wanglab/gogpt-training-data huggingface dataset:
Protein: Caveolin-1 (Q94051)
Organism: Caenorhabditis elegans
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-2
- Tyrosine protein-kinase src-1
- C-type lectin domain-containing protein
- Actin
- Transthyretin-like family protein
- Voltage-dependent L-type calcium channel subunit alpha
- Dynamin
- Ras-like GTP-binding protein rhoA
- Receptor tyrosine-protein kinase let-23
- Voltage-dependent T-type calcium channel subunit alpha
Sequence:
MSTEQDIKTEEQIPLTYAAVAAPTVQTEGEAVVAPEEPKPKKNWFTFGKKKAAPTDETNIEEGGAPGDEPVKEKKEKKCWWSRCQKGEGEQKEENIAIGVDLVNRDANSMNNHVQLNFEDIFGEADSQHSWDCVWRLNHTVFTAVRLFIYRLVSLLALPFTIIFAIFFGLLASINVFIIVPLGKLLSIPGTLLAKLWNWLIHAIFDPIASAVGLIFSNFNIRKYGINQETTAPCV
Protein: Calcium sensing receptor, chloroplastic (Sulfurtransferase 3) (AtStr3) (Q9FN48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Modulates cytoplasmic Ca(2+) concentration and is crucial for proper stomatal regulation in response to elevated levels of external Ca(2+). May function by regulating concentrations of inositol 1,4,5-trisphosphate (IP3), which in turn triggers release of Ca(2+) from internal stores. May play a role in de-etiolation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18331354, ECO:0000269|PubMed:18507772}; Single-pass membrane protein {ECO:0000269|PubMed:18331354, ECO:0000269|PubMed:18507772}; Stromal side {ECO:0000269|PubMed:18331354, ECO:0000269|PubMed:18507772}.
Interaction partners:
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha-2
- AP-2 complex subunit alpha-1
- Uncharacterized protein At1g03900
- Adaptin ear-binding coat-associated protein 1 NECAP-1
- Beta-adaptin-like protein B
- Beta-adaptin-like protein A
- 50S ribosomal protein L27
- Beta-adaptin-like protein C
- At5g57460
Sequence:
MAMAEMATKSSLSAKLTLPSSSTKKTLSLRQVSVSLPTSTSISLLSLFASPPHEAKAAVSIPKDQIVSSLTEVEKTINQVQETGSSVFDATQRVFQVVGDALKPALDTALPIAKQAGEEAMKLASPAFSEASKKAQEAMQSSGFDSEPVFNAAKTVTDVAQQTSKAIEDAKPIASSTMDTISSADPSVIVVAAGAAFLAYLLLPPVFSAISFNFRGYKGDLTPAQTLDLLCTKNYLMVDIRSEKDKEKAGIPRLPSNAKNRVISIPLEELPNKVKGIVRNSKRVEAEIAALKISYLKKINKGSNIIILDSYTDSAKIVAKTLKVLGYKNCYIVTDGFSGGRGWLQSRLGTDSYNFSFAQVLSPSRIIPAASRSFGTRSGTKFLPSSD
Protein: Rho GDP-dissociation inhibitor 1 (Rho GDI 1) (Rho-GDI alpha) (Q5XI73)
Organism: Rattus norvegicus (Rat)
Function: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19343716}.
Interaction partners:
- Transforming protein RhoA
- Cell division control protein 42 homolog
- Tumor necrosis factor receptor superfamily member 16
- small monomeric GTPase
- RSA-14-44 protein.
- Rho-related GTP-binding protein RhoG
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Ras homolog family member C.
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVIVTRLTLVCSTAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPMEEAPKGMLARGSYNIKSRFTDDDKTDHLSWEWNLTIKKEWKD
Protein: Nuclear factor I B (A0A1B0GWB8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLTFLWQRDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLGITWQSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN
Protein: Protein OS-9 homolog (AtOS9) (Protein EMS-MUTAGENIZED BRI1 SUPPRESSOR 6) (Q8GWH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Targets the misfolded LRR receptor kinase BRI1 and the misfolded receptor-like kinase EFR.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:22328055, ECO:0000269|PubMed:22516478}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase component HRD3A
- Derlin-1
- Derlin-2.1
- ERAD-associated E3 ubiquitin-protein ligase component HRD3B
- ERAD-associated E3 ubiquitin-protein ligase HRD1A
- Derlin-2.2
- ERAD-associated E3 ubiquitin-protein ligase HRD1B
- Cell division control protein 48 homolog A
- F-box protein At1g70590
- At2g25570
Sequence:
MRITQILLCLVIVALSSSSHVWSDQIFPAHLVGTFSRNNREPKYKIEFLPEDSPFHPGDNLESMVMLDKHGNRFLCYLPKEEKATSGWTSSQQNISTVMMETQQLVKLKTPDELLQPLSEKCLFRQEGWWSYEFCHQKYVRQLHVEDENKIVQEFFLGTFDPEATAAFNQTVSDASTDASQRYHSHVYTNGTTCDLTGSPREVEVRFVCAETRAMVTSITELSTCKYALTVQCPTLCKHPLFQLEKPVSHTIHCNAIPVEEDATRNKEEQAVDESPKMIADS
Protein: Protein mono-ADP-ribosyltransferase PARP10 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 10) (ARTD10) (Poly [ADP-ribose] polymerase 10) (PARP-10) (Q53GL7)
Organism: Homo sapiens (Human)
Function: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate and aspartate residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively regulate GSK3B kinase activity. Involved in translesion DNA synthesis in response to DNA damage via its interaction with PCNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15674325}. Cytoplasm {ECO:0000269|PubMed:15674325}. Note=Shuttles between the nuclear and cytoplasmic compartment (PubMed:15674325). A subpopulation concentrates in the nucleolus during late G1/S phase (PubMed:15674325). {ECO:0000269|PubMed:15674325}.
Interaction partners:
- Myc proto-oncogene protein
- Plectin
- Protein mono-ADP-ribosyltransferase PARP14
- Protein mono-ADP-ribosyltransferase PARP16
- Protein mono-ADP-ribosyltransferase PARP3
- Poly [ADP-ribose] polymerase 2
- Poly [ADP-ribose] polymerase 1
- ADP-ribose glycohydrolase MACROD2
- tRNA 2'-phosphotransferase 1
- Protein mono-ADP-ribosyltransferase PARP6
Sequence:
MVAMAEAEAGVAVEVRGLPPAVPDELLTLYFENRRRSGGGPVLSWQRLGCGGVLTFREPADAERVLAQADHELHGAQLSLRPAPPRAPARLLLQGLPPGTTPQRLEQHVQALLRASGLPVQPCCALASPRPDRALVQLPKPLSEADVRVLEEQAQNLGLEGTLVSLARVPQARAVRVVGDGASVDLLLLELYLENERRSGGGPLEDLQRLPGPLGTVASFQQWQVAERVLQQEHRLQGSELSLVPHYDILEPEELAENTSGGDHPSTQGPRATKHALLRTGGLVTALQGAGTVTMGSGEEPGQSGASLRTGPMVQGRGIMTTGSGQEPGQSGTSLRTGPMGSLGQAEQVSSMPMGSLEHEGLVSLRPVGLQEQEGPMSLGPVGSAGPVETSKGLLGQEGLVEIAMDSPEQEGLVGPMEITMGSLEKAGPVSPGCVKLAGQEGLVEMVLLMEPGAMRFLQLYHEDLLAGLGDVALLPLEGPDMTGFRLCGAQASCQAAEEFLRSLLGSISCHVLCLEHPGSARFLLGPEGQHLLQGLEAQFQCVFGTERLATATLDTGLEEVDPTEALPVLPGNAHTLWTPDSTGGDQEDVSLEEVRELLATLEGLDLDGEDWLPRELEEEGPQEQPEEEVTPGHEEEEPVAPSTVAPRWLEEEAALQLALHRSLEPQGQVAEQEEAAALRQALTLSLLEQPPLEAEEPPDGGTDGKAQLVVHSAFEQDVEELDRALRAALEVHVQEETVGPWRRTLPAELRARLERCHGVSVALRGDCTILRGFGAHPARAARHLVALLAGPWDQSLAFPLAASGPTLAGQTLKGPWNNLERLAENTGEFQEVVRAFYDTLDAARSSIRVVRVERVSHPLLQQQYELYRERLLQRCERRPVEQVLYHGTTAPAVPDICAHGFNRSFCGRNATVYGKGVYFARRASLSVQDRYSPPNADGHKAVFVARVLTGDYGQGRRGLRAPPLRGPGHVLLRYDSAVDCICQPSIFVIFHDTQALPTHLITCEHVPRASPDDPSGLPGRSPDT
Protein: Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) (P9WPW7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}.
Interaction partners:
- Argininosuccinate lyase
- Acetylglutamate kinase
- Ornithine carbamoyltransferase
- Acetylornithine aminotransferase
- Arginine repressor
- N-acetyl-gamma-glutamyl-phosphate reductase
- Carbamoyl phosphate synthase large chain
- Arginine biosynthesis bifunctional protein ArgJ
- Adenylosuccinate synthetase
- Putative asparagine synthetase
Sequence:
MSERVILAYSGGLDTSVAISWIGKETGREVVAVAIDLGQGGEHMDVIRQRALDCGAVEAVVVDARDEFAEGYCLPTVLNNALYMDRYPLVSAISRPLIVKHLVAAAREHGGGIVAHGCTGKGNDQVRFEVGFASLAPDLEVLAPVRDYAWTREKAIAFAEENAIPINVTKRSPFSIDQNVWGRAVETGFLEHLWNAPTKDIYAYTEDPTINWGVPDEVIVGFERGVPVSVDGKPVSMLAAIEELNRRAGAQGVGRLDVVEDRLVGIKSREIYEAPGAMVLITAHTELEHVTLERELGRFKRQTDQRWAELVYDGLWYSPLKAALEAFVAKTQEHVSGEVRLVLHGGHIAVNGRRSAESLYDFNLATYDEGDSFDQSAARGFVYVHGLSSKLAARRDLR
Protein: SAGA complex subunit spt3 (O14311)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (spt3, spt8 and spt20) and promoter selectivity, interaction with transcription activators (gcn5, ada2, ada3 and tra1), and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). Spt3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, spt3 and spt8 prevent binding of TBP to the TATA box (By similarity). SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. Spt3 regulates Ty1 as well as the mating factor genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:9559549}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex subunit Hfi1
- SAGA complex subunit Spt7
- SAGA complex subunit Ada2
- SAGA complex subunit Sgf73
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Ngg1
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf6
Sequence:
MTETGRTSKYRVEIQQMMFILGEVQDPLPETTQLVEELIRGQVMEMLIQANELALRRGSRSITVEDLFFLIRHDRAKVNRLKTYLSWKEVRKKAKEQDANPADTKDLFEEVDSKTRSMNAVAMPWEVKNMFTEPVPETEEFEEDNDTMEMAYATRQRLKMADERTKKMTREEYVHWSECRQASFTYRKGKRFREWCGMSILTDTRPDNDIVDILGFLTFEIVATLTEEALAVKDRMDRIQNSSGSGGSHAAHHPKNCSLFDGLTEGRTPLQVSHVLEAFRRLQIPDKTHTAMRSFHGGLVKSRVYLI
Protein: Probable 26S proteasome regulatory subunit rpn7 (Q10335)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn2
- 26S proteasome regulatory subunit rpn1
- Probable 26S proteasome regulatory subunit rpn9
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit 6B homolog
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit rpn12
Sequence:
MCSPSATLTHRTMTEKARTVSDLTISQAIFELSSPFLENKSQKALDTLFSAIRDHDLAPLYKYLSENPKTSASIDFDSNFLNSMIKKNEEKLAEFDKAIEDAQELNGEHEILEAMKNKADYYTNICDRERGVQLCDETFERATLTGMKIDVLFSKIRLAYVYADMRVVGQLLEKLKPLIEKGGDWERKNRLKAYQGIYLMSIRNFSGAADLLLDCMSTFSSTELLPYYDVVRYAVISGAISLDRVDVKTKIVDSPEVLAVLPQNESMSSLEACINSLYLCDYSGFFRTLADVEVNHLKCDQFLVAHYRYYVREMRRRAYAQLLESYRALSIDSMAASFGVSVDYIDRDLASFIPDNKLNCVIDRVNGVVFTNRPDEKNRQYQEVVKQGDVLLNKLQKYQATVMRGAFKV
Protein: Uncharacterized protein orf161 (Q2F978)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MLYGRMLRRIIRTMRFYFYGFHFGEGSNLRLLKRFMSHGKSLGLSYLSAAFGLPLHSTSDTGEDVRLIHLLNFRGEKRLPVHELLQSIENPYRLSISVIDGCRSGVLRTRGTCMQTGEEEENLECRLLRHNQGPLAQIETLNPRCDVHLFHFIISWKKRIN
Protein: 1,4-beta-D-glucan cellobiohydrolase C (EC 3.2.1.91) (Beta-glucancellobiohydrolase C) (Exocellobiohydrolase C) (Exoglucanase C) (Q5B2E8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Active against carboxymethylcellulose, beta-glucan and lichenan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- 1,4-beta-D-glucan cellobiohydrolase B
- Endo-beta-1,4-glucanase A
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Endo-beta-1,4-glucanase B
- Endo-beta-1,4-glucanase celB
- Extracellular endoglucanase, putative
- Glucanase
- beta-glucosidase
- Probable beta-glucosidase A
- Beta-glucosidase B
Sequence:
MHYSASGLALAFLLPAIQAQQTLYGQCGGSGWTGATSCVAGAACSTLNQWYAQCLPAATTTSTTLTTTTSSVTTTSNPGSTTTTSSVTVTATASGNPFSGYQLYVNPYYSSEVQSIAIPSLTGTLSSLAPAATAAAKVPSFVWLDVAAKVPTMATYLADIRSQNAAGANPPIAGQFVVYDLPDRDCAALASNGEFAISDGGVQHYKDYIDSIREILVEYSDVHVILVIEPDSLANLVTNLNVAKCANAQSAYLECTNYAVTQLNLPNVAMYLDAGHAGWLGWPANLQPAANLYAGVYSDAGSPAALRGLATNVANYNAWAIDTCPSYTQGNSVCDEKDYINALAPLLRAQGFDAHFITDTGRNGKQPTGQQAWGDWCNVIGTGFGARPSTNTGDSLLDAFVWVKPGGESDGTSDTSAARYDAHCGYSDALQPAPEAGTWFQAYFVQLLQNANPSF
Protein: Serine/arginine-rich splicing factor 1 (Splicing factor, arginine/serine-rich 1) (A0A8I6GMR8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSHISEEMD
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (D3ZP96)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell division cycle 45
- Cell division control protein
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA helicase
- DNA replication licensing factor MCM6
- Cell division cycle 7-related protein kinase
- DNA replication complex GINS protein SLD5
- DNA replication complex GINS protein PSF2
Sequence:
MAESSESFSAASSPAPQRRRISDPLTSSPGRSSRRADALTSSPGRDLPPFEDESEGLLGTEGPVEEEEDGEELIGDGMERDYRPIPELDVYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRHIERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCSKCNFILGPFCQSQNQEVKPGSCPECQSTGPFEINMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTTNGFPVFATIILANHVAKKDNKVAVGELTDEDVKMITSLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDVLCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKKDEGLTNGGTTEPAMPNTYGVEPLPQEVLKKYIIYAKERVRPKLNQMDQDKVARMYSDLRKESMATGSIPITVRHIESMIRMAEAHARMHLRDYVMEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLSFRRDNNDLLLFILKQLVAEQVTYQRNRFGAQQDTIEIPEKDLMDKARQINIHNLSAFYDSDLFKINKFSRDLKRKLILQQF
Protein: T-cell leukemia homeobox protein 1 (Homeobox TLX-1) (Homeobox protein Hox-11) (P43345)
Organism: Mus musculus (Mouse)
Function: Controls the genesis of the spleen. Binds to the DNA sequence 5'-GGCGGTAAGTGG-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein phosphatase EYA1
- Paired box protein Pax-2
- Rhombotin-1
- Protein lyl-1
- T-cell acute lymphocytic leukemia protein 1 homolog
- Rhombotin-2
Sequence:
MEHLGPHHLHPGHAEPISFGIEQILNSPDQGGCMGPNSRLQDGDYGLGCLVPGAYTYGGGGSAAGAGAGGTGAYGAGGPGGPGGPAGGGGGACSMGPLPGSYNVNMDLAGGPGPGGDGGGGGAARRALSAAGVIRVPAHRPLAGAVAHPQPLATGLPTVPSVPAVPGVNNLTGLTFPWMESNRRYTKDRFTGLPYQNRTPPKKKKPRTSFTRLQICELEKRFHRQKYLASAERAALAKALKMTDAQVKTWFQNRRTKWRRQTAEEREAESEQANRILLQLQQEAFQKSLAQPLPADPLCVHNSSLFALQNLQPWSDDSTKITSVTSVASACE
Protein: Probable histidine kinase 4 (OsHK4) (EC 2.7.13.3) (OsCRL1b) (A1A698)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Histidine-containing phosphotransfer protein 2
- Probable histidine kinase 3
- Probable histidine kinase 5
- Pseudo histidine-containing phosphotransfer protein 5
- Pseudo histidine-containing phosphotransfer protein 2
- Histidine-containing phosphotransfer protein 1
- Probable kinase CHARK
- Pseudo histidine-containing phosphotransfer protein 1
- Os02g0197050 protein
- Os12g0218701 protein
Sequence:
MGVGGGGGGGGGEAAAAVAVEGDEAGKGRRWWRVKVKLSTVAVVAWVLASAALWAGLHWRFRRAALHKAEEALVCMCEERARMLQDQFAVSVNHVHALAILVATFHYDKHPPALDQDTFAVYAARTSFERPLLSGVAYAQRVVHADRESFERQQGWIIKTMKHEPSPAQDEYAPVIYSQETISYIEGLDVMSGEEDRENILRARATGKAVLTRPFRLMSNHLGVVLTFPVYLVDLPNDTAVEDRVAATAGYLGGAFDVESLVENLLRQLAGNQELVVNVYDVTNHSNPLVMYGSEVPLGIPSPSHTYTLDFGDPLRKHQMVCRYRNKLHVSWSAITTPSGVFVICMLVGYIIYAAWSRYDNVKEDCRKMEALKKRAEAADIAKSQFLATVSHEIRTPMNGVLGMLDMLLDTELKSTQRDYAQTAQVCGKALISLINEVLDRAKIEAGKIDLESVPFDLRSILDDVISLFSSKSREKGIELAVYVSERVPEILLGDPGRFRQIITNLVGNSIKFTERGHIFVQVHLADHSNLATEAKIEPVVNGMNGHKDEAIAIPTSGSHNTLSGFEAADSRNNWENFKLLLSYEKNEMPYESDSDKVTLVVSVEDTGIGIPLHAQGRVFTPFMQADSSTSRNYGGTGIGLSISKCLVEIMGGQINFVSRPLVGSTFTFTAVLRRCDKNAISDSKTVALHPLPSSFKGLSALLVDKRPVRATVTKYHLQRLGITSEVVGTIDPTFGVLSGRNGSSLTSIGKKQPCMLLIESDSWGPQMDVSLHARLQEMKQSDRIHVLPKVFLLSAAESDKVKKIHAVDSVIPKPLKASALAACLFQALGITQPSHEKRDDSGSLHGRDGSGSLHGLLLGKNILVVDDNKVNLRVAAGTLKKYGAKVECVESGKDALSLLQVPHKFDLCLMDIQMPEMDGFEATRQIRAMEGKANEQADDSESGSEIAAKTAKWHLPILAMTADVIQATHEECTKCGMDGYVSKPFEEKQLFQAVQKFLGPCVSS
Protein: Mitochondrial import receptor subunit TOM7 homolog (Translocase of outer membrane 7 kDa subunit homolog) (Q9D173)
Organism: Mus musculus (Mouse)
Function: Required for assembly and stability of the TOM complex (By similarity). Positive regulator of PRKN translocation to damaged mitochondria. Acts probably by stabilizing PINK1 on the outer membrane of depolarized mitochondria (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9P0U1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9P0U1}.
Interaction partners:
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM40 homolog
- Serine/threonine-protein kinase PINK1, mitochondrial
- Mitochondrial import receptor subunit TOM40B
- Sorting and assembly machinery component 50 homolog
- Metaxin-1
Sequence:
MVKLSKEAKQRLQQLFKGGQFAIRWGFIPLVIYLGFTRGADPGMPEPSVLSLLWG
Protein: Type 3 secretion system secretin (T3SS secretin) (B7UMB3)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442, ECO:0000256|HAMAP-Rule:MF_02219, ECO:0000256|RuleBase:RU004004}.
Interaction partners:
Sequence:
MKKISFFIFTALFCCSAQAAPSSLEKRLGKNEYFIITKSSPVRAILNDFAANYSIPVFISSSVNDDFSGEIKNEKPVKVLEKLSKLYHLTWYYDENILYIYKTNEISRSIITPTYLDIDSLLKYLSDTISVNKNSCNVRKITTFNSIEVRGVPECIKYITSLSESLDKEAQSKAKNKDVVKVFKLNYASATDITYKYRDQNVVVPGVVSILKTMASNGSLPSTGKGAVERSGNLFDNSVTISADPRLNAVVVKDREITMDIYQQLISELDIEQRQIEISVSIIDVDANDLQQLGVNWSGTLNAGQGTIAFNSSTAQANISSSVISNASNFMIRVNALQQNSKAKILSQPSIITLNNMQAILDKNVTFYTKVSGEKVASLESITSGTLLRVTPRILDDSSNSLTGKRRERVRLLLDIQDGNQSTNQSNAQDASSTLPEVQNSEMTTEATLSAGESLLLGGFIQDKESSSKDGIPLLSDIPVIGSLFSSTVKQKHSVVRLFLIKATPIKSASSE
Protein: Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase) (O06769)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids.
Interaction partners:
- Dye-decolorizing peroxidase
- N-acetylglucosamine-6-phosphate deacetylase
Sequence:
MLSVGRGIADITGEAADCGMLGYGKSDQRTAGIHQRLRSRAFVFRDDSQDGDARLLLIVAELPLPMQNVNEEVLRRLADLYGDTYSEQNTLITATHTHAGPGGYCGYLLYNLTTSGFRPATFAAIVDGIVESVEHAHADVAPAEVSLSHGELYGASINRSPSAFDRNPPADKAFFPKRVDPHTTLVRIDRGEATVGVIHFFATHGTSMTNRNHLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPNVDGPLSPEAPPDREFDNTRRTGLCQFEDAFTQLSGATPIGAGIDARFTYVDLGSVLVRGEYTPDGEERRTGRPMFGAGAMAGTDEGPGFHGFRQGRNPFWDRLSRAMYRLARPTAAAQAPKGIVMPARLPNRIHPFVQEIVPVQLVRIGRLYLIGIPGEPTIVAGLRLRRMVASIVGADLADVLCVGYTNAYIHYVTTPEEYLEQRYEGGSTLFGRWELCALMQTVAELAEAMRDGRPVTLGRRPRPTRELSWVRGAPADAGSFGAVIAEPSATYRPGQAVEAVFVSALPNNDLRRGGTYLEVVRREGASWVRIADDGDWATSFRWQRQGRAGSHVSIRWDVPGDTTPGQYRIVHHGTARDRNGMLTAFSATTREFTVV