wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Heat shock protein family B member 1) (Stress-responsive protein 27) (SRP27) (P04792)
Organism: Homo sapiens (Human)
Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10777697, ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000269|PubMed:19464326}.
Interaction partners:
- MAP kinase-activated protein kinase 2
- MAP kinase-activated protein kinase 5
- Cytochrome c
- Heat shock 70 kDa protein 4
- RAC-alpha serine/threonine-protein kinase
- Eukaryotic translation initiation factor 4 gamma 1
- Heat shock cognate 71 kDa protein
- BAG family molecular chaperone regulator 3
- MAP kinase-activated protein kinase 3
- Death domain-associated protein 6
Sequence:
MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK
Protein: Cytochrome c oxidase subunit 13, mitochondrial (Cytochrome c oxidase polypeptide VIa) (P32799)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 3
Sequence:
MFRQCAKRYASSLPPNALKPAFGPPDKVAAQKFKESLMATEKHAKDTSNMWVKISVWVALPAIALTAVNTYFVEKEHAEHREHLKHVPDSEWPRDYEFMNIRSKPFFWGDGDKTLFWNPVVNRHIEHDD
Protein: GTPase Era (Q5SM23)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity).
Subcellular location: Cytoplasm. Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAEKTYSGFVAIVGKPNVGKSTLLNNLLGVKVAPISPRPQTTRKRLRGILTEGRRQIVFVDTPGLHKPMDALGEFMDQEVYEALADVNAVVWVVDLRHPPTPEDELVARALKPLVGKVPILLVGNKLDAAKYPEEAMKAYHELLPEAEPRMLSALDERQVAELKADLLALMPEGPFFYPEDYAKSDQTFGEWVAEILREEAMKRLWHEVPYAVATKVEEVAERENGVLYIKAILYVERPSQKAIVIGEGGRKIKEIGQATRKQLEALLGKKVYLDLEVKVYPDWRKDPEALRELGYRSSVG
Protein: Sugar utilization regulatory protein IMP2 (P32351)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Controls the nucleo-mitochondrial dependence of galactose, maltose and raffinose utilization. Becomes essential in the absence of functioning mitochondria.
Interaction partners:
- Mitochondrial inner membrane protease subunit 2
- Altered inheritance of mitochondria protein 20
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MQKSILLTKPDGTQSNLHSIKTETPTTVEFDSEQMERGHRERGRSKKKRGERDSNVSSLSRSRSRASSRSRVREEEFLKWTVLRQDPSMRLRVVDVDSEEEGEGNDEDDDDGDGDDMDEEESDEEQVSDIENDLEIDEEFHYDLGMKVLPNFCTSINEVLDSSKPWIAKYEISIRGHENEDVSLEQLDGGYVRAMQLLTKGAGAEAGNQRSFILYTDLSSESTYALTYLMGAAVNQGDTVYIVHWEPSKPTDDSQMFANVARIRKHVMHLFDCVAGVLDDLDVVVLSLTHPYPKHLLNEMIHGLKPVALCCSLSVILSTLQNFVCSVPILAVRKKLKRAKRKGISE
Protein: Villin-3 (Q67U26)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Ca(2+)-regulated actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. MF severing is promoted by VLN1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O81644}.
Interaction partners:
- Os03g0225600 protein
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 3
- Os11g0157701 protein
- Conserved oligomeric Golgi complex subunit 8
- Expressed protein
Sequence:
MAVSMREVDAVFQGAGQKDGLEIWRIEKLQAVPVPKESHGRFFTGDSYVILKTTALKNGSFRHDIHYWLGKDTSQDEAGTAAIKTVELDAALGGRAVQYREVQGNETERFLSYFKPCIIPEEGGIASGFRHTEINEREHVTRLFVCRGKHTVHVKEVPFARSSLNHDDIFILDTKSKIFQFNGSNSSIQERAKALEVVQYLKDSNHEGKCDVGSVEDGKLMADADAGEFWGLFGGFAPLPRKTFSDLNGKDSAFSSKLICLNKGQTVPVDFDVLTRELLDSTKCYLLDCGSEIYVWMGRETPLEERKRAGSAAEELLREVNRPKSHIVRLMEGFETVIFRSKFSKWPKKADAVVSDESRGKVAALLKRQGFNVKGLAKAAPVKEEPQPQIDCTGNLQVWRVNGTEKTFLSFSEQCKFYSGDCYIFQYSYPGEEGEECLIGTWFGKKSVQDEKTTAISVASKMVESLKFQAVMVRLYEGKEPAEFFSIFQNLVIFKGGVSTGYKKFVSENGIEDDTYSENGVALFRVQGSGPENMQAIQVDTAATSLNSSYCYVLHDGDTLFTWIGNLSSSMDQELAERQLDVIKPNLQSRMLKEGSEYDQFWKLLGVKSEYPSQKIAKDQESDPHLFSCTFSKGVLKVREIFNFTQDDLMTEDVFILDCHSCVFVWVGQRVDTKMRAQALSVGEKFLELDILMENSSQETPVYVITEGSEPQFFTRFFTWDSAKSAMHGNSFERRLSIVKDGVKPKLDKPKRRPTTSSSHTGRSSVPEKSQRSRSMSFSPDRVRVRGRSPAFNALAANFENPNARNLSTPPPAIRKPSPKSPSSDPTKPPQRAASIAAISASFERPRPTLIPKSIKASPDVNKPQVEASKPKPEANGKDSTPSKDSPTVTPTIQEDLKEGQPENEEGLPVYPYERLRTSSINPVTDIDVTKRETYLSAAEFRERFGMTKEAFAKLPKWKQNRLKIALQLF
Protein: Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (Beta-2 adrenoceptor) (P07550)
Organism: Homo sapiens (Human)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23166351, ECO:0000269|PubMed:25220262, ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}; Multi-pass membrane protein {ECO:0000269|PubMed:19584355}. Early endosome {ECO:0000269|PubMed:20559325}. Golgi apparatus {ECO:0000269|PubMed:27481942}. Note=Colocalizes with VHL at the cell membrane (PubMed:19584355). Activated receptors are internalized into endosomes prior to their degradation in lysosomes (PubMed:20559325). Activated receptors are also detected within the Golgi apparatus (PubMed:27481942). {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:27481942}.
Interaction partners:
- Beta-arrestin-2
- Beta-arrestin-1
- Na
- Guanine nucleotide-binding protein G
- S-arrestin
- Beta-adrenergic receptor kinase 1
- A-kinase anchor protein 12
- Sorting nexin-27
- Beta-1 adrenergic receptor
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL
Protein: Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39) (P00879)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:24907906}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:24907906). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000269|PubMed:24907906}.
Interaction partners:
- Ribulose bisphosphate carboxylase small subunit
- Ribulose bisphosphate carboxylase/oxygenase activase
- Carboxysome assembly protein CcmM
- RuBisCO accumulation factor 1
- Phosphoribulokinase
- RuBisCO chaperone RbcX
- phosphoribulokinase
- Phosphoglycerate kinase
- All2681 protein
- Phosphoglycolate phosphatase
Sequence:
MSYAQTKTQTKSGYKAGVQDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQFIAYIAYPLDLFEEGSITNVLTSIVGNVFGFKALRALRLEDIRFPVAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSAPFQRWRDRFLFVADAITKAQAETGEIKGHYLNVTAPTCEEMLKRAEYAKELKQPIIMHDYLTAGFTANTTLARWCRDNGVLLHIHRAMHAVIDRQKNHGIHFRVLAKALRLSGGDHIHTGTVVGKLEGERGITMGFVDLLRENYVEQDKSRGIYFTQDWASLPGVMAVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREAAKWSPELAVACELWKEIKFEFEAMDTV
Protein: RAB6-interacting golgin (N-terminal kinase-like-binding protein 1) (NTKL-BP1) (NTKL-binding protein 1) (mNTKL-BP1) (SCY1-like 1-binding protein 1) (SCYL1-BP1) (SCYL1-binding protein 1) (Q8BRM2)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12783284}. Golgi apparatus {ECO:0000269|PubMed:18997784}.
Interaction partners:
- N-terminal kinase-like protein
- Ras-related protein Rab-6A
- RING finger and CHY zinc finger domain-containing protein 1
- ADP-ribosylation factor 5
- Serine/threonine-protein kinase PDIK1L
Sequence:
MAQDWAGFSEEELRRLKQNKDPFEPQRRIPVKKTRQQLQREKALLEQSQKLGLQDGSASLLPEQLLSAPKQRANSQKPRSPSPVAPSPLTPTSSSGDGKLPGVGSQPQEPGLENSHHGHKSAEVRAPKPDCKVEKKKMELQEKSRWEVLQQEQRLMEEKNKRKKALLAQAIAERSKKTQAETIKLKRIQKELQALDDMVSADIGILRNRIDQASLEYSYARKRFDRAEAEYITAKLDLQRKTETKEQLTEHLCTIIQQNELRKAKKLEELMQQLDVQADEEALQLEVEVEQLLREQEAEAAKQMASVERLCPPDGESVSSELAEENNEPQKQAPSPETDKPGKCCSSSPHRLDCPDPGAKNFSAAVAT
Protein: Cytochrome c biogenesis protein CcsA (P0C376)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01391}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01391}.
Interaction partners:
- Uncharacterized protein
- ResB-like domain-containing protein
- Cytochrome C biogenesis protein transmembrane domain-containing protein
- uroporphyrinogen-III C-methyltransferase
- Glutamyl-tRNA reductase, chloroplastic
- NAD
Sequence:
MLFATLEHILTHISFSTISIVITIHLITLLVRELGGLRDSSEKGMIATFFCITGFLVSRWASSGHFPLSNLYESLIFLSWALYILHMIPKIQNSKNDLSTITTPSTILTQGFATSGLLTEMHQSTILVPALQSQWLMMHVSMMLLSYATLLCGSLLSAALLMIRFRKNLDFFSKKKKNVLLKTFFFNEIEYFYAKRSALKSTFFPLFPNYYKYQLIERLDSWSYRVISLGFTLLTIGILCGAVWANEAWGSYWNWDPKETWAFITWTIFAIYLHSRTNPNWKGTKSAFVASIGFLIIWICYFGINLLGIGLHSYGSFTLPI
Protein: CUE domain-containing protein 5 (O14319)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 26S proteasome regulatory subunit rpn12
- Vacuole membrane protein hfl11
- SH3 domain-containing protein PJ696.02
Sequence:
MASEQSNPRLPRRPPYMAEKARATLKEAFPNTDDAIIRAVLAASGYKLEPAFNALLGLSDPQVAEEMEQAETSYAYDTAAHDDPVQRQLEEDERCARELANRYNSHRPERRRKTNNDRRNYPPQNRTAKPNDNDGDDYSFFEDDLPVIKDTFMRGFQSFKQRSMEWVENIASKFDGEEEDDDDEKYSAPSKIYPSPRRSTAATLESAYEERPPSLPRRKPSRPGTAITLPPYESDPHMLNEKDFERLRLESSSSPMMRRSSLNSNRRSVESSSSAAFVEGQSFILDSNGAIEVANSAFALDDSDLESAYNEELEMKKDTSKPTASTKEVVVEKKPDESRKQAARTLETVSEEQMGSSNAKSKVLTSEPKDSTSVEAEKTETDEPAVGKGASDVSDTAEISEKTEAKNADSEANLEEKSDVGEEKESKDENNKASLHKDVEEKDTKITNEDTGKTETDVKAKETDSIEANDKDEKTDSKETEDKVEETESKEADVKAKETDSIEVDDKEEKTDSKETADKVEQTDSKDTNEKPAKDDNKEANEKAEKVDSKDVKEKIEEAADLQNSGKET
Protein: Regulator of microtubule dynamics protein 1 (Protein FAM82B) (Q387R8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MSTWEQAVEEADKAFAKRDCKAVCEIIEKAESDGTCHVQLMWRRARALHTLGDESLDKSEKERYARDAAVAAERAVEEDPTSAEANLWKAICIGILCDYLTTKERMSNVYVIRDHLLRSLELKSDNPDALHGMGMWSLSLLQISWFERSAASLLFGSLPTVSHEECLKYFLASHELRPSIRNCLALGNLFRYQGNWTEAKTWYQKALDIPAETHAHKQKQDEAVQLLNSC
Protein: Serine/threonine-protein kinase Aurora-2 (AtAur2) (EC 2.7.11.1) (Aurora-like kinase 2) (Q683C9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylates specifically 'Ser-10' of histone H3 in vitro. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. Might colocalize with gamma-tubulin and function in microtubule organizing centers (MTOCs).
Subcellular location: Nucleus membrane. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Nuclear membrane in interphase cells, spindle poles at prophase and mitotic spindle from metaphase to telophase.
Interaction partners:
- Kinetochore protein NDC80 homolog
- Mitotic spindle checkpoint protein MAD2
- Microtubule-associated protein RP/EB family member 1C
- Microtubule-associated protein RP/EB family member 1A
- Microtubule-associated protein RP/EB family member 1B
- Kinesin-like protein KIN-10A
- Mitotic checkpoint protein BUB3.1
- Ubiquitin-conjugating enzyme E2 20
- Chromatin structure-remodeling complex protein SYD
- Zinc finger, C3HC4 type
Sequence:
MLYQAASEAAQKRWTTSDFDIGKPLGRGKFGHVYLAREKRSDHIVALKVLFKAQLQQSQVEHQLRREVEIQSHLRHPNILRLYGYFYDQKRVYLILEYAVRGELYKELQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENLLIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAREHSETYKRIVQVDLKFPPKPIVSSSAKDLISQMLVKESTQRLALHKLLEHPWIVQNADPSGLYRG
Protein: p53 protein long form variant 2 (Q2XVY7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLHKSASFSLTFNQNTSIVSRSNSRTIFEAFKEFLDFWDIGNEVSAESAVRVSSNGAFNLPQSFGNESNEYAHLATPVDPAYGGNNTNNMMQFTNNLEILANNNSDGNNKINACNKFVCHKGTDSEDDSTEVDIKEDIPKTVEVSGSELTTEPMAFLQGLNSGNLMQFSQQSVLREMMLQDIQIQANTLPKLENHNIGGYCFSMVLDEPPKSLWMYSIPLNKLYIRMNKAFNVDVQFKSKMPIQPLNLRVFLCFSNDVSAPVVRCQNHLSVEPLTANNAKMRESLLRNENPNSVYCGNAQGKGISERFSVVVPLNMSRSVTRSGLTRQTLAFKFVCQNSCIGRKETSLVFCLEKACGDIVGQHVIHVKICTCPKRDRIQDERQLNSKKRKSVPEAAEEDEPSKVRRCIAIKTEDTESNDSRDCDDSAAEWNVSRTPDGDYRLAITCPNKEWLLQSIEGMIKEAAAEVLRNPNQENLRRHANKLLSLKKRAYELP
Protein: Transcription factor MYB3R-4 (Myb-related protein 3R-4) (Protein ENHANCED DEFECTIVE CYTOKINESIS) (Q94FL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds 5'-AACGG-3' motifs in gene promoters. Involved in the regulation of cytokinesis, probably via the activation of several G2/M phase-specific genes transcription (e.g. KNOLLE). Required for the maintenance of diploidy.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Transcription factor E2FB
- Retinoblastoma-related protein 1
- Protein tesmin/TSO1-like CXC 5
- Cyclin-dependent kinase A-1
- Transcription factor E2FC
- SUPPRESSOR OF GAMMA RESPONSE 1
- Cyclin-dependent protein kinase inhibitor SMR7
- Cyclin-B1-1
- CRC domain-containing protein TSO1
- Kinesin-like protein KIN-7N
Sequence:
MEAESSTPQERIPKLRHGRTSGPARRSTRGQWTAEEDEILRKAVHSFKGKNWKKIAEYFKDRTDVQCLHRWQKVLNPELVKGPWTKEEDEMIVQLIEKYGPKKWSTIARFLPGRIGKQCRERWHNHLNPAINKEAWTQEEELLLIRAHQIYGNRWAELTKFLPGRSDNGIKNHWHSSVKKKLDSYMSSGLLDQYQAMPLAPYERSSTLQSTFMQSNIDGNGCLNGQAENEIDSRQNSSMVGCSLSARDFQNGTINIGHDFHPCGNSQENEQTAYHSEQFYYPELEDISVSISEVSYDMEDCSQFPDHNVSTSPSQDYQFDFQELSDISLEMRHNMSEIPMPYTKESKESTLGAPNSTLNIDVATYTNSANVLTPETECCRVLFPDQESEGHSVSRSLTQEPNEFNQVDRRDPILYSSASDRQISEATKSPTQSSSSRFTATAASGKGTLRPAPLIISPDKYSKKSSGLICHPFEVEPKCTTNGNGSFICIGDPSSSTCVDEGTNNSSEEDQSYHVNDPKKLVPVNDFASLAEDRPHSLPKHEPNMTNEQHHEDMGASSSLGFPSFDLPVFNCDLLQSKNDPLHDYSPLGIRKLLMSTMTCMSPLRLWESPTGKKTLVGAQSILRKRTRDLLTPLSEKRSDKKLEIDIAASLAKDFSRLDVMFDETENRQSNFGNSTGVIHGDRENHFHILNGDGEEWSGKPSSLFSHRMPEETMHIRKSLEKVDQICMEANVREKDDSEQDVENVEFFSGILSEHNTGKPVLSTPGQSVTKAEKAQVSTPRNQLQRTLMATSNKEHHSPSSVCLVINSPSRARNKEGHLVDNGTSNENFSIFCGTPFRRGLESPSAWKSPFYINSLLPSPRFDTDLTIEDMGYIFSPGERSYESIGVMTQINEHTSAFAAFADAMEVSISPTNDDARQKKELDKENNDPLLAERRVLDFNDCESPIKATEEVSSYLLKGCR
Protein: PelG (Q9HZF0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PelF
- PelE
- PelD
- PelC
- PelA
- PelB
- Uncharacterized protein
Sequence:
MAGIGFELRKILSRDSYTATLRAYLYAGLISSGPWVLSIVSVMLIGVLSLGVVVPDVLVRQFLITVTYLMALSLIFTGGLQLFFTRFISDRLFERKHEAILPNLVGVLLLVTLAAGLLSAILLATLFDEPFAYRLLVMANFVVLCNLWLVIIFLSGMKAYKRILLVMFIGYALMVACAYLLRFMQMDGLLLALLIGHASLLFVFLYDILREYPARRMVAFDFLDRRQVFVSLLLTGLCYNLGIWIDKFIFWFNPSTSDLVIGPLRASILYDLPIFLAYLSIIPGMAVFLVRIETDFAEWYERVYEAIRGGETLQHIGLLKEQMILAIRQGLLEICKVQGLAVVLLFLLAPQLLGWLGISRYYLPLFYIDLIGVSIQVVFMALLNVFFYLDKRRIVLELCVLFVIVNGALTFVSLLLGPSFFGYGFTLSLLVCVLVGLYRLTTALDDLEYETFMLNR
Protein: Gna13a protein (Guanine nucleotide binding protein (G protein), alpha 13a) (Q4VBH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADFLPSRTAIVCIPNCLLSGGEIDQIRKSKEFDKSLSREKTYVKKLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAKEEFRATIYSNVIKGVRVLVDAREKLHIPWGNPENQAHGETVMAFDTRSSLMAKGMMETKVFLNFLPAIRALWQDSGIQNAYDRRREFQLGESVKYFLDNVDKLGQLDYLPSQKDILLARKPTKGIHEYEFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEYDQVLMEDRQTNRLTESLNIFETIVNNRVFANVSIILFLNKTDLLEDKVKTVNIKDYFSEFTGEPHNLQDVQKFLVECFRNKRREQQQKPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
Protein: Ribonucleoside-diphosphate reductase large subunit-like protein (Q6SW87)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Does not possess a ribonucleotide reductase activity. Betaherpesviruses probably use another strategy to expand the dNTP pool in a quiescent host cell.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04027}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04027}.
Interaction partners:
Sequence:
MNPADADEEQRVSSVPAHRCRPGRIPSRSAETETEESSAEVAADTIGGDDSELEEGPLPGGDKEASAGNTNVSSGVACVAGFTSGGGVVSWRPESPSPDGTPSVLSLTRDSGPAVPSRGGRVSSGLSTFNPAGATRMELDSVEEEDDFGASLCKVSPPIQAMRMLMGKKCHCHGYWGKFRFCGVQEPARELPSDRNALWREMDTVSRHSAGLGSFRLFQLIMRHGPCLIRHSPRCDLLLGRFYFKANWARESRTPLCYASELCDESVRRFVLRHMEDLPKLAEETARFVELAGCWGLYAAILCLDKVCRQLHGQDESPGGVFLRIAVALTAAIENSRHSRIYRFHLDARFEGEVLESVLKRCRDGQLSLSTFTMSTVGFDRVPQYDFLISADPFSRDASWAAMCKWMSTLSCGVSVSVNVTRLNADVNSVIRCLGGYCDLIREKEVHRPVVRVFVDMWDVAAIRVINFILKESTSELTGVCYAFNVPSVLMKRYRAREQRYSLFGRPVSRRLSDLGQESAFEKEYSRCEQSCPKVVVNTDDFLKKMLLCALKGRASVVFVHHVVKYSIMADSVCLPPCLSPDMASCHFGECDMPVQRLTVNVARCVFARSDEQKLHLPDVVLGNTRRYFDLSVLRELVTEAVVWGNARLDALMSASEWWVESALEKLRPLHIGVAGLHTALMRLGFTYFASWDLIERIFEHMYFAAVRASVDLCKSGLPRCEWFERTIYQEGKFIFELYRLPRLSIASARWEALRADMLEFGLRNCQFLAVGPDDEVAHLWGVTPSVWASRGTVFEEETVWSLCPPNRECYFPTVVRRPLRVPVVNYAWLEQHQEEGKATQCLFQAAPAIQNDVEMAAVNLSVFVDQCVALVFYYDSGMTPDVLLARMLKWYHWRFKVGVYKYCAS
Protein: Carnosine dipeptidase 2 (J3QRD0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDK
Protein: Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4) (Q684P5)
Organism: Homo sapiens (Human)
Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15632203}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15632203}.
Interaction partners:
- Ras-related protein Rap-1b
- 14-3-3 protein zeta/delta
- Ras-related protein Rap-1A
- 14-3-3 protein beta/alpha
Sequence:
MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQKNKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRHFLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVLYPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVESVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYKVSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGPEEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPIKRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSSTSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDKLSHASSGAGH
Protein: Fucose-specific lectin (Aleuria aurantia lectin) (AAL) (P18891)
Organism: Aleuria aurantia (Orange peel mushroom)
Function: Lectin that specifically binds to L-fucose. Has strongest preference for the alpha-1,6-fucosylated chain (core fucose) on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and alpha-1,6-fucosylated chains. Might play a role in the differentiation of the fruiting body. Exhibits antifungal activity against Mucor racemosus and thus could act as an antifungal protein in natural ecosystems.
Interaction partners:
Sequence:
MPTEFLYTSKIAAISWAATGGRQQRVYFQDLNGKIREAQRGGDNPWTGGSSQNVIGEAKLFSPLAAVTWKSAQGIQIRVYCVNKDNILSEFVYDGSKWITGQLGSVGVKVGSNSKLAALQWGGSESAPPNIRVYYQKSNGSGSSIHEYVWSGKWTAGASFGSTVPGTGIGATAIGPGRLRIYYQATDNKIREHCWDSNSWYVGGFSASASAGVSIAAISWGSTPNIRVYWQKGREELYEAAYGGSWNTPGQIKDASRPTPSLPDTFIAANSSGNIDISVFFQASGVSLQQWQWISGKGWSIGAVVPTGTPAGW
Protein: Ribosomal large subunit pseudouridine synthase D (EC 5.4.99.23) (23S rRNA pseudouridine(1911/1915/1917) synthase) (Large ribosomal subunit assembly factor RluD) (rRNA pseudouridylate synthase D) (rRNA-uridine isomerase D) (P33643)
Organism: Escherichia coli (strain K12)
Function: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA. Isomerization occurs as a late step during the assembly of the large ribosomal subunit.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:33639093}. Note=Associates with late stage pre-50S ribosomal subunits (PubMed:33639093). {ECO:0000269|PubMed:33639093}.
Interaction partners:
- GTPase ObgE/CgtA
- Purine nucleoside phosphorylase YfiH
- Ribosomal silencing factor RsfS
- Dual-action ribosomal maturation protein DarP
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL15
Sequence:
MAQRVQLTATVSENQLGQRLDQALAEMFPDYSRSRIKEWILDQRVLVNGKVCDKPKEKVLGGEQVAINAEIEEEARFEPQDIPLDIVYEDEDIIIINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVESLQRREITREYEAVAIGHMTAGGTVDEPISRHPTKRTHMAVHPMGKPAVTHYRIMEHFRVHTRLRLRLETGRTHQIRVHMAHITHPLVGDPVYGGRPRPPKGASEAFISTLRKFDRQALHATMLRLYHPISGIEMEWHAPIPQDMVELIEVMRADFEEHKDEVDWL