wanglab/gogpt-training-data huggingface dataset:
Protein: Protein FosB (Transcription factor AP-1 subunit FosB) (D3ZLB7)
Organism: Rattus norvegicus (Rat)
Function: Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (By similarity). Exhibits transactivation activity in vitro (By similarity). As part of the AP-1 complex, facilitates enhancer selection together with cell-type-specific transcription factors by collaboratively binding to nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex to establish accessible chromatin (By similarity). Together with JUN, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Involved in the display of nurturing behavior towards newborns (By similarity). May play a role in neurogenesis in the hippocampus and in learning and memory-related tasks by regulating the expression of various genes involved in neurogenesis, depression and epilepsy (By similarity). Implicated in behavioral responses related to morphine reward and spatial memory (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P13346}.
Interaction partners:
- Protein c-Fos
- Transcription factor JunD
- Transcription factor Jun
- Fos-related antigen 1
- Transcription factor JunB
- Fos-related antigen 2.
- Early growth response protein 1
- Mitogen-activated protein kinase 8
- Histone deacetylase 1
- Histone deacetylase 2
Sequence:
MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTSTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGSQRTSGSEQPSDPLNSPSLLAL
Protein: Vicilin-like antimicrobial peptides 2-2 (MiAMP2) [Cleaved into: Antimicrobial peptide 2a (Antimicrobial peptide Mac i 1) (MiAMP2a); Antimicrobial peptide 2b (MiAMP2b); Antimicrobial peptide 2c-1 (MiAMP2c-1); Antimicrobial peptide 2c-2 (MiAMP2c-2); Antimicrobial peptide 2c-3 (MiAMP2c-3); Antimicrobial peptide 2d (MiAMP2d)] (Q9SPL4)
Organism: Macadamia integrifolia (Macadamia nut)
Function: Antimicrobial peptides 2b, 2c and 2d have antibacterial and antifungal activity against a range of species.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAINTSNLCSLLFLLSLFLLSTTVSLAESEFDRQEYEECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQDDPQTDCQQCQRRCRQQESGPRQQQYCQRRCKEICEEEEEYNRQRDPQQQYEQCQERCQRHETEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQREDEEKYEERMKEEDNKRDPQQREYEDCRRRCEQQEPRQQYQCQRRCREQQRQHGRGGDLINPQRGGSGRYEEGEEKQSDNPYYFDERSLSTRFRTEEGHISVLENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLDADAILLVTGGRGALKMIHRDNRESYNLECGDVIRIPAGTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAGGQNPEPYLSTFSKEILEAALNTQAERLRGVLGQQREGVIISASQEQIRELTRDDSESRRWHIRRGGESSRGPYNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDVSVFIANITQGSMMGPFFNTRSTKVVVVASGEADVEMACPHLSGRHGGRRGGKRHEEEEDVHYEQVKARLSKREAIVVPVGHPVVFVSSGNENLLLFAFGINAQNNHENFLAGRERNVLQQIEPQAMELAFAAPRKEVEELFNSQDESIFFPGPRQHQQQSSRSTKQQQPLVSILDFVGF
Protein: Galactokinase (EC 2.7.1.6) (Galactose kinase) (P96993)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}.
Interaction partners:
- Galactose-1-phosphate uridylyltransferase
- UDP-glucose 4-epimerase
- Galactose operon repressor GalR
- Uncharacterized protein
- Galactose-6-phosphate isomerase subunit LacA
- Tagatose 1,6-diphosphate aldolase 1
- Galactose-6-phosphate isomerase subunit LacB
- UDP-glucose 4-epimerase
- Tagatose-6-phosphate kinase
- Alpha-galactosidase
Sequence:
MKKQELNQAFTHVFGREADATFFSPGRINLIGEHTDYNGGRVFPAAITLGTYGAARKRDDKLLRFYSANFEELGIIEISLDHLIFNKKDSWTNYPKGVIKYLQEAGHSIDTGMDVYVFGNIPNGSGLSSSSSLELLIGIMAEELFDLKLDRLDLVKIGKRTENDFIGVNSGIMDQFAIGMGAEKKAIYLDTKTLEYDLVPLDLGDNVIVIMNTNKRRELADSKYNERRTECEKAVEELNVLLDIKSLGELDEETFDEYAYLIKDAKRIKRARHAVSENQRTLKAKKALAAGDLEKFGRLVNASHVSLEHDYEVTGIELDTLAHTAWEQEGVLGARMTGAGFGGCGIAIVAKDKVAALKENVGRIYTETVGYAPAFYIAEIAGGSRVLSRK
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (P55263)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of the purine nucleoside adenosine at the 5' position in an ATP-dependent manner. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:19635462}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19635462}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Adenosine deaminase
- Purine nucleoside phosphorylase
- AMP deaminase 3
- AMP deaminase 2
- Adenylosuccinate lyase
- AMP deaminase 1
- Adenylate kinase 2, mitochondrial
- 5'-nucleotidase
- Adenylate kinase isoenzyme 1
Sequence:
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH
Protein: Alkaline ceramidase 2 (AlkCDase 2) (Alkaline CDase 2) (maCER2) (EC 3.5.1.-) (EC 3.5.1.23) (Acylsphingosine deacylase 3-like) (Cancer-related gene liver 1 protein) (CRG-L1) (N-acylsphingosine amidohydrolase 3-like) (Q8VD53)
Organism: Mus musculus (Mouse)
Function: Golgi ceramidase that catalyzes the hydrolysis of ceramides into sphingoid bases like sphingosine and free fatty acids at alkaline pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Has a better catalytic efficiency towards unsaturated long-chain ceramides, including C18:1-, C20:1- and C24:1-ceramides (By similarity). Saturated long-chain ceramides and unsaturated very long-chain ceramides are also good substrates, whereas saturated very long-chain ceramides and short-chain ceramides are poor substrates. Also hydrolyzes dihydroceramides to produce dihydrosphingosine (By similarity). It is the ceramidase that controls the levels of circulating sphingosine-1-phosphate and dihydrosphingosine-1-phosphate in plasma through their production by hematopoietic cells. Regulates cell proliferation, autophagy and apoptosis by the production of sphingosine and sphingosine-1-phosphate. As part of a p53/TP53-dependent pathway, promotes for instance autophagy and apoptosis in response to DNA damage. Through the production of sphingosine, may also regulate the function of the Golgi complex and regulate the glycosylation of proteins (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5QJU3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5QJU3}.
Interaction partners:
- Neutral ceramidase
- Acid ceramidase
- Ceramide synthase 4
- Ceramide kinase
- Sphingosine kinase 2
- Ceramide synthase 2
- Ceramide synthase 6
- Ceramide synthase 5
- Ceramide synthase 3
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
Sequence:
MGAPHWWDHLRAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCFNSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAILWVLMCALAMWFPRRYLPKIFRNDRGRFKAVVCVLSAITTCLAFIKPAINNISLMILGLPCTALLVAELKRCDNVRVFKLGLFSGLWWTLALFCWISDQAFCELLSSFHFPYLHCVWHILICLASYLGCVCFAYFDAASEIPEQGPVIRFWPSEKWAFIGVPYVSLLCAHKKSPVKIT
Protein: Amidophosphoribosyltransferase 2, chloroplastic (AtATase2) (AtPURF2) (PRPP2) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase 2) (AtGPRAT2) (Protein CHLOROPLAST IMPORT APPARATUS 1) (Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS) (Q9STG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the first committed step of 'de novo purine biosynthesis from glutamine. Required for chloroplast biogenesis and cell division. Confers sensitivity to the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15266056, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Phosphoribosylamine--glycine ligase, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- Ribose-phosphate pyrophosphokinase 1, chloroplastic
- Ribose-phosphate pyrophosphokinase 5, chloroplastic
- Ribose-phosphate pyrophosphokinase 2, chloroplastic
- Glutamine synthetase cytosolic isozyme 1-5
- Glutamine synthetase cytosolic isozyme 1-4
Sequence:
MAATSSISSSLSLNAKPNKLSNNNNNNKPHRFLRNPFLNPSSSSFSPLPASISSSSSSPSFPLRVSNPLTLLAADNDDYDEKPREECGVVGIYGDSEASRLCYLALHALQHRGQEGAGIVTVSKDKVLQTITGVGLVSEVFSESKLDQLPGDIAIGHVRYSTAGSSMLKNVQPFVAGYRFGSVGVAHNGNLVNYTKLRADLEENGSIFNTSSDTEVVLHLIAISKARPFFMRIVDACEKLQGAYSMVFVTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLIEATYEREVYPGEVLVVDKDGVKCQCLMPHPEPKQCIFEHIYFSLPNSIVFGRSVYESRHVFGEILATESPVDCDVVIAVPDSGVVAALGYAAKAGVAFQQGLIRSHYVGRTFIEPSQKIRDFGVKLKLSPVRGVLEGKRVVVVDDSIVRGTTSSKIVRLLREAGAKEVHMRIASPPIIASCYYGVDTPSSNELISNRMSVDEIRDYIGCDSLAFLSFETLKKHLGEDSRSFCYACFTGDYPVKPTEDKVKRGGDFIDDGLVGGIHNIEGGWVR
Protein: Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 (Mitochondrial targeting suppressor 1 protein) (Nuclear polyadenylated RNA-binding protein 1) (Nuclear protein localization protein 3) (Polyadenylate-binding protein NPL3) (Q01560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mRNA processing and export. Required for efficient splicing of a large set of pre-mRNAs by efficient co-transcriptional recruitment of the splicing machinery. Remains associated with the mRNP during early steps of translation elongation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:7962083, ECO:0000269|PubMed:9499403}. Cytoplasm, Stress granule {ECO:0000269|PubMed:26777405}. Note=Nuclear at steady state and its import is mediated by the karyopherin MTR10 (PubMed:14676199, PubMed:15542855). Export is dependent on active transcription and the export of mRNAs in general (PubMed:14676199, PubMed:8675010). {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:15542855, ECO:0000269|PubMed:8675010}.
Interaction partners:
- Serine/arginine
- Serine/threonine-protein kinase SKY1
- U1 small nuclear ribonucleoprotein A
- Protein NAM8
- U1 small nuclear ribonucleoprotein component SNU71
- mRNA transport regulator MTR10
- mRNA export factor MEX67
- RNA annealing protein YRA1
- Nuclear polyadenylated RNA-binding protein NAB2
- Pre-mRNA-splicing factor CEF1
Sequence:
MSEAQETHVEQLPESVVDAPVEEQHQEPPQAPDAPQEPQVPQESAPQESAPQEPPAPQEQNDVPPPSNAPIYEGEESHSVQDYQEAHQHHQPPEPQPYYPPPPPGEHMHGRPPMHHRQEGELSNTRLFVRPFPLDVQESELNEIFGPFGPMKEVKILNGFAFVEFEEAESAAKAIEEVHGKSFANQPLEVVYSKLPAKRYRITMKNLPEGCSWQDLKDLARENSLETTFSSVNTRDFDGTGALEFPSEEILVEALERLNNIEFRGSVITVERDDNPPPIRRSNRGGFRGRGGFRGGFRGGFRGGFSRGGFGGPRGGFGGPRGGYGGYSRGGYGGYSRGGYGGSRGGYDSPRGGYDSPRGGYSRGGYGGPRNDYGPPRGSYGGSRGGYDGPRGDYGPPRDAYRTRDAPRERSPTR
Protein: Beta-selinene synthase (EC 4.2.3.66) (Terpene synthase 21) (ZmTps21) (A0A291LSD6)
Organism: Zea mays (Maize)
Function: Sesquiterpene cyclase that converts farnesyl diphosphate to the volatile beta-selinene and the corresponding nonvolatile antibiotic derivative beta-costic acid, especially in roots upon infection by rootworm larvae (D.balteata) and fungal pathogens (e.g. Fusarium spp.).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
Interaction partners:
- Putative cytochrome P450 superfamily protein
Sequence:
MDGDIAAALPPVNQQSKADGTAVAAAAAAAACHGDFEPSVWGDFFVTYTSPPSLSQEPEEQMRERANFLKGEVRKKFEAAAAMSAINSAMLVDAVVHLGIDHCFREEIATALRSVHKEEGEFGSCDDLHTVAVRFLVLRQHGLWVSADVFDKFRDDTGSLSKSLLCSNPRGLLSLYNAAHMVTPEEKVLDDAIAFARSHLEAMIGELRSPMVEQVSRSLDIPLPRFSRRLESMHYIAEYGQEEGHDAQILELARLEFELVRSLHLRELREICRWWRELYNDVKLPYARDRIVEIYFWACGVIHEEEMSRARMIFAKTFAFTSLIDDTCDVHATLEEVQKFNEAMQSWEEDAVSIVPEYLRTLYSRTIKGFQEFEDMLEPNEKYSMSYVKKAYKLLLQYYLKEATWANENHTPSFKEHVQVSIISSGLPMLVPVLLMGTGLATREAFEWADSAPDMVLASGEVGRFLNDMASYKLGKNKKDVANAHECYMKEYGATGEEAFAFIANMTENAWRKINQACMEMDPAMLPAFKVAVVDLSRSMEIIYLGGKRDAYTFGSNLKDLVTSLFLKPCA
Protein: G1/S-specific cyclin-D3 (P48961)
Organism: Rattus norvegicus (Rat)
Function: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Shows transcriptional coactivator activity with ATF5 independently of CDK4.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30281}. Cytoplasm {ECO:0000250|UniProtKB:P30281}.
Interaction partners:
- cyclin-dependent kinase
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase inhibitor 1C
- Retinoblastoma-associated protein
- Retinoblastoma-like protein 2
- M-phase inducer phosphatase 1
Sequence:
MELLCCEGTRLAPRAGPDPRLLGDQRVLQSLLRLEERYVPRGSYFQCVQKEIKPHMRKMLAYWMLEVCEEQRCEEDVFPLAMNYLDRYLSCVPTRKAQLQLLGTVCLLLASKLRETTPLTIEKLCIYTDQAMAPWQLREWEVLVLGKLKWDLAAVIAHDFLALILHRLSLPSDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVLGLGACSMSADELTELLAGITGTEVDCLRACQEQQIEAALRESLREAAQTAPSPVPKAPGGSSSQGPSQTSTPTDVTAIHL
Protein: Heat shock protein 70 (Hsp 70) family protein (B3H683)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g17830
- Heat shock protein 90-6, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Mitochondrial import inner membrane translocase subunit TIM44-1
- Elongation factor G-1, mitochondrial
- Elongation factor G-2, mitochondrial
- Similar to part of disease resistance protein domain family protein)
- Heat shock 70 kDa protein 17
- AT4g14060/dl3070w
- Major latex protein-like
Sequence:
MLSKARVVSWRSGNVKSGMLSKARVVSWRAGNANGHGERSRVACSERQRKELIDTKNTADTTIYSIEKSLGEYREKIPSEIAKEIEDAVADLRSASSGDDLNEIKAKIEAANKAVSKIGEHMSGGSGGGSAPGGGSEGGSDQAPEAEYEEVKK
Protein: MYB transcription factor (Myb domain protein 69) (Putative transcription factor) (Q9SZC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NAC domain-containing protein 73
- NAC domain-containing protein 10
- NAC domain-containing protein 12
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 66
- NAC domain-containing protein 43
- NAC domain-containing protein 30
- NAC domain-containing protein 104
Sequence:
MEMSRGSNSFDNKKPSCQRGHWRPVEDDNLRQLVEQYGPKNWNFIAQHLYGRSGKSCRLRWYNQLDPNITKKPFTEEEEERLLKAHRIQGNRWASIARLFPGRTDNAVKNHFHVIMARRKRENFSSTATSTFNQTWHTVLSPSSSLTRLNRSHFGLWRYRKDKSCGLWPYSFVSPPTNGQFGSSSVSNVHHEIYLERRKSKELVDPQNYTFHAATPDHKMTSNEDGPSMGDDGEKNDVTFIDFLGVGLAS
Protein: Enkurin, TRPC channel interacting protein L homeolog (LOC496000 protein) (Q5PQ29)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- WD repeat-containing protein 90
- Uncharacterized protein.
- Enkurin domain-containing protein 1 isoform X1
- Parkin coregulated gene protein homolog isoform X1
- EF-hand domain
- EF-hand domain-containing family member C2
- EF-hand domain-containing family member C2
- Uncharacterized protein.
- DUF667 domain-containing protein.
- SEC14 domain and spectrin repeat-containing protein 1-A isoform X1
Sequence:
MKEMYPSESIYNLIPQEEVKVSKPPRYVSTFRESVKVENKKVKAAHKTMGPAKVEPPIPGDFLHKHTKEFMLAEKSASMDPSEKIPRCLDEEKRRPPVPHHTDHPVMGVHSNKNFIKTNVAEAVMAVPKKPQPISVDTKKGDKHVLESSGLVPKYLKKKDYGETPEYIVKRNEEVKRAQEEYDAYVKERLRMGAMKQLSDEERQSVLEGLKKNWDKLHHDYQALSVVIDTPPKKAHKERLEAEMKQLEKDIDRLERHKIIYIANN
Protein: C2H2-type domain-containing protein (I2HAK0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGEFQYNFDDEDTVLIGNYEEVGTEIDEADEQHNEENSEDDEEDESPIPSKKRVSFAVPLVQSRSKQKDEMNKVHIIKCHFDKCNKSYNWRKKYGKLRLVDHAFTHVPHLKMKCNFCDYMCKGIRNIRLHHKKSHPDEQLTGFGIKSVVRTSKKGKDLAKVWDECFKKNRVLQHGSGTDSNLLHFSRQDKGSKRSQKSMDSGAKQKLDEARDEDVKPFYFFRIR
Protein: HIRA-interacting protein 3 (Q7SXB4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKEKDAIRKFVVAQLQKCSDLSTLTLGILRRRYLVKVGRESLSAQDRQLMKVIVEEELLKMQASSDDEPLIKMVNPSKTQSKRKRVDDEDDEEEERKVMDRTKRSRLEESPPPDSPDSGIEKAMNEVGHKEEAGSDKDTDEDSEEEEKEKMKGKPQKKKGGKKSPQVEDNRKKKKLKKKTIESDEDEELEDSEEEERQKPKEKEDSDSEEAAKSESASDSEDEKPKSKTKTPSKRKDIRKKKPVERDVVKEVEREVFGSSSESEEEKNQSAKIKNGSISEDESAGDSDEERDKSEDAAGLPSKETKNNEKLRDGQEEAEDSDSSSLPSLEDEEEQEKEKTKKEGKKSVRKKSSEERENTSRGKDEENKAVSRLKRYIALCGVRRNYKKLLDGCRSVKAKVAVLKKELEELGVEGQPSIEKCKKARLKREEAQELAELDMSNIITTQGRPKRRAAAAVWPPAQNASPPSSAYKRVVDSDSDSGYSHTNRGRKRGAWANLHGIISDDGDSE
Protein: Mitochondrial import receptor subunit TOM40 homolog (Mitochondrial outer membrane protein of 38 kDa) (OM38) (Translocase of outer membrane 40 kDa subunit homolog) (Q75Q40)
Organism: Rattus norvegicus (Rat)
Function: Channel-forming protein essential for import of protein precursors into mitochondria. Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I components from the cytosol to the mitochondria (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O96008}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the mitochondria-associated ER membrane via interaction with BCAP31. {ECO:0000250|UniProtKB:O96008}.
Interaction partners:
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM22 homolog
- Translocase of outer mitochondrial membrane 5
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM20 homolog
- Translocase of outer mitochondrial membrane 6.
- Sorting and assembly machinery component 50 homolog
- Metaxin-1
- Metaxin
- Superoxide dismutase
Sequence:
MGNVLAASSPPAGPPPPPTPSLVGLPPPPPSPPGFTLPPLGGGLGTGSNAGRGSERTPGAAASGAAASSNDGNCGCLPNPGTFEECHRKCKELFPVQMEGVKLTVNKGLSNRFQVTHTVALGTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLSPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGELVYHRRPGEKGTVMSLAGKYTLNNWLATVTLGQAGMHATYYHKASDQLQVGVEFEASTRMQDTSASFGYQLDLPKANFLFKGSVNSNWIVGATLEKKLPPLPLTLSLCAFLNHRKNKFLCGFGLTIG
Protein: CBS domain-containing protein CBSX2, chloroplastic (CBS domain-containing protein 1) (AtCDCP1) (Protein LOSS OF THE TIMING OF ET AND JA BIOSYNTHESIS 1) (AtLEJ1) (Q9C5D0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18633119}.
Interaction partners:
- CBS domain-containing protein CBSX3
- CBS domain-containing protein CBSX6
- F-box/LRR-repeat protein At3g62440
- CBS domain-containing protein CBSX5
- SNF1-related protein kinase regulatory subunit gamma-like PV42b
- CBS domain-containing protein CBSCBSPB3
- RNA-binding
- BRISC and BRCA1-A complex member 1
- Uncharacterized protein At1g27050
- CBS domain-containing protein CBSCBSPB4
Sequence:
MGSISLSNSMPITRLPLLTSLYHQSFLPISSSSFSLLPLSNRRRSSTFSPSITVSAFFAAPASVNNNNSVPAKNGGYTVGDFMTPRQNLHVVKPSTSVDDALELLVEKKVTGLPVIDDNWTLVGVVSDYDLLALDSISGRSQNDTNLFPDVDSTWKTFNELQKLISKTYGKVVGDLMTPSPLVVRDSTNLEDAARLLLETKFRRLPVVDADGKLIGILTRGNVVRAALQIKRETENST
Protein: DNA polymerase II subunit B4 (Nuclear transcription factor Y subunit B-11) (AtNF-YB11) (Q9ZQH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon catalytic subunit B
- DNA polymerase alpha catalytic subunit
- DNA polymerase alpha subunit B
- Probable DNA primase large subunit
- DNA primase
- DNA polymerase delta catalytic subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase II subunit B3-1
Sequence:
MESEKVVVDELPLAIVRRVVKKKLSECSPDYDVSIHKEALLAFSESARIFIHYLSATANDFCKDARRQTMKADDVFKALEEMDFSEFLEPLKSSLEDFKKKNAGKKAGAAAASYPAGGAALKSSSGTASKPKETKKRKQEEPSTQKGARKSKIDEETKRNDEETENDNTEEENGNDEEDENGNDEEDENDDENTEENGNDEENDDENTEENGNDEENEKEDEENSMEENGNESEESGNEDHSMEENGSGVGEDNENEDGSVSGSGEEVESDEEDE
Protein: Ras-related protein Rab-25 (EC 3.6.5.2) (CATX-8) (P57735)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia. Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tight junctions (By similarity). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:17925226}. Cell projection, pseudopodium membrane {ECO:0000269|PubMed:17925226}. Note=Colocalizes with integrin alpha-V/beta-1 in vesicles at the pseudopodial tips. Colocalizes with RAB11A in subapical vesicles (By similarity). {ECO:0000250|UniProtKB:P46629, ECO:0000269|PubMed:17925226}.
Interaction partners:
- Rab11 family-interacting protein 2
- Rab11 family-interacting protein 1
- Rab11 family-interacting protein 5
- Unconventional myosin-Vb
- Rab11 family-interacting protein 3
- Rab11 family-interacting protein 4
- Epithelial splicing regulatory protein 1
- Optineurin
- Rab proteins geranylgeranyltransferase component A 2
- Keratinocyte differentiation factor 1
Sequence:
MGNGTEEDYNFVFKVVLIGESGVGKTNLLSRFTRNEFSHDSRTTIGVEFSTRTVMLGTAAVKAQIWDTAGLERYRAITSAYYRGAVGALLVFDLTKHQTYAVVERWLKELYDHAEATIVVMLVGNKSDLSQAREVPTEEARMFAENNGLLFLETSALDSTNVELAFETVLKEIFAKVSKQRQNSIRTNAITLGSAQAGQEPGPGEKRACCISL
Protein: Translation initiation factor IF-1 (Q8IKE7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Eukaryotic translation initiation factor 4C
- Translation initiation factor SUI1, putative
Sequence:
MCSVFITRLSFDFFVFLFFCFFFLYFPSEEIKVEKKTFSFLNFNNNISQWKNNKTSRFFHKISWNKKHIKNNINHFLRDKKGVHILYEKNENVKNEIPKTKENDTFEMNGVVVECLANTNFIVSIPNGEKFLCFISGKLRINKVKINLGDMVKFQIHKLNFEKRRGKIVFRYLQHTSLKKKK
Protein: 14 kDa phosphohistidine phosphatase (EC 3.9.1.3) (Phosphohistidine phosphatase 1) (PHPT1) (Protein histidine phosphatase) (PHP) (P59083)
Organism: Sus scrofa (Pig)
Function: Exhibits phosphohistidine phosphatase activity.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MAAAADLAQIPDVDIDSDGVFKYVLIRVHAVSPPGTPAGESKEIVRGYKWAEYHADIYDKVSGEMQKKGIDCECLGGGRISHQSQDKKIHVYGYSMGYGRAQHSISTEKIKARYPDYSVTWADDGY