wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase F(0) complex subunit k, mitochondrial (ATP synthase membrane subunit DAPIT, mitochondrial) (Diabetes-associated protein in insulin-sensitive tissues) (Up-regulated during skeletal muscle growth protein 5) (Q9JJW3)
Organism: Rattus norvegicus (Rat)
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. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q96IX5}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- 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
Sequence:
MAGPESDGQFQFTGIKKYFNSYTLTGRMNCVLATYGGIALLVLYFKLRPKKTPAVKAT
Protein: Interleukin 22 (G3V6X6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interleukin 22 receptor subunit alpha 1.
- Interleukin 10 receptor subunit beta
- Interleukin-22 receptor subunit alpha-2
- Interleukin-17A
- Interleukin-23 receptor
- Interleukin-17F
- T-cell surface glycoprotein CD4
- Interleukin 20 receptor subunit alpha
- Interferon alpha/beta receptor 1
- Interferon gamma
Sequence:
MSVLRKSMSFSLMGTLAASCLLLVALWAQKADALPINSQCKLEAANFQQPYIVNRTFMLAKEASLADNNTDVRLIGEELFRGVKAKDQCYLMKQVLNFTLEDVLLPQSDRFQPYMQEVVPFLTKLSSHLSPCHISGDDQNIQKNVRQLKETVQKLGESGEIKAIGELDLLFMSLRNACV
Protein: Transcription initiation factor TFIID subunit 12 (Transcription initiation factor TFIID 20 kDa subunits) (TAFII-20) (TAFII20) (Q8VE65)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Component of the TATA-binding protein-free TAF complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 10
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 9
- TATA-box-binding protein
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 6
- Transformation/transcription domain-associated protein
Sequence:
MNQFGPSALINLSSFSSVKPEPASTPPQGSMANSTTVGKIAGTPGTGGRLSPENNQVLTKKKLQDLVREVDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWIPGFGSEEIRPYKKACTTEAHKQRMALIRKTTKK
Protein: RH64582p (Q8IGB7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VERCACYDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Phosphoprotein (Protein P) (P14252)
Organism: Sendai virus (strain Fushimi) (SeV)
Function: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity).
Subcellular location: Host cytoplasm.
Interaction partners:
Sequence:
MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLETDSTKKGIGENTSSMKEMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQESVESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPDLIREDEFRDEIRNPLYQERDTEPRASNASRLLPSKEKPTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEEDIESLTN
Protein: Cold-inducible RNA-binding protein (Glycine-rich RNA-binding protein CIRP) (Q53XX5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE
Protein: Extracellular matrix receptor III (H0YD90)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
XFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATKQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLL
Protein: Transposon Ty3-I Gag polyprotein (Gag3) (Transposon Ty3-2 protein A) (TY3A) [Cleaved into: Capsid protein (CA) (p24); Spacer peptide p3; Nucleocapsid protein p9 (NC) (p7)] (Q99219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome.
Subcellular location: Cytoplasm.
Interaction partners:
- TATA-box-binding protein
- Transcription factor IIIB 70 kDa subunit
- Ran GTPase-activating protein 1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2
- Replication factor A protein 1
- Transcription factor TFIIIB component B''
- ATP-dependent DNA helicase MPH1
- Replication factor A protein 2
- DNA repair protein RAD1
- Endosomal protein P24B
Sequence:
MSFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNRYVHTVRTRRSYNKPMSNHRNRRNNNASREECIKNRLCFYCKKEGHRLNECRARKASSNRS
Protein: Transmembrane protein 64 (Q3U145)
Organism: Mus musculus (Mouse)
Function: Positively regulates TNFSF11-induced osteoclast differentiation. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with SERCA2 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation. Negatively regulates osteoblast differentiation and positively regulates adipocyte differentiation via modulation of the canonical Wnt signaling pathway. Mediates the switch in lineage commitment to osteogenesis rather than to adipogenesis in mesenchymal stem cells by negatively regulating the expression, activity and nuclear localization of CTNNB1.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:23395171}.
Interaction partners:
Sequence:
MRNPGGSLPHTLPRALQHAGRTGVVEQPGRWAPERTAGGDRSEDRLPRGGGASAAAAAAAAAASGALLGAYLERHGLPAASDLPAPAGALAGGPGSGGGVVVGVAEVRNWRCCCLGSTCWCRSLVLVCVLAALCFASLALVRRYLQHLLLWVESLDSLLGVLLFVVGFIVVSFPCGWGYIVLNVAAGYLYGFVLGMGLMVVGVLIGTFIAHVVCKRLLTAWVAARIQNSDKLSAVIRVVEGGSGLKVVALARLTPIPFGLQNAVFSITDVPLPSYLMASSAGLLPTQLLNSYLGTTLRTMEDVIAEQSLSGYFVFCLQIVISIGLMFYVVHRAQVELNAAIVACEMELKTSLVKGNQSDPSGSSFYNKRTLTFSGGGINIV
Protein: Aflatoxin biosynthesis regulatory protein (Aflatoxin biosynthesis protein R) (Q6UEG8)
Organism: Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Function: Transcription factor involved in regulation of the aflatoxin biosynthesis gene cluster. Binds with its co-regulator aflS to AFLR1 elements (5'-TCGSWNNSCGR-3') present in the promoters of the aflatoxin cluster genes. The ratio of the expression data between aflS:aflR plays a crucial role in the regulation of aflatoxins production. A high ratio, produced at a range between 17 and 30 degrees Celsius, corresponds with the production profile of aflatoxin G1 biosynthesis. A low ratio, produced over 30 degrees Celsius, is related to aflatoxin B1 biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:23342682}. Endosome {ECO:0000269|PubMed:23342682}.
Interaction partners:
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
- RibosomalL22
- KOW domain-containing protein
- Large ribosomal subunit protein uL6m
- Ribosomal protein L23 N-terminal domain protein
- Large ribosomal subunit protein uL3m
- Ribosomal protein S8
- RpsQ
- Ribosomal protein S19-domain-containing protein
- Ribosomal protein S11-domain-containing protein
Sequence:
MVDHISPRASPGPIRSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRRPSESLPSAGSEQGLPAHNTYSTPHAHTQAHTHAHSHPQPHPQSHPQSNQPPHALPTPNGSSSVSAIFSHQSPPPLVETQGLGGDLAGQAQSTLSSLTVDSEFGGSLQSMEHGNHADFLAESTGSLFDAFLEVGTPMIDPFLESAPLPPFQARYCCFSLALQTLTCLFPHAPLGCQLRLTDGEDSSCNLMTTDMVISGNKKATDAVRKILGCSCAQDGYLLSMVVLIVLKVLGWYAAAAGTQCTSTAAGGETNSGSCSNSPATVSSGCLTEERVLHHPSMVGEDCVDEEDQPRVAAQLVLSELHRVQSLANLLAKRLQEGGDDAAGIPAHHPASPFSLLGFSGLEANLRHRLRAVSSDIIDYLHRE
Protein: Metastasis-associated 1 family, member 2 (Metastasis-associated protein MTA2 isoform X1) (F1QLG2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCLFRRRDISASLNTLADSNARDFEEESKQPSTSEQQKHQLKHRELFLSRQFESLPATHIRGKCNVTLLNETDVLTGYLEREDCFFYSLVFDPVQKTLLADQGEIRVGSKYQAEIPDKLAEVEADSRVQEKLETKVWDPNNQLKDPQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQKNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASVVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQITAPGNKPGMNGATGYQKGLSCESCHTAQSQQWYAWGPPNMQCRLCSSCWIYWKKYGGLKTPTQLEGATRASSEAAPRGHMTRQEVQGMSPFTSSAGRAKLLAKNRQTFILQTTKLTRIARRVCQDILQSRRAARRPYASINANAVKAECMIRLPKAAKSGVKNRPIPRPSLINIVKDLAIQAPLKLKAPRGAPTPINRNQVNQPRSASALLGKRPFDNAGGHLLSTNGRPFAMGMRAANQSVIKRQKVSQGDAPNPVVFVATKDTRALRKHLTQAEMRRAARKPHLPVKIKLPLPPRPLPVPIIPSSISEPIVLED
Protein: Nucleolar complex protein 3 homolog (NOC3 protein homolog) (NOC3-like protein) (Nucleolar complex-associated protein 3-like protein) (Q6DRN3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- NOC2-like nucleolar-associated transcriptional repressor
- Ribosome biogenesis protein BRX1 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- Nucleolar GTP-binding protein 1
- Protein MAK16 homolog
- Pescadillo
- Ribosomal L1 domain-containing protein 1
- EBNA1-binding protein 2.
- Ribosome biogenesis protein wdr12
- Ribosome production factor 2 homolog
Sequence:
MGPASKRNKKKRPSFRKLLKTSNLKLENKLKNRQFKQQSSAKKQRKEQRKLHKAISDVSHQTLKPLERYKKRPEDEEEEEEFLESLPTDMMDEDDLEHIRAIAQKASFLTRDLSSCAPVHAKKHKSEQALENYEKMPRKMQQEEEKELIHLLPIKDKSGLIPQSMEKPVLPQAEEEEEEPNQEVYLQKEEEPESAPLLTPQEQFEQRAQKLMEKKLRIAALSSAILADPHVNIKKLKELRAMLMETDPCVAVTVRKLVMVSLMEVFKDIVPAYRIRPLTEEEKAAKVKKETLQLREFEEGLVSQYKFYLEELEQTVKDWKQKKEKRSQAVSLQSYKGLAEVAVRCICELLVALPHFNFHNNIIVMLVPLMNDSDKKVSEMCCEAVKKLLKQDKVGQASLAMVKVISGMVKSRNYRIKPVVLNCLLCLRIKEVDMKKDTEDTAPKKKFMSFKEKRKNLSRMQRKWKKAEEKLQKELLEAEATESKEKKIKLHTETLNVVFLIYFRILKKAQKSVLLSSVLEGLAKFAHLINLEFFDDLLAVLYNLITSGDLTYRESLHCILTSFHILSGQGDVLNIDPLKFYSHLYRTLLTLHAGGVNEDTVIVLQCLDVMLSKRRKQVTLQRAQAFLKRLNTVALHLLPDSCVGILAANRMLMQTFPKCDILLDNETQGSGVYLPELDVPEYCNPQNTALWELHLLKSHYHPVVRKFAAHLMKGAPSEGSGALGVELSRRSPLQLFEDYSVKDMSFNPPVAGPPSKKKEYFTIGHAFLHSELSRQIDAALQEEPEQMSLDFTSPHTQQEP
Protein: RNA polymerase sigma-54 factor (P24255)
Organism: Escherichia coli (strain K12)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of enzymes involved in arginine catabolism. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for the receipt of the melting signal from the remotely bound activator protein GlnG(NtrC).
Interaction partners:
- Psp operon transcriptional activator
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- DNA-binding transcriptional regulator NtrC)
- Transcriptional regulatory protein GlrR
- DNA-directed RNA polymerase subunit omega
- Nitrogen regulatory protein
- ECF RNA polymerase sigma-E factor
- RNA polymerase sigma factor RpoH
Sequence:
MKQGLQLRLSQQLAMTPQLQQAIRLLQLSTLELQQELQQALESNPLLEQIDTHEEIDTRETQDSETLDTADALEQKEMPEELPLDASWDTIYTAGTPSGTSGDYIDDELPVYQGETTQTLQDYLMWQVELTPFSDTDRAIATSIVDAVDETGYLTVPLEDILESIGDEEIDIDEVEAVLKRIQRFDPVGVAAKDLRDCLLIQLSQFDKTTPWLEEARLIISDHLDLLANHDFRTLMRVTRLKEDVLKEAVNLIQSLDPRPGQSIQTGEPEYVIPDVLVRKHNGHWTVELNSDSIPRLQINQHYASMCNNARNDGDSQFIRSNLQDAKWLIKSLESRNDTLLRVSRCIVEQQQAFFEQGEEYMKPMVLADIAQAVEMHESTISRVTTQKYLHSPRGIFELKYFFSSHVNTEGGGEASSTAIRALVKKLIAAENPAKPLSDSKLTSLLSEQGIMVARRTVAKYRESLSIPPSNQRKQLV
Protein: Conidiogenone synthase (Bifunctional terpene synthase PchDS) (BFTS PchDS) (Conidiogenone biosynthesis cluster protein PchDS) (Diterpene synthase PchDS) (DS) [Includes: Terpene cyclase (EC 4.2.3.-); Geranylgeranyl diphosphate synthase (GGDP synthase) (GGS) (EC 2.5.1.29)] (B6HFX8)
Organism: Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of conidiogenone, a diterpene known to induce the conidiation. The bifunctional terpene synthase PchDS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into deoxyconidiogenol. The C-terminal prenyltransferase (PT) domain of PchDS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GGPP into deoxyconidiogenol. The cytochrome P450 monooxygenase PchP450 then catalyzes two rounds of oxidation to furnish conidiogenone.
Interaction partners:
Sequence:
MADKITDEYAVGIDPEIYANNPAYSSLFNPYIHKQTIIADHVSVQCHIDLNGIDAVGSKFGNLNAHAGNFTSLCAPNCLPERFALVAYTVEYAFLHDALNQSGMTSVSTRVSDKAQRKSEVQAKIAAEYLRLDPVFGEWFLNKWQTFTACVKDVRSLEFPSLDDYLEFRIVDAAADWTLYNFRWGSGITLTPEEEKIADPMSYVAYAELCLVNDLFSWDKEYASHIKSNGDVPLVNAVHIVAVTQGLTHCAAKAVVQAEVRAHEERFCQLKEQYEATDKPSHEVLRWLRLLEHSMAGNWVWSLCVPRYCKVDRNPYKDHLEKYGSDAVRVLTPLDRLCWPKQEIKDMKQSELKDPSSSTYKSHFSPLEPNPGPEQMRLTISQTQQQRPVLNPYTYINSLPSKNVRQTLIAALNSWYKVPVKSLLIIEGAVNFLHNSSLLLDDIQDGSFLRRGRPVAHQIFGVGQTINTATYLMNEALYLIQMLSPSAVSVYTEIDEMRNLQLGQGRDLYWSYHTHVPTPAQYISMVDGKTGGLFRLISRLMRSEATKNSDLDISQFATLLGRHFQIRDDYQNLQSEDYTKNKGFCDDLDEGKLSFPIILSMQSPGFSNTALSSVFKGSQKGQTLSLEMKQYMLEEITARGAFSETKAVLRKLHTELLRLLIETEKKAGGVENWALRLLIMKLDIAEEKKVAPPKSDSHWGVNQRRAWKGCQKNGRPIDKACFLRAMEETLQK
Protein: Ferruginol synthase (SfFS) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH24) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase) (A0A0C5QRZ2)
Organism: Salvia fruticosa (Greek sage)
Function: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products. Catalyzes the oxidation of abietatriene to produce ferruginol. Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol. Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant. May also convert miltiradiene into 11-oxomiltiradiene (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAMGRDPSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHKGVLFGFAVRRAVPLKIVPIKA
Protein: Tetraspanin-33 (Tspan-33) (Penumbra) (mPen) (Proerythroblast new membrane) (Q8R3S2)
Organism: Mus musculus (Mouse)
Function: Plays an important role in normal erythropoiesis. It has a role in the differentiation of erythroid progenitors. Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity). Mediates docking of ADAM10 to zonula adherens by interacting with ADAM10 and, in a PDZD11-dependent manner, with the zonula adherens protein PLEKHA7.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30463011}; Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011}. Cytoplasm {ECO:0000269|PubMed:30463011}. Note=Is localized to zonula adherens by PLEKHA7 by a PDZD11-dependent interaction. {ECO:0000269|PubMed:30463011}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10
- Pleckstrin homology domain-containing family A member 7
- PDZ domain-containing protein 11
- Afadin
- Hematopoietic progenitor cell antigen CD34
- Tetraspanin-3
- Non-selective voltage-gated ion channel VDAC1
- Complement component C8 beta chain
- Complement component C8 alpha chain
- Complement C5
Sequence:
MARRPGVPAAYGDEFSFVSPLVKYLLFFFNMLFWVISMVMVAVGVYARLMKHAEAALACLAVDPAILLIVVGVLMFLLTFCGCIGSLRENICLLQTFSLCLTIVFLLQLAAGILGFVFSDKARGKVSEIINNAIVHYRDDLDLQNLIDFGQKKFSCCGGISYRDWSQNMYFNCSEDNPSRERCSVPYSCCLPTPNQAVINTMCGQGMQALDYLEASKVIYTNGCIDKLVNWIHSNLFLLGGVALGLAIPQLVGILLSQVLVNQIKDQIKLQLYNQQHRADPWY
Protein: Uncharacterized protein (A0A0H2UQB7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKLNIQEIRKQSEGLNFEQTLDLVDDLRARNQEILDVKDILAVGKVQYEDRMYFLDYQLSYTIVLASSRSMEPVELVESYPVTEVFMEGATNQLDQEVLDDDLVLPIENGELDLAESVSDNILLNIPIKVLTAEEEAGQGFISGNDWQIMTEEEYQAQKAVKKEENSPFAGLQGLFDGDE
Protein: Relaxin family peptide receptor 2 (F1RSS8)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
YSSFLHFLIHPSYFARTEGSSITSLCPKGYFPCGNLTQCLPRAFHCDGVDDCGNGADEENCGDTSGWATIFGTVHGNANNVALTQECFLNQYPQRCYCKETELDCINAGLTSVPTVSSNVTLLSLKKNNIHSLSDKVFIKYTELKKIFLQHNRIRHISRKAFFGLHNLQILYLNHNCITTLSPGVFRDLHRLTWLILDDNPITRISQRLFAGLNSLFFLSMVNNYLEALPRQMCANMPHLNWLDLEGNGIKHLTNSTFLSCGSLTVLFLPRNQIDIVPEKTFSSLKNLGELDLSSNLIMELPPHIFKDLKLLQKLNLSSNPLLYLHKNQFESLKQLQSLDLERIEIASISTRMFQPMKNLSHIYFKNFRYCSYAPHVRICMPLTDGISSFEDLLANNILRIFVWVIAFITCFGNLFVIGMRSFIKAENTTHATSIKTLCCADCLMGVYLFFIGFFDLKYRGQYQKYALLWMESLQCRLLGFLAMLSTEVSVLLLTYLTLEKFLAVVFPFSNIRPGKWQTSGILIGIWIVGFLIAAIPFWKEDYFGNFYGKNGVCFPLYYDQTEAIGSKGYSLGIFLGVNLLAFLIIVFAYTIMFCSIQKTALQTSEVRSPTGREVAVANRFFFIVFSDAICWIPVFVIKILSLFRVEIPGSLTSWVVIFFLPVNSALNPILYTLTTSFFKDTLKQLLHNQRRKSIFKTKKKSLSTSIVWTDDSSSLKRGVLNKIPLGDNIVKPLS
Protein: Peroxidase (EC 1.11.1.7) (Q8RVP6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362060}.
Interaction partners:
Sequence:
MYRFPWVLLLVAAVNMAVAAEPLRPGFYSETCPPAEFIVRDVMKKAMIREPRSLASVMRLQFHDCFVNGCDGSLLLDDTADMVGEKQALSNINSLRSFEVVDEIKEALEDACPSTVSCADILVLAARDAVALSGGPNWEVRLGRKDSLTASQQDSDNIMPSPRADATSLINLFAQFNLSVKDLVALSGSHSIGKARCFSIMFRLYNQSGSGKPDPAIEPEFREKLNQLCPLGVDENVTGPLDATPRVFDNQFFKDLVGGRGFLNSDQTLFTSRRTRPYVRVFSKDQDEFFKAFVEGMLKMGELQVEQPGEIRINCRVVNGRPVDVLMSY
Protein: Tripartite motif-containing protein 26 (EC 2.3.2.27) (Acid finger protein) (AFP) (RING finger protein 95) (Zinc finger protein 173) (Q12899)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs). Promotes nuclear IRF3 ubiquitination and proteasomal degradation. Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25763818, ECO:0000269|PubMed:34017102, ECO:0000269|PubMed:35872575}. Nucleus {ECO:0000269|PubMed:25763818, ECO:0000269|PubMed:33419081}. Note=Viral infection mediates TRIM26 nuclear translocation. {ECO:0000269|PubMed:25763818}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- T-cell receptor-associated transmembrane adapter 1
- Interferon regulatory factor 3
- E3 ubiquitin-protein ligase PPP1R11
Sequence:
MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDVRPISGSRPVCPLCKKPFKKENIRPVWQLASLVENIERLKVDKGRQPGEVTREQQDAKLCERHREKLHYYCEDDGKLLCVMCRESREHRPHTAVLMEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAALKKLQDQRQYIVAEFEQGHQFLREREEHLLEQLAKLEQELTEGREKFKSRGVGELARLALVISELEGKAQQPAAELMQDTRDFLNRYPRKKFWVGKPIARVVKKKTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYTSLYKSAYLHPQQFDCEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGDGYDDWETDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTSPEAELFPALRPRRVGIALDYEGGTVTFTNAESQELIYTFTATFTRRLVPFLWLKWPGTRLLLRP