wanglab/gogpt-training-data huggingface dataset:
Protein: Disabled homolog 1 (Q8CJH2)
Organism: Rattus norvegicus (Rat)
Function: Adapter molecule functioning in neural development. May regulate SIAH1 activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P97318}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 8
- Very low-density lipoprotein receptor
- Reelin
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Amyloid-beta precursor protein
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Tyrosine-protein kinase Fyn
- SH3 domain-containing kinase-binding protein 1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Sequence:
MSTETELQVAVKTSAKKDSRKKGQDRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIRDPETEENIYQVPTSQKKEGVYDVPKSQPVSAVTQLELFGDMSTPPDITSPPTPATPGDAFLPAPSQTLPGSADVFGSMSFGTAAVPSGYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAQVIPGAQPIAWGQPGLFPATQQPWPTVAGQFPPAAFMPTQTVMPLPAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMGKEMFKDFQMAQPPPVPSRKPDQPSLTCTSEAFSSYFNKVGVAQDTDDCDDFDISQLNLTPVTSTTPSTNSPPTPAPRQSSPSKSSASHVSDPTADDIFEEGFESPSKSEEQEAPDGSQASSTSDPFGEPSGEPSGDNISPQDGS
Protein: Methyltransferase domain-containing protein (Q9HWK3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
Sequence:
MSATALYTDLSHYYDLMCADIDYQAQSHCVRRLHQLFGNQGRRHLDLACGTGPHVRHFLDFGYRSAGLDINQPMLDLARQRCPEAHFSRQDMAGFQVDEPLDLITCFLYSIHYNAGLERLRACLASVHGALADGGVFCFNTVDKGQIDNRSFVRHSVEHRGSRFTFGSGWYYSGEGERQALRLGIEKTTDGTTQTWEDEHPMVALGFAELQHLLQTHFEVQVFEHDYERITPWAGSSGNALFVCVKR
Protein: N-acetylneuraminate lyase (NALase) (EC 4.1.3.3) (N-acetylneuraminate pyruvate-lyase) (N-acetylneuraminic acid aldolase) (Sialate lyase) (Sialate-pyruvate lyase) (Sialic acid aldolase) (Sialic acid lyase) (Q9BXD5)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (Probable).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- N-acetylneuraminate-9-phosphate synthase
- N-acylglucosamine 2-epimerase
Sequence:
MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLLDFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS
Protein: 2-amino-5-chloromuconate deaminase (2A5CM deaminase) (2-aminomuconate deaminase (2-hydroxymuconate-forming)) (EC 3.5.99.11) (Q09KQ6)
Organism: Comamonas testosteroni (Pseudomonas testosteroni)
Function: Involved in the biodegradation of xenobiotic compounds, such as nitrobenzene and 4-chloronitrobenzene (4-CNB). CnbZ preferentially catalyzes the deamination of 2-amino-5-chloromuconate (2A5CM) to yield 2-hydroxy-5-chloromuconate (2H5CM). Also able to catalyze the deamination of 2-aminomuconate to yield 2-hydroxymuconate, which spontaneously converts into its keto form, 2-oxalocrotonate.
Interaction partners:
Sequence:
MPDAVVFSPGGYRYIPAVFQYSAGIAAEPGFEIERVRFHRPVPLAEAFVAVESHLRAIGRPTTSFAQCELRSPDPFNDQGFIDFNTEYVKTLERWGIYKDRVNPVARTNVCPMYDKPTTPSMFAFSYTVPTTSAAKRPSFQLAGGGDARGGSAPYKDRIVAFGDTSPEGLREKVVFVIEEMESRLKTLGLGWADAVSTQLYTVQNIGHLVGPELARRGCGAGGLVWNYTRPPVIGLEYEMDVRGAVRETVL
Protein: ATP synthase peripheral stalk subunit OSCP, mitochondrial (ATP synthase subunit O) (Oligomycin sensitivity conferral protein) (OSCP) (P48047)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MAAPAVSGLSRQVRCFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEKELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPSILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV
Protein: Methoxy mycolic acid synthase MmaA3 (EC 2.1.1.-) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (P0CH91)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of methoxymycolic acid. It catalyzes the O-methylation of the hydroxy group of the hydroxymycolate to form a methyl ether.
Interaction partners:
- Hydroxymycolate synthase MmaA4
Sequence:
MSDNSTGTTKSRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLLHSITGLHVKQVIERGIPLTMEMAKFIRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEALQAHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQFTLAK
Protein: Rho-related BTB domain-containing protein 3 (EC 3.6.1.-) (O94955)
Organism: Homo sapiens (Human)
Function: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:19490898}.
Interaction partners:
- Perilipin-3
- Cullin-3
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Ras-related protein Rab-9A
- Ras-related protein Rab-9B
- GRIP and coiled-coil domain-containing protein 2
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MSIHIVALGNEGDTFHQDNRPSGLIRTYLGRSPLVSGDESSLLLNAASTVARPVFTEYQASAFGNVKLVVHDCPVWDIFDSDWYTSRNLIGGADIIVIKYNVNDKFSFHEVKDNYIPVIKRALNSVPVIIAAVGTRQNEELPCTCPLCTSDRGSCVSTTEGIQLAKELGATYLELHSLDDFYIGKYFGGVLEYFMIQALNQKTSEKMKKRKMSNSFHGIRPPQLEQPEKMPVLKAEASHYNSDLNNLLFCCQCVDVVFYNPNLKKVVEAHKIVLCAVSHVFMLLFNVKSPTDIQDSSIIRTTQDLFAINRDTAFPGASHESSGNPPLRVIVKDALFCSCLSDILRFIYSGAFQWEELEEDIRKKLKDSGDVSNVIEKVKCILKTPGKINCLRNCKTYQARKPLWFYNTSLKFFLNKPMLADVVFEIQGTTVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQSMPSRELASMNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRCLVM
Protein: SET domain containing 5 (H0Y3R4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVEMCVDARTFGNDARFIRRSCTPNAEVRHMIADGMIHLCIYAVSAITKDAEVTIAFDYEYSNCNYKVDCACHKGNRNCPIQKRNPNATELPLLPPPPSLPTIGAETRRRKARRKELEMEQQNEASEENNDQQSQEVPEKVTVSSDHEEVDNPEEKPEEEKEEVIDDQENLAHSRRTREDRKVEAIMHAFENLEKRKKRRDQPLEQSNSDVEITTTTSETPVGEETKTEAPESEVSNSVSNVTIPSTPQSVGVNTRRSSQAGDIAAEKLVPKPPPAKPSRPRPKSRISRYRTSSAQRLKRQKQANAQQAELSQAALEEGGSNSLVTPTEAGSLDSSGENRPLTGSDPTVVSITGSHVNRAASKYPKTKKYLVTEWLNDKAEKQECPVECPLRITTDPTVLATTLNMLPGLIHSPLICTTPKHYIRFGSPFIPERRRRPLLPDGTFSSCKKRWIKQALEEGMTQTSSVPQETRTQHLYQSNENSSSSSICKDNADLLSPLKKWKSRYLMEQNVTKLLRPLSPVTPPPPNSGSKSPQLATPGSSHPGEEECRNGYSLMFSPVTSLTTASRCNTPLQFELCHRKDLDLAKVGYLDSNTNSCADRPSLLNSGHSDLAPHPSLGPTSETGFPSRSGDGHQTLVRNSDQAFRTEFNLMYAYSPLNAMPRADGLYRGSPLVGDRKPLHLDGGYCSPAEGFSSRYEHGLMKDLSRGSLSPGGERACEGVPSAPQNPPQRKKVSLLEYRKRKQEAKENSAGGGGDSAQSKSKSAGAGQGSSNSVSDTGAHGVQGSSARTPSSPHKKFSPSHSSMSHLEAVSPSDSRGTSSSHCRPQENISSRWMVPTSVERLREGGSIPKVLRSSVRVAQKGEPSPTWESNITEKDSDPADGEGPETLSSALSKGATVYSPSRYSYQICD
Protein: Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (P0AC13)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
Interaction partners:
- Dihydrofolate synthase/folylpolyglutamate synthase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Dihydroneopterin aldolase
- GTP cyclohydrolase 1
- Phosphoglucosamine mutase
- Aminodeoxychorismate lyase
- Dihydrofolate reductase
- Dihydromonapterin reductase
- Dihydroneopterin triphosphate 2'-epimerase
- Aminodeoxychorismate synthase component 2
Sequence:
MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE
Protein: (6-4) photolyase (EC 4.1.99.13) ((6-4)DNA photolyase) (DNA photolyase PhrB) (Photoreactivating enzyme PhrB) (A9CH39)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Photolyase involved in the repair of UV-induced (6-4) lesions in DNA. Catalyzes the photoreactivation of (6-4) pyrimidine-pyrimidone photoproducts by using blue-light energy. Can repair (6-4) photoproducts in ssDNA as well as in dsDNA.
Interaction partners:
- Deoxyribodipyrimidine photo-lyase
Sequence:
MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWLAGPDYVDSNFFENDRSLPVFYWTGKTHMNCMAKVITETIENAYAHHIQRLMITGNFALLAGIDPKAVHRWYLEVYADAYEWVELPNVIGMSQFADGGFLGTKPYAASGNYINRMSDYCDTCRYDPKERLGDNACPFNALYWDFLARNREKLKSNHRLAQPYATWARMSEDVRHDLRAKAAAFLRKLD
Protein: EG:BACR25B3.11 protein (Q9NEG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MACNCNQSMIYQSNERRDYNCPGAPQYPYNRFKGGVSLKDTPCMVLYICADFKSSKLSSAKPIISGPATTRAPAISYVCQPNDFKCVSHPHTCVRANMVCDGIYDCTDHSDEFNCIAGKGSGKSESNSGSGSFKRWKKSPEQGRRSLAKAVKNRKLRKRSFAKSRDYSLKLDDQSSNLRAGESTDVECYSSDDTYTDVVWERSDGAPLSNNVRQVGNRLVISNVSPSDAGNYVCKCKTDEGDLYTTSYKLEVEDQPHELKSSKIVYAKVGANADLQCGADESRQPTYRWSRQYGQLQAGRSLMNEKLSLDSVQANDAGTYICTAQYADGETADFPNILVVTGAIPQFRQEPRSYMSFPTLPNSSFKFNFELTFRPENGDGLLLFNGQTRGSGDYIALSLKDRYAEFRFDFGGKPMLVRAEEPLALNEWHTVRVSRFKRDGYIQVDEQHPVAFPTLQQIPQLDLIEDLYIGGVPNWELLPADAVSQQVGFVGCISRLTLQGRTVELIREAKYKEGITDCRPCAQGPCQNKGVCLESQTEQAYTCICQPGWTGRDCAIEGTQCTPGVCGAGRCENTENDMECLCPLNRSGDRCQYNEILNEHSLNFKGNSFAAYGTPKVTKVNITLSVRPASLEDSVILYTAESTLPSGDYLALVLRGGHAELLINTAARLDPVVVRSAEPLPLNRWTRIEIRRRLGEGILRVGDGPERKAKAPGSDRILSLKTHLYVGGYDRSTVKVNRDVNITKGFDGCISRLYNFQKPVNLLADIKDAANIQSCGETNMIGGDEDSDNEPPVPPPTPDVHENELQPYAMAPCASDPCENGGSCSEQEDVAVCSCPFGFSGKHCQEHLQLGFNASFRGDGYVELNRSHFQPALEQSYTSMGIVFTTNKPNGLLFWWGQEAGEEYTGQDFIAAAVVDGYVEYSMRLDGEEAVIRNSDIRVDNGERHIVIAKRDENTAILEVDRMLHSGETRPTSKKSMKLPGNVFVGGAPDLEVFTGFRYKHNLNGCIVVVEGETVGQINLSSAAVNGVNANVCPA
Protein: Fructose-bisphosphate aldolase B (EC 4.1.2.13) (Aldolase 2) (Liver-type aldolase) (Q91Y97)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P05062}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:P05062}.
Interaction partners:
- Fructose-1,6-bisphosphatase 1
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, muscle type
- ATP-dependent 6-phosphofructokinase, platelet type
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase isozyme 2
- Triokinase/FMN cyclase)
- Glyceraldehyde-3-phosphate dehydrogenase
- Pyruvate kinase PKLR
- Transaldolase
Sequence:
MAHRFPALTPEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAMANCQAAQGQYVHTGSSGAAATQSLFTASYTY
Protein: Homeotic protein distal-less (Protein brista) (P20009)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor that plays a role in larval and adult appendage development. Specifies the identity of ventral appendages (including legs and antennae) and suppresses dorsal appendage development. Involved in patterning the distal-proximal limb axis. May control the adhesive properties of cells during limb morphogenesis. Also has a secondary role in the normal patterning of the wing margin.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:1358457}.
Interaction partners:
- Homeobox protein extradenticle
- Homeobox protein homothorax
- Protein decapentaplegic
- Protein wingless
- Protein serrate
- Neurogenic locus Notch protein
- Zinc finger protein sens
- FI23031p1
- Protein Optix
- Achaete-scute complex protein T5
Sequence:
MDAPDAPHTPKYMDGGNTAASVTPGINIPGKSAFVELQQHAAAGYGGIRSTYQHFGPQGGQDSGFPSPRSALGYPFPPMHQNSYSGYHLGSYAPPCASPPKDDFSISDKCEDSGLRVNGKGKKMRKPRTIYSSLQLQQLNRRFQRTQYLALPERAELAASLGLTQTQVKIWFQNRRSKYKKMMKAAQGPGTNSGMPLGGGGPNPGQHSPNQMHSGGNNGGGSNSGSPSHYLPPGHSPTPSSTPVSELSPEFPPTGLSPPTQAPWDQKPHWIDHKPPPQMTPQPPHPAATLHPQTHHHNPPPQMGGYVPQYWYQPETNPSLVTVWPAV
Protein: Pre-mRNA-splicing factor SAD1 (snRNP assembly-defective protein 1) (P43589)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Promotes the assembly of newly synthesized U4 snRNA into the U4/U6 snRNP particle. Required for splicing of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10022888, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor SNU114
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing ATP-dependent RNA helicase PRP28
- Pre-mRNA-processing factor 31
- U4/U6 small nuclear ribonucleoprotein PRP4
- U4/U6 small nuclear ribonucleoprotein PRP3
- Proteasome subunit beta type-4
- Small nuclear ribonucleoprotein E
- Pre-mRNA-splicing factor PRP21
Sequence:
MEVDNKRRHSEDELKQEAVKKIKSQEPNYAYLETVVREKLDFDSEKICCITLSPLNVYCCLVCGHYYQGRHEKSPAFIHSIDENHHVFLNLTSLKFYMLPQNVQILHDGEVQLLNSIKFAAYPTYCPKDLEDFPRQCFDLSNRTYLNGFIGFTNAATYDYAHSVLLLISHMVPVRDHFLLNHFDNQGEFIKRLSICVKKIWSPKLFKHHLSVDDFVSYLKVREGLNLNPIDPRLFLLWLFNKICSSSNDLKSILNHSCKGKVKIAKVENKPEASESVTGKVIVKPFWVLTLDLPEFSPFEDGNSVDDLPQINITKLLTKFTKSRSSSTSTVFELTRLPQFLIFHFNRFDRNSDHPVKNRNQTLVEFSSELEILHVKYRLKANVVHVVIKQPSTDGNAFNGDEKSHWITQLYDNKSEKWIEIDGINTTEREAELLFLKETFIQVWEKQE
Protein: Nonstructural protein (B2ZA87)
Organism: Bombyx mori densovirus Zhenjiang
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MESKSNFRILSNEIISKPSSLISNISSPSTSLIPRSLQKSAKRLTISSLESGNGKQQMKSKLAQVQRALRFCRDYNIVKYYQFMDIPPEEYRELRTHCSKDVLETAADINYQEYYYEEVNNRLQVFLSYGDGSWGEEEEEIVMLFKHNNVDISKFCEALYSIFTMSDYRKNCIFLNGNIKTGKTLMMRLITGNFKCVGKGCNNGVNSEFYYQKFIGRSICVLEEPFLDPQTLEDFKSIFGGEGFDISCKFHNPQTLNRTPFIITSNFSLLSRGHAPSISEMAIKDRFYIFNFNNSYTPKCKLSPKNFVNVYNKYYG
Protein: RRM domain-containing protein (Q5ARJ0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- mRNA splicing protein
- U1 small nuclear ribonucleoprotein C
- PWI domain-containing protein
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 snRNP splicing complex subunit
- Nuclear cap-binding protein subunit 2
- PAB1 binding protein
- snRNA cap binding complex subunit
- Cap binding protein
- U2 small nuclear ribonucleoprotein A'
Sequence:
MSFQNFDSFQNQHPAADAAATAPGAPATADTTMTGQADPSTAPFQGPAPGEGAPAVAQQGNEGKTTLWMGELEPWIDENFVRNLWFQMGEQVNVKMIRDKFSGRSNAGYCFVDFASPAAAAKALSLNGTPMPNTNRLFKLNWATGGGLADRSRDDRGPEYSIFVGDLGPEVNEYVLVSLFQSRFPSCKSAKIMTDPISGMSRGYGFVRFSDENDQQRALSEMQGVYCGNRPMRISTATPKNKGPGVVPGGMGMPGPAGMYPPMGAPPMGFYGAPQPMNQFTDPNNTTVFVGGLSGYVTEDELRSFFQGFGEITYVKIPPGKGCGFVQFVQRHAAEMAINQMQGYPIGNSRVRLSWGRSQNNSGPAGSPYRPAPPPPPMYLPPQHQYGGFAPMK
Protein: E3 SUMO-protein ligase CBX4 (EC 2.3.2.-) (Chromobox protein homolog 4) (E3 SUMO-protein transferase CBX4) (Polycomb 2 homolog) (Pc2) (mPc2) (O55187)
Organism: Mus musculus (Mouse)
Function: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00257}. Nucleus speckle {ECO:0000250|UniProtKB:O00257}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Polycomb complex protein BMI-1
- Chromobox protein homolog 8
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 2
- Chromobox protein homolog 2
- Polyhomeotic-like protein 2
- Polyhomeotic-like protein 3
- Chromobox protein homolog 7
- Chromobox protein homolog 6
Sequence:
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSADNRAKLELGTQGKGQGHQYELNSKKHHQYQPHSKERSGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGTKSHPPDKWAHGAAAKGYLGAVKPLGGGAGAPGKGSEKGPPNGMTPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEAAEGEARSPSHKKRAAEERHPQGDRTFKKAAGASEEKKAEVPCKRREEEALVSGDAQPQDLGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARSSHPPAHHHHHHHHHHHHHTVGLNLSHARKRCLSETHGEREPCKKRLTARSISTPTCLGGSPVSEHPANVSPTAASLPQPEVILLDSDLDEPIDLRCVKMRSDAGEPPSTLQVKPEAPAVAAVVAPAPASEKPPAEAQEEPVEPLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
Protein: Endothelial monocyte-activating polypeptide II pro-EMAP II family protein (Q54DX3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable methionine--tRNA ligase, cytoplasmic
- Probable methionine--tRNA ligase, mitochondrial
- Probable glutamine--tRNA ligase
- tyrosine--tRNA ligase
- arginine--tRNA ligase
- Probable isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- proline--tRNA ligase
Sequence:
MNVQLFFNLLSKVEPSTPTTLPTFDSTKEKLSKLFTENEFIKSLYPNIDSNTLKTLDEISDAFNTQDKKKEVLLHKLNKDLLTKTFILNEKLSALDLVYYVILYSWMNELNDKQRFTFCNITRWFNLIQNQKSILNIQPLITISVVPPPVEKKEEKKPAAAAAANKTENVNVDKKSTEQQTSEQQPKKEKRVAPVVAEPPMDISRFEIRVGKIVECEKHPNADSLYVEKIDLGEKEGPRTIVSGLVKFIPLDQMLNRMVLVLCNLKPANLKSIKSFGMVLCASNADHTHVEFVEPPANATIGERVVFDKYPGEFDKVLKPATFDAVSADFKTDDNKIASYKGDLSKTSAGPCVAKTLPNTLIK
Protein: Coxsackievirus and adenovirus receptor homolog (CAR) (mCAR) (P97792)
Organism: Mus musculus (Mouse)
Function: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. {ECO:0000250|UniProtKB:P78310}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
Interaction partners:
- Junctional adhesion molecule-like
- E3 ubiquitin-protein ligase LNX
- Complement decay-accelerating factor, GPI-anchored
- Membrane cofactor protein
- Tight junction protein 1
- Occludin
- Desmoglein-2
- Complement decay-accelerating factor transmembrane isoform
Sequence:
MARLLCFVLLCGIADFTSGLSITTPEQRIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPSDNQIVDQVIILYSGDKIYDNYYPDLKGRVHFTSNDVKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKFLLTVLVKPSGTRCFVDGSEEIGNDFKLKCEPKEGSLPLQFEWQKLSDSQTMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRAGTIAGAVIGTLLALVLIGAILFCCHRKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERAPQSPTLAPAKVAAPNLSRMGAVPVMIPAQSKDGSIV
Protein: Kv channel-interacting protein 4 (KChIP4) (A-type potassium channel modulatory protein 4) (Potassium channel-interacting protein 4) (Q99MG9)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24811166}; Peripheral membrane protein {ECO:0000269|PubMed:24811166}. Cytoplasm, cytosol {ECO:0000269|PubMed:19441798}. Peroxisome {ECO:0000250|UniProtKB:Q6PIL6}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily A member 4
- A-type voltage-gated potassium channel KCND1
- Voltage-gated potassium channel KCNC1
- A-type potassium channel modulatory protein KCNIP1
- A-type potassium channel modulatory protein DPP6
- Inactive dipeptidyl peptidase 10
Sequence:
MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI
Protein: Beta-glucan synthesis-associated protein SKN1 (P33336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for synthesis of the major beta-glucans of the yeast cell wall.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Inositolphosphotransferase 1
- Cell wall synthesis protein KRE9
- Cell wall synthesis protein KNH1
- Killer toxin-resistance protein 5
- Protein KRE1
- Protein ROT1
Sequence:
MSVRNLTNNRHSNSENSVSGSENSFYSSNEQSRQSSSLEPADGQNVRVSGNPFLGSEEFDEDYNSPSGDDERRGANEYSSSSSINYNNDPNSDTSLLANEKNSPERNGQRMSDYKGYYAKTNLTSANNLNNHNNNNYKNIISSSNDNSFASHLQPPDRNLPSHPSSNNMSSFSNNSLIKSPPPFDRYPLVGTRHISAAQSQSQNLINEKKRANMTGSSSSAHDSSLSSTNLYMGEQDFSPFGGYPASFFPLTLDEKEDDDYIHNPNVEEEAKLDRRRFVDDFKHMDRRSFLGLLGILFLFMAGIFIFIVLPAITFSGVVYHHEHVHAANSAGSSSSNTTSKSLTEYQYPQLAAIRTTLVDPDTPDSAKTRVAKDGSKWQLVFSDEFNAEGRTFYDGDDQFWTAPDIHYDATKDLEWYSPDAVTTTNGTLTLRMDAFRNHDLYYRSGMVQSWNKLCFTEGALEVSANLPNYGRVTGLWPGMWTMGNLGRPGYLASTQGVWPYSYEACDAGITPNQSSPDGISYLPGQKLSVCTCDNEDHPNQGVGRGAPEIDILEGEADTILGVGVASQSLQIAPFDIWYMPDYDFIEVYNFTTTTMNTYAGGPFQQAVSAISTLNVTWYEFGEEAGYFQKYAIEYLNDDDNGYIRWFVGENPTFTLYATSLHPSGNIDWRRISKEPMSAILNLGISNNWAYIDWQYIFFPVTMSIDYVRLYQPKGSTSITCDPEDYPTYDYIQSHLNAYYNANLTDWEQAGYTFPKNILTGGCSSSKFSLS