wanglab/gogpt-training-data huggingface dataset:
Protein: Sensor histidine kinase CheAY (EC 2.7.13.3) (O25153)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Member of the two-component regulatory system CheAY/CheY that regulates chemotaxis and colonization of the gastric mucosa. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of CheY. In turn, phosphorylated CheY (CheY-P) interacts with the flagellar motor protein FliM to cause clockwise flagellar rotation and bacterial reversals, as opposed to straight swimming when CheY is not phosphorylated (By similarity).
Interaction partners:
- Methyl-accepting chemotaxis transducer
- Chemotaxis protein CheW
- Chemotaxis protein CheV1
- Methyl-accepting chemotaxis protein
- Methyl-accepting chemotaxis protein
- Chemotaxis protein CheV2
- Chemotaxis protein CheV3
- Hemolysin secretion protein
- Flagellar motor switch protein FliN
- Chemotaxis protein CheY1
Sequence:
MDDLQEIMEDFLIEAFEMNEQLDQDLVELEHNPEDLDLLNRIFRVAHTIKGSSSFLNLNILTHLTHNMEDVLNRARKGEIKITPDIMDVVLRSIDLMKTLLVTIRDTGSDTNNGKENEIEEAVKQLQAITSQNLESAKERTTEAPQKENKEETKEEAKEENKENKAKAPTAENTSSDNPLADEPDLDYANMSAEEVEAEIERLLNKRQEADKERRAQKKQEAKPKQEVTPTKETPKAPKTETKAKAKADTEENKAPSIGVEQTVRVDVRRLDHLMNLIGELVLGKNRLIRIYSDVEERYDGEKFLEELNQVVSSISAVTTDLQLAVMKTRMQPVGKVFNKFPRMVRDLSRELGKSIELIIEGEETELDKSIVEEIGDPLIHIIRNSCDHGIEPLEERRKLNKPETGKVQLSAYNEGNHIVIKISDDGKGLDPVMLKEKAIEKGVISERDAEGMSDREAFNLIFKPGFSTAKVVSNVSGRGVGMDVVKTNIEKLNGIIEIDSEVGVGTTQKLKIPLTLAIIQALLVGVQEEYYAIPLSSVLETVRISQDEIYTVDGKSVLRLRDEVLSLVRLSDIFKVDAILESNSDVYVVIIGLADQKIGVIVDYLIGQEEVVIKSLGYYLKNTRGIAGATVRGDGKITLIVDVGAMMDMAKSIKVNITTLMNESENTKSKNSPSDYIVLAIDDSSTDRAIIRKCLKPLGITLLEATNGLEGLEMLKNGDKIPDAILVDIEMPKMDGYTFASEVRKYNKFKNLPLIAVTSRVTKTDRMRGVESGMTEYITKPYSGEYLTTVVKRSIKLEGDQS
Protein: At3g56830 (YCF20-like protein (DUF565)) (Q9LES5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g43050
- Defensin-like protein 130
- Methyl-CpG-binding domain-containing protein 2
Sequence:
MGFAITVTLPNCGSKFLPKRSFRDKGALSLAICSLCHFLHPAQPLLVRHQRRMSWTTIKSSVGGDRFDPASGSSSNNSSRGLRLIKAIQVLRSKLLVKIQEIKKDLPKKLFFLLVGFYSATAFSTFIGQTGDWDVLSAGLAVLVVECIGALMYRASIPLINKMRSTITMFNYWKTGLALGLFLDSFKF
Protein: Antitoxin ParD1 (P58091)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of cognate toxin ParE1, but no other RelE or ParE toxin. May act as a DNA gyrase inhibitor (By similarity).
Interaction partners:
- Toxin ParE1
- Antitoxin ParD4
- Toxin ParE4
- Toxin ParE3
- Toxin RelE4
- Toxin RelE1
- DNA topoisomerase 4 subunit B
- Orphan antitoxin ParD2
Sequence:
MASKNTSVVLGDHFQAFIDSQVADGRYGSASEVIRAGLRLLEENEAKLAALRAALIEGEESGFIEDFDFDAFIEERSRASAPQGFHEE
Protein: Pituitary homeobox 2 (Homeobox protein PITX2) (cPITX2) (Paired-like homeodomain transcription factor 2) (O93385)
Organism: Gallus gallus (Chicken)
Function: May play an important role in development and maintenance of anterior structures. May play a role in determining left-right asymmetry and in vasculogenesis during avian embryogenesis.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:P97474}.
Interaction partners:
- Left-right determination factor.
- Sonic hedgehog protein
- Insulin gene enhancer protein ISL-1
- Bone morphogenetic protein 4
- T-box transcription factor TBX5
- Fibroblast growth factor 8
Sequence:
MSCMKDPLSLERLGAGNNKLCSSSPSSSSSSSSCHHQQPALAMATALAPGQARSSLEAAKHRLEVHTISDTSSPEAAEKEKSQQGKSEDAGPEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSGLNSLNNLNNLSNPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPASNLSACQYPVDRPV
Protein: Neuronal acetylcholine receptor subunit alpha-2 (P12389)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:Q15822}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q15822}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-7
- Neuronal acetylcholine receptor subunit beta-3
- Muscle, skeletal receptor tyrosine protein kinase
- Agrin
- Acetylcholine receptor subunit alpha
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholinesterase
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit epsilon
- Acetylcholine receptor subunit delta
Sequence:
MTLSHSALQFWTHLYLWCLLLVPAVLTQQGSHTHAEDRLFKHLFGGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWDPAEFGNVTSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFFTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMERTVDLKDYWESGEWAIINATGTYNSKKYDCCAEIYPDVTYYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHNMPNWVRVALLGRVPRWLMMNRPLPPMELHGSPDLKLSPSYHWLETNMDAGEREETEEEEEEEDENICVCAGLPDSSMGVLYGHGGLHLRAMEPETKTPSQASEILLSPQIQKALEGVHYIADRLRSEDADSSVKEDWKYVAMVVDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
Protein: GDNF family receptor alpha-3 (GDNF receptor alpha-3) (GDNFR-alpha-3) (GFR-alpha-3) (O60609)
Organism: Homo sapiens (Human)
Function: Receptor for the glial cell line-derived neurotrophic factor, ARTN (artemin). Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9576965}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:9576965}.
Interaction partners:
- Artemin
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Persephin
- Neurturin
- Glial cell line-derived neurotrophic factor
- GDNF family receptor alpha-1
- High affinity nerve growth factor receptor
- GDNF family receptor alpha-4
Sequence:
MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLGNYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRGSGNLQEECEMLEGFFSHNPCLTEAIAAKMRFHSQLFSQDWPHPTFAVMAHQNENPAVRPQPWVPSLFSCTLPLILLLSLW
Protein: P2X purinoceptor 1 (P2X1) (ATP receptor) (Purinergic receptor) (P51576)
Organism: Mus musculus (Mouse)
Function: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51575}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}. Note=Detected at plasma membrane lipid rafts. {ECO:0000250|UniProtKB:P51575}.
Interaction partners:
- P2X purinoceptor 7
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 2
- P2X purinoceptor
- Glutamate receptor ionotropic, NMDA 1
- P2Y purinoceptor 12
- Neuronal acetylcholine receptor subunit alpha-7
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 2A
Sequence:
MARRLQDELSAFFFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFVYEKGYQTSSGLISSVSVKLKGLAVTQLQGLGPQVWDVADYVFPAHGDSSFVVMTNFIMTPQQAQGHCAENPEGGICQDDSGCTPGKAERKAQGIRTGNCVPFNGTVKTCEIFGWCPVEVDDKIPSPALLHEAENFTLFIKNSISFPRFKVNRRNLVEEVNGTYMKKCLYHKILHPLCPVFSLGYVVRESGQDFRSLAEKGGVVGITIDWECDLDWHVRHCKPIYQFHGLYGEKNLSPGFNFRFARHFVQNGTNRRHLFKVFGIRFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKRHYYKQKKFKYAEDMGPGEGERDPAATSSTLGLQENMRTS
Protein: Phenylacetic acid degradation protein PaaY (P77181)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Transcriptional repressor PaaX
- Bifunctional protein PaaZ
- Acyl-coenzyme A thioesterase PaaI
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- Phenylacetate-coenzyme A ligase
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-epoxyphenylacetyl-CoA isomerase
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 3-hydroxyadipyl-CoA dehydrogenase
Sequence:
MPIYQIDGLTPVVPEESFVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPEQDTVVGEDGHIGHSAILHGCIIRRNALVGMNAVVMDGAVIGENSIVGASAFVKAKAEMPANYLIVGSPAKAIRELSEQELAWKKQGTHEYQVLVTRCKQTLHQVEPLREIEPGRKRLVFDENLRPKQ
Protein: Contig An14c0180, genomic contig (EC 1.16.3.1) (A2R3T0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MIRTLITLGLYGFVQQVSSKDVYLDWNITWVTAAPDGYARPVIGINGHWPCPQIDVDVGDNLIVDVYNGLGNESTGIHWHGLHQNYNGYMDGVPGVTQCELHPNQRMRYIVPINQTGTYWYHSHEPGQYPDGLRGPIIVHDNVPAPYHYDEEMTLTLSDWYHVQIPVLLDEFIVPSDHAPYGGQEPLPDAVLFNDMHNTKISVKPGTTYLIHVVCMGNFPGHALVIDDHDMTIVGMDGIAVEPHFLPPQYLRVAVGQRVDILLTTKNDTSKNYAIWDGLDIDEMFVQEGRSPPQGYNPNGTAWLMYNEDAPLPPPPVIHVNNASLDFLDDVTLTPRDHLPLIDPIQHQFIFDVYPTTVDGKPAYSINNMTYNAPDSPTLYTAIYSDPEACMDPDLYGDVNPFVVNYGDVVEIVLNNHHDNLHPWHLHGHDFQVLQRTYPYGGFFDGYRNVSATPMRRDTLMVEPLGHFVIRFRAMNPDKLDVSKLTLIGQLRIWMFHCHIEWHVEIRLMAIIIEAPDQLQNMTIPDDHLKICGNTQPSNWAPLAPSP
Protein: Lamin-B1 (P14733)
Organism: Mus musculus (Mouse)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Subcellular location: Nucleus lamina {ECO:0000269|PubMed:28241138}.
Interaction partners:
- Prelamin-A/C
- Delta
- Lamin-B2
- SUN domain-containing protein 1
- Emerin
- Barrier-to-autointegration factor
- SUN domain-containing protein 2
- Caspase-6
- Nesprin-2
- Nesprin-1
Sequence:
MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSCAIM
Protein: Inhibitor of growth protein 3 (p47ING3) (Q9NXR8)
Organism: Homo sapiens (Human)
Function: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome.
Subcellular location: Nucleus.
Interaction partners:
- Histone acetyltransferase KAT5
- Mortality factor 4-like protein 1
- Chromatin modification-related protein MEAF6
- DNA methyltransferase 1-associated protein 1
- Transformation/transcription domain-associated protein
- YEATS domain-containing protein 4
- Bromodomain-containing protein 8
- Enhancer of polycomb homolog 1
- RuvB-like 1
- RuvB-like 2
Sequence:
MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDTPSQPVNNHHAHSHTPVEKRKYNPTSHHTTTDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASSNNAYNVNSSQPLGSYNIGSLSSGTGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMARETVGYSSSSALMTTLTQNASSSAADSRSGRKSKNNNKSSSQQSSSSSSSSSLSSCSSSSTVVQEISQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWYCPQCTAAMKRRGSRHK
Protein: Ribosome quality control complex subunit 1 (Q05468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. RQC1 is essential for the recruitment of CDC48 to ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome quality control complex subunit 2
- E3 ubiquitin-protein ligase listerin
- Cell division control protein 48
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- tRNA endonuclease VMS1
- E3 ubiquitin-protein ligase HEL2
- Elongation factor 1 alpha-like protein
- Protein DOM34
Sequence:
MSSRALRRLQDDNALLESLLSNSNANKMTSGKSTAGNIQKRENIFSMMNNVRDSDNSTDEGQMSEQDEEAAAAGERDTQSNGQPKRITLASKSSRRKKNKKAKRKQKNHTAEAAKDKGSDDDDDDEEFDKIIQQFKKTDILKYGKTKNDDTNEEGFFTASEPEEASSQPWKSFLSLESDPGFTKFPISCLRHSCKFFQNDFKKLDPHTEFKLLFDDISPESLEDIDSMTSTPVSPQQLKQIQRLKRLIRNWGGKDHRLAPNGPGMHPQHLKFTKIRDDWIPTQRGELSMKLLSSDDLLDWQLWERPLDWKDVIQNDVSQWQKFISFYKFEPLNSDLSKKSMMDFYLSVIVHPDHEALINLISSKFPYHVPGLLQVALIFIRQGDRSNTNGLLQRALFVFDRALKANIIFDSLNCQLPYIYFFNRQFYLAIFRYIQSLAQRGVIGTASEWTKVLWSLSPLEDPLGCRYFLDHYFLLNNDYQYIIELSNSPLMNCYKQWNTLGFSLAVVLSFLRINEMSSARNALLKAFKHHPLQLSELFKEKLLGDHALTKDLSIDGHSAENLELKAYMARFPLLWNRNEEVTFLHDEMSSILQDYHRGNVTIDSNDGQDHNNINNLQSPFFIAGIPINLLRFAILSEESSVMAAIPSFIWSDNEVYEFDVLPPMPTSKESIEVVENIKTFINEKDLAVLQAERMQDEDLLNQIRQISLQQYIHENEESNENEG
Protein: Meiotically up-regulated gene 82 protein (Q9HDZ3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL33m
- Uncharacterized peptide chain release factor-like protein C1105.18c
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein bS16m
- Putative peptide chain release factor 1, mitochondrial
- Large ribosomal subunit protein bL32m
Sequence:
MFANFRNCFKIKNSRLIYDNINKCLLTKEETNQLLKFIHLKWKPAKDQVQISFSRSSGPGGQNVNKLNTKVIVNLPFKQLESCIPMFLINHFKTCEMLRNYRIQNGIKIYSQKTRSQHKNIEDALNKISDLLNKSAETLYVPDTPPEKIARISILKKESNEKRLSEKKYKQKKKTQRRITMD
Protein: S-phase delaying protein 1 (Protein p14) (Q10585)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates the ribonucleotide reductase activity through its mediation of the nuclear localization of suc22, the small subunit of the ribonucleotide reductase. Delays the progression of the G1-S phase transition, thereby ensuring the G1 phase is complete. Interacts with both p34 and the p34-p56 complex, although no direct inhibitory effect on the bound proteins has been demonstrated. The action of p14 may happen coincidentally with the cdc10 function or may happen downstream of this.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- DNA damage-binding protein 1
- Cell division cycle protein cdt2
- Cullin-4
- Ribonucleoside-diphosphate reductase large chain
- COP9 signalosome complex subunit 1
- Protein kinase rad3
- Ribonucleoside-diphosphate reductase small chain
Sequence:
MHSSKRVMTTKTHVEQPESSMRPQLPESIQGSLMDVGMRVRKSISTGYKSKQTTFPAYNPPLYNTVSENIALKNTAFSYEPNGTKRPFEQAIPNYNWANPPQDFEEPEWLKPFDVVMEGTNERL
Protein: Ferritin (EC 1.16.3.2) (B5Z726)
Organism: Helicobacter pylori (strain G27)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361145}.
Interaction partners:
Sequence:
MLSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAKKLIVFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKSKDHATFNFLQWYVAEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIAKSRKS
Protein: Splicing regulator RBM11 (RNA-binding motif protein 11) (P57052)
Organism: Homo sapiens (Human)
Function: Tissue-specific splicing factor with potential implication in the regulation of alternative splicing during neuron and germ cell differentiation. Antagonizes SRSF1-mediated BCL-X splicing. May affect the choice of alternative 5' splice sites by binding to specific sequences in exons and antagonizing the SR protein SRSF1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:21984414}. Nucleus speckle {ECO:0000269|PubMed:21984414}. Note=Enriched in SRSF2-containing splicing speckles; shuttles between nucleoplasm and speckles.
Interaction partners:
- Zinc finger CCHC domain-containing protein 8
Sequence:
MFPAQEEADRTVFVGNLEARVREEILYELFLQAGPLTKVTICKDREGKPKSFGFVCFKHPESVSYAIALLNGIRLYGRPINVQYRFGSSRSSEPANQSFESCVKINSHNYRNEEMLVGRSSFPMQYFPINNTSLPQEYFLFQKMQWHVYNPVLQLPYYEMTAPLPNSASVSSSLNHVPDLEAGPSSYKWTHQQPSDSDLYQMTAPLPNSASVSSSLNHVPDLEAGPSSYKWTHQQPSDSDLYQMNKRKRQKQTSDSDSSTDNNRGNECSQKFRKSKKKKRY
Protein: Neuron navigator 2 (B2RWS4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNGSLGTKLLLCVSAGSANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQQQQQPEKQPLSSSPLPPAGSQVAGAPSQCQAGTPQHQGLATPQAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMSENVPAPLENSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKSKDLTKRVSVTDRPDLKEEPKVDLSGVAVTEMPKKSSKIASFIPKGGKLNSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLPPQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYR
Protein: Large ribosomal subunit protein mL51 (39S ribosomal protein L51, mitochondrial) (L51mt) (MRP-L51) (bMRP-64) (bMRP64) (Q4U2R6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL64
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL52
Sequence:
MAGNLLSGAGRRLWDWVPLACRSFSLGVPRLIGIRLTLPPPKVVDRWNEKRAMFGVYDNIGILGNFEKHPKELIRGPIWLRGWKGNELQRCIRKRKMVGSRMFADDLHNLNKRIRYLYKHFNRHGKFR
Protein: NUDIX hydrolase, conserved (Q381M2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRKQLFFTLARPCVAVGRRFISGDNKSIDSSAFISDDDALRGELASALDTEGHALPFDVHLQQPHSSGDGTAGDTSTIQLEKLSHPPARFDLLTNSFVYKWQTKAALARKVSGPMREWAAELKYRTGVHIELEPTYPERLSENAVKGSGSDEGDGTQWGAYETADDVDITVYLFGSERGIFNCHKLMEAAIQQDPVYVRLGIFRRLANSSEVEWLMLRRINRELRPPDIPPISLKLPGKWTLLYERYKEAAIRTLWEETGITVDASNVYPTGHLYQTVPQYYWRVPVRYFVAEVPSDIRVEGPQVVPLQYMRNWDARLLRQSPDPIDRAWAQLADPATGCAWMKASMIDQLQKPLRGDNYMAIRYTPPPYSNLQEVVGLGDGSITPSTGNGEDAS
Protein: Nucleotide/nucleic acid binding protein (F4JT92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Putative U3 small nucleolar ribonucleoprotein
- Periodic tryptophan protein 2
- rRNA processing protein-like protein
- Putative WD-repeat membrane protein
- Bystin
- DEAD-box ATP-dependent RNA helicase 32
- F18K10.11 protein
- DEAD-box ATP-dependent RNA helicase 16
- Pescadillo homolog
Sequence:
MSRICVKNLPKHVKEDQLRDHFSQKGEITDAKLMRSNDGKSRQFGFIGFRSAQEAQQAIKYFNNTYLGTSLIIVEIAHKVGDENAPRPWSRLSHKKEEEAKKSSSEGLKDGNAKGGKKRKAEVDDPEFQEFLEVHQRSKSKIWSNDMSIPPAPEETGKEKVLVKKADEQIVSNGVEPKKAKKSSDTEKTKKSKVVAASDDVSDMEYFKSRIKKNLSDSESDNESEDSSEDEAGDDDGKAETDGQDADIRYFPIDGDVEAGGVGKDDDGDAMEVEGDGKVAQESKAVSDDVLDTGRLFVRNLPYTATEEELMEHFSTFGKISEVHLVLDKETKRSRGIAYILYLIPECAARAMEELDNSSFQGRLLHILPAKHRETSDKQVNDTSNLPKTFKQKREEQRKASEAGGDTKAWNSLFMRPDTILENIVRVYGVSKSELLDREAEDPAVRLALGETKVIAETKEALAKAGVNVTSLEKFATRNGDEKNRSKHILLVKNLPFASTEKELAQMFGKFGSLDKIILPPTKTMALAVFLEPAEARAALKGMAYKRYKDAPLYLEWAPGNILEPKNLPDTNEERSDIEENGVRRVNLEQQVEIDPDVTESNVLNVKNLSFKTTDEGLKKHFTKLVKQGKILSVTIIKHKKNEKYLSSGYGFVEFDSVETATSVYRDLQGTVLDGHALILRFCENKRSDKVGKDSNKDKPCTKLHVKNIAFEATKRELRQLFSPFGQIKSMRLPKKNIGQYAGYAFVEFVTKQEALNAKKALASTHFYGRHLVLEWANDDNSMEAIRKRSAAKFDEENDNARKRKSSKAVEGKNEV
Protein: Secreted aspartic protease 3 (ACP 3) (Aspartate protease 3) (EC 3.4.23.24) (Candidapepsin-3) (P0CY29)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Induces host inflammatory cytokine production in a proteolytic activity-independent way. Plays a role in tissue damage during superficial infection. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0CY27}.
Interaction partners:
Sequence:
MFLKNIFIALAIALLADATPTTFNNSPGFVALNFDVIKTHKNVTGPQGEINTNVNVKRQTVPVKLINEQVSYASDITVGSNKQKLTVVIDTGSSDLWVPDSQVSCQAGQGQDPNFCKNEGTYSPSSSSSSQNLNSPFSIEYGDGTTSQGTWYKDTIGFGGISITKQQFADVTSTSVDQGILGIGYKTHEAEGNYDNVPVTLKNQGIISKNAYSLYLNSRQATSGQIIFGGVDNAKYSGTLIALPVTSDNELRIHLNTVKVAGQSINADVDVLLDSGTTITYLQQGVADQVISAFNGQETYDANGNLFYLVDCNLSGSVDFAFDKNAKISVPASEFTAPLYTEDGQVYDQCQLLFGTSDYNILGDNFLRSAYIVYDLDDNEISLAQVKYTTASNIAALT
Protein: Cd68 molecule (Q4FZY1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Endosome membrane {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004352, ECO:0000256|PROSITE-ProRule:PRU00740}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004352, ECO:0000256|PROSITE-ProRule:PRU00740}.
Interaction partners:
- Scavenger receptor cysteine-rich type 1 protein M130
- Allograft inflammatory factor 1
- T-cell surface glycoprotein CD4
- Glial fibrillary acidic protein
- Integrin alpha-D
- Interleukin-1 beta
- CX3C chemokine receptor 1
- Receptor-type tyrosine-protein phosphatase C
- Interleukin-6
- Tumor necrosis factor
Sequence:
MRFPVCLTLLVLLVAQGTGKDCPHKKAATLLPSFTETPTTTGSTASPTTTHRPTTTSHRPTTTSHRPTTTSHRPTTTSHRPTTTSHRPTTTSHGNATVSPTTNSPGFSTVGPHPGPPPPSPSPSPSSTGALGNYTWTNGSQPCVQLQAQIQIRILYLTQGGKKAWGLSVLNPNKTKVQGGCDSAHPHLALSFPYGQLTFGFKQDRHQSHSTVYLNYMAVEYNVSFPQAAQWTFSAQNSSLQELQAPLGQSFCCGNTSIVLSPAIHLDLLSLRLQAAQLPDKGHFGPCFSCASDQSLLLPLIIGLVLLGLLTLVLIAFCVTRRRQSTYQPL
Protein: Probable cytosol aminopeptidase (EC 3.4.11.1) (Leucine aminopeptidase) (LAP) (EC 3.4.11.10) (Leucyl aminopeptidase) (C4ZRD1)
Organism: Escherichia coli (strain K12 / MC4100 / BW2952)
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
Interaction partners:
Sequence:
MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE