKANTAVVPATETLPTPQKANTAIVPATETPPAPQKTNTAVAPSTEIPPTPQKANTADVPATEIPPTPQNANTADVPSTEIPPTPQKSNTADVPATEIPPTPQKANTADVPATEIPPTPQNANTADVPSTEIPPTPQKTNTAKVSAIKPATAQMSLISTTVFAQTPPITQHPTTVNSSAVQTAQTTRGFATAKPSLTQNPPATQRPTISHFSMTKGLHTVTQIFTSAHITATQHVPVSKTTVRHPTRTSKDRGESNSGGDHFIYGHTCLITMTILHVMLLLTG