wanglab/gogpt-training-data huggingface dataset:
Protein: Retinoic acid receptor responder protein 2 (Chemerin) (RAR-responsive protein TIG2) (Tazarotene-induced gene 2 protein) (Q99969)
Organism: Homo sapiens (Human)
Function: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2. Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9DD06}.
Interaction partners:
- Chemerin-like receptor 1
- Chemerin-like receptor 2
- C-C chemokine receptor-like 2
- Leukotriene B4 receptor 1
- Serpin A12
- Intelectin-1
- Nicotinamide phosphoribosyltransferase
- Adiponectin
- Resistin
- Resistin-like beta
Sequence:
MRRLLIPLALWLGAVGVGVAELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKRDWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQRAGEDPHSFYFPGQFAFSKALPRS
Protein: Neutral alpha-glucosidase AB (EC 3.2.1.207) (Alpha-glucosidase 2) (Glucosidase II subunit alpha) (Q14697)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:33097077, ECO:0000305|PubMed:10929008}. Golgi apparatus {ECO:0000250|UniProtKB:P79403}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Glucosidase 2 subunit beta
- Mannosyl-oligosaccharide glucosidase
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Calnexin
- Calreticulin
- N-acetylglucosamine-1-phosphotransferase subunit gamma
- Endoplasmin
- Protein disulfide-isomerase A3
- DnaJ homolog subfamily B member 11
- Endoplasmic reticulum chaperone BiP
Sequence:
MAAVAAVAARRRRSWASLVLAFLGVCLGITLAVDRSNFKTCEESSFCKRQRSIRPGLSPYRALLDSLQLGPDSLTVHLIHEVTKVLLVLELQGLQKNMTRFRIDELEPRRPRYRVPDVLVADPPIARLSVSGRDENSVELTMAEGPYKIILTARPFRLDLLEDRSLLLSVNARGLLEFEHQRAPRVSQGSKDPAEGDGAQPEETPRDGDKPEETQGKAEKDEPGAWEETFKTHSDSKPYGPMSVGLDFSLPGMEHVYGIPEHADNLRLKVTEGGEPYRLYNLDVFQYELYNPMALYGSVPVLLAHNPHRDLGIFWLNAAETWVDISSNTAGKTLFGKMMDYLQGSGETPQTDVRWMSETGIIDVFLLLGPSISDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNLPCDVIWLDIEHADGKRYFTWDPSRFPQPRTMLERLASKRRKLVAIVDPHIKVDSGYRVHEELRNLGLYVKTRDGSDYEGWCWPGSAGYPDFTNPTMRAWWANMFSYDNYEGSAPNLFVWNDMNEPSVFNGPEVTMLKDAQHYGGWEHRDVHNIYGLYVHMATADGLRQRSGGMERPFVLARAFFAGSQRFGAVWTGDNTAEWDHLKISIPMCLSLGLVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLPSQHNDIIRDALGQRYSLLPFWYTLLYQAHREGIPVMRPLWVQYPQDVTTFNIDDQYLLGDALLVHPVSDSGAHGVQVYLPGQGEVWYDIQSYQKHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSECMKDDPITLFVALSPQGTAQGELFLDDGHTFNYQTRQEFLLRRFSFSGNTLVSSSADPEGHFETPIWIERVVIIGAGKPAAVVLQTKGSPESRLSFQHDPETSVLVLRKPGINVASDWSIHLR
Protein: Interleukin (Q5UB38)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMCKVLIFGCISVAMLMTTAYGASLSSAKRKPLQTLIKDLEILENIKNIHLELYTPTETQECTQQTLQCYLGEVVTLKKETEDDTEIKEEFVTAIQNIDKNLKSLTGLNHTGSECKVCEANNKKKFPDFLHELTNFVRYLQK
Protein: Vacuolar protein sorting-associated protein 16B (Protein full-of-bacteria) (Q9VAG4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for phagosome maturation and the innate immune response to bacteria. During phagosome maturation it is required for the fusion of late endosomes/lysosomes and phagosomes.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H269}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H269}. Early endosome {ECO:0000250|UniProtKB:Q9H269}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q920Q4}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9H269}.
Interaction partners:
- Vacuolar protein sorting 33B
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar protein sorting-associated protein 41 homolog
Sequence:
MDLQLDSESYWNRSSRAAFSFDDEDEVDLAPDLVSNGILADDTISEASFNNSVALNLSIKSILSEEALKLVLQEQALDDRVLPKGVSPEEELKLLRRQLQSTLYSPNLEATAQKLLQGKTAPLEMFKSLHEKQQLLDTLMAQGGGHAVITVLLFLKRTLNTTQFHGILRERPKALEQYLSYLKESGDLAGHIELLQLFGRHQEAALKQFQAALASGDTSTRKKHLQLLVDAYATAGVGVIPLYEQVFHAALKMQQLMEKDSALGKLLRDQPTPVEVLYACCQVNSNWKEQDMLKPVSPQRFAADQQISPAQYEWTALNERAQAQAYADLECIFERVPSWHPLKTKQFHISFDLTLAVLRLYELQAPSTVLQLFLSKMGNSVEKLALAQRVKCIKAVIDAMAGLKQQQELQQLKDTLPERSEEQFYCENALKSLQSKRWTTDNIKLKL
Protein: Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) (dp28b) (Q9XZT1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 31
- Cyclin-C
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MAIVSSARESLSHAMNNRFLPNLEYLLQGSILDSAVEHLMHRLKGLCDNVDTSPEPFHDLEVCMSLRQPNANQPLLLRVRRALGRDAPFQMRYLGNPEVDLRRPTLVRSCMDCACTNGILEFLTEMGFRLEFEYIAKGYMFRKGRMKITVSKLIKIVPGKQQDMANEPISQSYIVELSVVAPTGQENVGEEMRVFAEQLKPLVQLEKIDYKRLGGMP
Protein: Lysosomal amino acid transporter 1 homolog (PQ-loop repeat-containing protein 2) (Solute carrier family 66 member 1) (B0BMY1)
Organism: Rattus norvegicus (Rat)
Function: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:23169667}; Multi-pass membrane protein {ECO:0000269|PubMed:23169667}.
Interaction partners:
- Cystinosin
Sequence:
MVWRTLVASNFSTCPNGSIQWIWDVFGECAQDGWDEASVALGLVSIFCFAASTFPQYIKACKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLLMLTLYFHYKFKKQPSLLSAPINSVLLFILGTVCITPLLSSTDPVAVPREGFRGRTLLSVEPGNKPFTKKEVVGFVIGSASSVLYLLSRLPQIRTNFVRQSTQGISYSLFALVMLGNTLYGLSVLLKNPEVGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRSHDADAASEREPLLPS
Protein: Scm polycomb group protein like 2 (A0A571BDL9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAEPATGVQLAGSGELVAEPGPSSTEAREPATGVQLAGSGQLVAEQGPPSTGGREPATGVQLAGSGELVAEPGPSSTEAREPATAEGTSGLGQQVTKQGHPSTGEMEPATGVQLAGSGELVAEPGPSSTEARENTEEANTMGQTANEDHFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKEEPPRPLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPGKIVEKRPRR
Protein: GH18144p (Q95U01)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRERHDIERHTRWYDIKKKFESDPRYRMVDSMYREEYFEDYLHIMKEEKRKEREMREQRERERHRELKSDRKEKDKEKDKGRKDRGRSRSKDKDREHKSSKEKDKDKEEKSKSEKSKKRDTTPEEGEHREESEREERAGSDDSEVARQRENEAEQKQKEREKKLRVEQSIREREKEVQRTLAGHLRDRDKEREHHMREECIGHFTALLTDLVRTPDFTWKEVKRQLRKDHRWELIESLDREDRERKFNEHIDNLMKKKRERFREMLDEISTLQLTSTWKEIKKLIKEDPRYLKYNSDKGEREFRDYIKDKTMTAKTSLRELLQECKFITHKSSDLIKENPNHLKEIQDILKNDKRYLVLDHMEEERNTIVLGFLEELNKRGPPPPPTASESTRRNK
Protein: DNA primase small subunit (EC 2.7.7.102) (DNA primase 49 kDa subunit) (p49) (P20664)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which play an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit. Can add both ribo- and deoxynucleotides during elongation of the primers. Synthesizes 9-mer RNA primers (also known as the 'unit length' RNA primers) (By similarity). Incorporates only ribonucleotides in the presence of ribo- and deoxy-nucleotide triphosphates (rNTPs, dNTPs). Requires template thymine or cytidine to start the RNA primer synthesis, with an adenine or guanine at its 5'-end (By similarity). Binds single stranded DNA.
Interaction partners:
- DNA polymerase alpha subunit B
- DNA polymerase alpha catalytic subunit
- DNA primase large subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit A
- Replication factor C subunit 4
- DNA polymerase delta subunit 2
- DNA polymerase epsilon subunit 2
- DNA replication licensing factor MCM5
- DNA polymerase zeta catalytic subunit
Sequence:
MEPFDPAELPELLKLYYRRLFPYAQYYRWLNYGGVTKNYFQHREFSFTLKDDIYIRYQSFNNQSELEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDDVRRCCSSADICSKCWTLMTMAMRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLNEKVHPFVRKSINIIKKYFEEYALVGQDILENKENWDKILALVPETIHDELQRGFQKFHSSPQRWEHLRKVANSSQNMKNDKCGPWLEWEVMLQYCFPRLDVNVSKGVNHLLKSPFSVHPKTGRISVPIDFHKVDQFDPFTVPTISAICRELDMVSTHEKEKEENEADSKHRVRGYKKTSLAPYVKVFEQFLENLDKSRKGELLKKSDLQKDF
Protein: Bone morphogenetic protein 5 (BMP-5) (P49003)
Organism: Mus musculus (Mouse)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cartilage and bone formation or neurogenesis. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathway such as MAPK p38 signaling cascade to promote chondrogenic differentiation (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1A
- Noggin
- Activin receptor type-2B
- Activin receptor type-1
- Activin receptor type-2A
- Bone morphogenetic protein receptor type-1B
- Chordin
- Neuroblastoma suppressor of tumorigenicity 1
- Hemojuvelin
Sequence:
MHWTVFLLRGIVGFLWSGWVQVGYAKGGLGDNHVHSSFIYRRLRNHERREIQREILSILGLPHRPRPFSPGKQASSAPLFMLDLYNAMASEDNPEEYLVRVSLAGEAKETRKGYPASPNGYAHRLHLPPRTPLTTQSPPLASLHDTNFLNDADMVMSFVNLVERDKDFSHQRRHYKEFRFDLTQIPHGEAVTAAEFRIYKDKGNHRFENETIKISIYQIIKEYTNRDADLFLLDTRKTQALDVGWLVFDITVTSNHWVINPQNNLGLQLCAETGDGRSINVKSAGLVGRHGPQSKQPFMVAFFKASEVLLRSVRAASKRKNQNRNKSNSHQDPSRMPSAGDYNTSEQKQACKKHELYVSFRDLGWQDWIIAPEGYAAFYCDGECSFPLNAHMNATNHAIVQTLVHLMFPDHVPKPCCAPTKLNAISVLYFDDSSNVILKKYRNMVVRSCGCH
Protein: Uncharacterized protein (Q583K3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
- Bms1-type G domain-containing protein
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S23, putative
- Bystin, putative
- Protein LTV1 homolog
- 40S ribosomal protein S8
- RNA-binding protein NOB1
- PNO1 second type I KH domain-containing protein
Sequence:
MPPTRPEFEAPPDILYNADGAQRYTRSGRVQMVQRAMTRRALELLALPSGCPALLLDVGCGSGLSGEVLRECGHTWIGIDISTDMLGMAKASEELMREDDEKEDEGPIEGVDLRDVRWGPIHDENENENENDDHDSTDGDGNEAEAVLPPGPSIVEVMRGDMGEGLPFRPGAFDGAVSISAVQWLCQSDRRGQVPQRRLRALFQCLYNALRRGAKAAIQFYPANVEQLHMITRAAMLCGFSGGVVVDFPHSTKAKKHYLVVQAGQVAGGFMPPRPLSVCNEGGEEVEEEEECEEEDGEEEGEEENDEGQRFGARVGGRVAHKRSRSHGGRQAGARRRKDNRPVTGTKEWVLLKKAERRKFGLKTSEDTKYTMRRRRPRF
Protein: Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (Q9P3A8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor (Probable).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cullin-1
- Cullin-3
- RING-box protein pip1
- Cullin-4
- COP9 signalosome complex subunit 5
- BTB/POZ domain-containing protein 3
Sequence:
MEEGILLKKYVESSDKDIRYMALSDLAARLNDANHLKNLKLESFPDTLDVLLQALSDASPEVQQEAVRCVAIISSKIPQDKLKSTVENLLSGVAGKKSKNYLSALSLLLSNSNVQPFVNKFYTSTVFPSFLQILKQYNVAQEEFFAILCVVCDSLEIYHSNLSTLLPNNFELCIDVFQKCTTQCQRELIIKKACYLLSDVSLYGPRFAYKYIIEVLDRGLGPSTQMSEVNISIKLLNEILLSSKKEKDSSTSFISTAVADYTNKILSLLKKEEAPDELTQKLLEVLGLLLEYQQVNILKIWPELHGLLISKISYDPNLISDTNDEDDIADFLEEMSDYSSIYEDEEDVSWIVRRESLKVVLSVILSRLEYLPIVLQALGTSVVSKLNDREESVCLISIEVLKQAFLHVPRWIEVYATSNDRKRRYEGLPSDRSAISDTSIYLVSVIGKHVSKLSDKTPLSIVSELLNLVTVIFSSRDLGVQSEFSNLSSIIYRFPDFSTLDIKIKLNLVRLISAIISCGCEEIENMESKMSTILSLAVQNNYPQLSYEALITELSFCKYIHKKQPTNVSTDFSTMIDSSLQLLESKISDLKVRLALIDLVSQYVILFYEPDFDSIFLRRVLIILCKKLQEEPTRSAAARALCDIFMSVTDITKIENGTKIYEEILQDCCRHIDKSGNEFTTAYLELLEVLLKVGQKYLAESLLEHILGLLIETLKRNTENTVAILKCLLIIPLSILLKSKNLLIDTIISHLQSSTIHLNEESVCLLSRIIAVISKEEDLELIINSFTCAQKPVEEMVTLALIAAQLICIFQSKAIVTSLNKSFMSPKSEVRIKVFTTLIFGQLDYGKLTLPANEYFDTIASNLNSPNADVMKAAAIALGSLTSQSEKFIKELCALYVSDAYDKELLLISFLTFLKKSKIDYETADKIWDILSKDIENIKDFSTSPFRTLLSECLGLLICNESSSLYYKLELLSSSEASNHMLLSLSVFRFSLTLDCPKLKAYEKQFFEKAYKLFQNPDLEVSQETLQVIISVIKNRRSCIADVYNELLQGLISKSSVDSSNVHVVQMGPFQHVVDNSINQRQLVFETLYSLLDIPESLNHLTHFLQVSVMGLEDEHYIKLVSLSILEKLVDCSPSIIDEQVDTILEALRKIIELRKTEKTLKTDSDNILDLVRSALRVLFTMKLKCDNPVISEFESQVQKGPYSLEYEGIKNEIKTTIKT
Protein: Suppressor of Mek1 (SMEK) (Q54I18)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Suppresses MEK1 null cell polarity, chemotaxis, and gene expression defects. Required for proper cytokinesis during vegetative growth, timely exit from the mound stage during development, and myosin II assembly. May be a regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) and may control localization of PP4 to the nucleus. Involved in the regulation of some ppp4c functions, such as developmental progression, chemotaxis, expression of stress response genes and cell movement.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:16107728}. Nucleus {ECO:0000269|PubMed:16107728}. Note=Localizes to the cell cortex in vegetative cells but translocates to the nucleus during starvation and development (PubMed:16107728).
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Probable serine/threonine-protein phosphatase 2A activator 2
- Probable serine/threonine-protein phosphatase 2A activator 1
- Protein phosphatase 2A catalytic subunit B
- Serine/threonine-protein phosphatase 2A catalytic subunit A
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Uncharacterized protein
- Histone H2AX
- Protein KRTCAP2 homolog
Sequence:
MEPLRKRVKVYQLDNSGKWDDKGTGHVSCIYVDALCAMGLIVRSESDNSVILQTRLSAEDIYQKQQDSLIVWTEPDSQLDLALSFQDSLGCQDIWENILQYQNQRTGSCDSVDLDLPPVSINNLQTINELLEASLPMLDKDKIINSIFKEDLVRSLLDLFDEIEKSGEGGVHLFQIFNIFKNLILFNDTSILEVILSEDYLVRVMGALEYDPEISENNRIKHREFLNQQVVFKQVIKFPSKSLIGTIHQTFRIQYLKDVVLPRVLDDVTFSSLNSLIYFNNIDIVSQIQNDSDFLENLFSEIQKSEKNSEERKDLILFLQDLCNLAKGLQIQSKSTFFTVVVSLGLFKTLSAILDDENVQTRVSCTEIVLSTLLHDPEILRSYLCSPTSGNSKFLVQLINLFITDKDIGVKNQIVEIIKTLLEADSYDSSDFFRLFYDKGIDLLVSPLNEVYKGEPTIPGDPSSNLDSFVLYNIMELVIYCIKHHCYRIKHFIVEEGIAKKILRYTNPTGSGGGGGGGGNSERYLILGSIRFFRSMVNMKDDLYNQHIIQENLFEPIIEVFKSNISRYNLLNSAIIELFQYIYKENIRDLIVYLVERYRELFESVTYTDVLKQLILKYEQIKDSSFESPETSCNNNDSSSNDIDSKPIIGNNKINHNYQRTQREIDEEEEEAYFNRDDDSEDSDDEDELIPISINNNNNNNNNNKQICTNNENNMEKNDDNIEKDNENTNNGNGSSHIKIVDYEDEDDEDDEINKSVESDDIVEKHEIIDKNEKKDEIMKENNDSDNDDNDNNDNDNDNDNNSDIENKNHLNNNGNNENNENNDDVQDKSNNKNNSDKINEDEKIEKQDEMKENLEMEEIDEKVKEKQPKDIKKENQSQPDETVFNGKSNNSNNNNNNNNNNSNNQEIGDNRKTTPKRKLDYEKNESVVSKKIDKSNGPTSIDKDINGCDESPNKKLNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNQNDENELSSASEEEEEQLENGKHIKKFKRGKKDSNNSSNNSNNSSPTPSELHV
Protein: Putative thiosulfate sulfurtransferase SseA (EC 2.8.1.1) (P9WHF7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized SufE-like protein Rv3284
- Putative thiosulfate sulfurtransferase SseB
- IscS-like cysteine desulfurase
- Sulfite reductase [ferredoxin]
- Adenosine 5'-phosphosulfate reductase
- Putative thiosulfate sulfurtransferase
- cysteine-S-conjugate beta-lyase
- Putative cystathionine beta-lyase
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- L-cysteine desulfhydrase Cds1
Sequence:
MPLPADPSPTLSAYAHPERLVTADWLSAHMGAPGLAIVESDEDVLLYDVGHIPGAVKIDWHTDLNDPRVRDYINGEQFAELMDRKGIARDDTVVIYGDKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPTKTCTGYPVVQRNDAPIRAFRDDVLAILGAQPLIDVRSPEEYTGKRTHMPDYPEEGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYDFINPDDQTVVYCRIGERSSHTWFVLTHLLGKADVRNYDGSWTEWGNAVRVPIVAGEEPGVVPVV
Protein: Transcription factor PIF3 (Basic helix-loop-helix protein 8) (AtbHLH8) (bHLH 8) (Phytochrome-associated protein 3) (Phytochrome-interacting factor 3) (Transcription factor EN 100) (bHLH transcription factor bHLH008) (O80536)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor acting in the phytochrome signaling pathway. Activates transcription by binding to the G box (5'-CACGTG-3'). Acts as a negative regulator of phytochrome B signaling. Represses chlorophyll biosynthesis and photosynthesis in the dark. Recruits the histone deacetylase HDA15 to the promoters of chlorophyll biosynthetic and photosynthetic genes. HDA15 represses their transcription by histone deacetylation. Promotes the expression of MDP60 to modulate hypocotyl cell elongation in response to light and ethylene signaling. Required for submergence-induced and ethylene-dependent underwater hypocotyl elongation.
Subcellular location: Nucleus {ECO:0000269|PubMed:23548744}.
Interaction partners:
- Phytochrome A
- Phytochrome B
- DELLA protein RGA
- DELLA protein GAI
- DELLA protein RGL2
- DELLA protein RGL1
- DELLA protein RGL3
- Histone deacetylase 15
- Transcription factor HY5
- Transcription factor PIF4
Sequence:
MPLFELFRLTKAKLESAQDRNPSPPVDEVVELVWENGQISTQSQSSRSRNIPPPQANSSRAREIGNGSKTTMVDEIPMSVPSLMTGLSQDDDFVPWLNHHPSLDGYCSDFLRDVSSPVTVNEQESDMAVNQTAFPLFQRRKDGNESAPAASSSQYNGFQSHSLYGSDRARDLPSQQTNPDRFTQTQEPLITSNKPSLVNFSHFLRPATFAKTTNNNLHDTKEKSPQSPPNVFQTRVLGAKDSEDKVLNESVASATPKDNQKACLISEDSCRKDQESEKAVVCSSVGSGNSLDGPSESPSLSLKRKHSNIQDIDCHSEDVEEESGDGRKEAGPSRTGLGSKRSRSAEVHNLSERRRRDRINEKMRALQELIPNCNKVDKASMLDEAIEYLKSLQLQVQIMSMASGYYLPPAVMFPPGMGHYPAAAAAMAMGMGMPYAMGLPDLSRGGSSVNHGPQFQVSGMQQQPVAMGIPRVSGGGIFAGSSTIGNGSTRDLSGSKDQTTTNNNSNLKPIKRKQGSSDQFCGSS
Protein: Evasin P1080 (A0A090XBL6)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
FFQLAVFVVILFNINLLSASAGSKGSSAPQSSGDSVVAEFCDTNCTMKKDGKWTECNGDCFCVHVGNETVGRCMRLDGDYDYTSSKTTRRNKKTRNGLCRLDRNRTTVDYPERNTREP
Protein: Regulator of microtubule dynamics protein 3 (RMD-3) (hRMD-3) (Cerebral protein 10) (Protein FAM82A2) (Protein FAM82C) (Protein tyrosine phosphatase-interacting protein 51) (TCPTP-interacting protein 51) (Q96TC7)
Organism: Homo sapiens (Human)
Function: Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:16820967, ECO:0000269|PubMed:17361080, ECO:0000269|PubMed:22131369, ECO:0000269|PubMed:29858488}; Single-pass membrane protein {ECO:0000269|PubMed:16820967}. Cytoplasm {ECO:0000269|PubMed:17361080}. Nucleus {ECO:0000269|PubMed:17361080}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. {ECO:0000269|PubMed:18070910}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein B/C
- Oxysterol-binding protein-related protein 5
- Oxysterol-binding protein-related protein 8
- Tyrosine-protein phosphatase non-receptor type 1
- Motile sperm domain-containing protein 2
- Mitofusin-2
- Regulator of microtubule dynamics protein 2
- 14-3-3 protein beta/alpha
- Prolyl 3-hydroxylase 3
- B-cell receptor-associated protein 31
Sequence:
MSRLGALGGARAGLGLLLGTAAGLGFLCLLYSQRWKRTQRHGRSQSLPNSLDYTQTSDPGRHVMLLRAVPGGAGDASVLPSLPREGQEKVLDRLDFVLTSLVALRREVEELRSSLRGLAGEIVGEVRCHMEENQRVARRRRFPFVRERSDSTGSSSVYFTASSGATFTDAESEGGYTTANAESDNERDSDKESEDGEDEVSCETVKMGRKDSLDLEEEAASGASSALEAGGSSGLEDVLPLLQQADELHRGDEQGKREGFQLLLNNKLVYGSRQDFLWRLARAYSDMCELTEEVSEKKSYALDGKEEAEAALEKGDESADCHLWYAVLCGQLAEHESIQRRIQSGFSFKEHVDKAIALQPENPMAHFLLGRWCYQVSHLSWLEKKTATALLESPLSATVEDALQSFLKAEELQPGFSKAGRVYISKCYRELGKNSEARWWMKLALELPDVTKEDLAIQKDLEELEVILRD