wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein 5-2 (Keratin-associated protein 5-8) (Keratin-associated protein 5.2) (Keratin-associated protein 5.8) (Ultrahigh sulfur keratin-associated protein 5.2) (Q701N4)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin associated protein 5-4
Sequence:
MGCCGCSRGCGSGCGGCGSSCGGCGSGCGGCGSGRGGCGSGCGGCSSSCGGCGSRCYVPVCCCKPVCSWVPACSCTSCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQSSCCKPCCCSSGCGSSCCQSSCCKPCCCQSSCCVPVCCQSSCCKPCCCQSNCCVPVCCQCKI
Protein: Utp13p (A0A1D8PNG5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- SnoRNA-binding rRNA-processing protein
- rRNA-processing protein
- Nan1p
- Ribosome biosynthesis protein
- Nucleolar protein 58
- Utp20p
- Rrp9p
- Utp5p
- SnoRNA-binding rRNA-processing protein
- U3 small nucleolar RNA-associated protein 22
Sequence:
MDVLKTTYAHTDIEPIYVGGTSASISTSNGELLLATPLNEDVIITNLDTNEIIYKIPGDGEVITNLTITPDGSYLAMISQSQLLRIFDLNKGSVIKNFKLPSPVYISSVDSTSSLFAFGGSDGVITVWDIENGYVTHSLKGHGTTICSLTFHGELNSQDWRLASGDTMGTVKIWDLVKRRCIHTLKDHNTAVRGVGFDQDGDLFISGGRDNVVIIYNTKNFKTINTFPINEQIEAAGFVSLIDDRQYFYTGGSENVLKIWDIKSGEMIGRSPIPLKTNEELLIIDVIKLYNNNLYLVISDQTLIELDLQELTPGHGHGHGQGDEIVEFPIVKRIAGNQGIIADIKYVGPEFNLLAMATNSPALRIVDIEKPLELRVYEGHTDILNAVDVSTDGKWIATASKDNEARLWRWNGELQDFEPFARFQGHAGAITAISLSKSQNEPKFLVTGSTDLTIKKWKIPNTPNSIVKTSEYTRRAHDKDINSIDVSPNDEYFATASYDKLGKVWQTDSGETIGVLKGHKRGLWDINFYKFDKLIVTGSGDKTIKVWSLLDFSCKKTLEGHTNSVQRVKFFNREHPQLLSCGADGLIKLWDYKQGEIIKSLDNHDQRIWAMDLKNDGEYFTTADADGKLSFWTDNTEEEVKFKELQAKEKIEQEQSLSNYIKNKDWSNAFLLALTLDHSMRLYNVIKSSIETNDDKDSIIGSFSLENTISLLDDGQLVKLFKKIRDWNVNFKFFEISQKLLNVVLNNFAVDKLTEVPGLMKIMESIIPYNERHYNRIEEMVEQTYVLDYTVEQMNKLIA
Protein: Phosphatidyl-myo-inositol mannosyltransferase (EC 2.4.1.345) (Alpha-mannosyltransferase) (GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (A0QWG6)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). In contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositol of PIM1.
Subcellular location: Cell membrane {ECO:0000305|PubMed:12068013, ECO:0000305|PubMed:19520856}; Peripheral membrane protein {ECO:0000305|PubMed:19520856}; Cytoplasmic side {ECO:0000305|PubMed:19520856}.
Interaction partners:
- Phosphatidylinositol mannoside acyltransferase
- Hydrolase, nudix family protein
- HIT family protein hydrolase
- Phosphatidylinositol phosphate synthase
- Threonine--tRNA ligase
- 1,4-alpha-glucan branching enzyme GlgB
- Malto-oligosyltrehalose trehalohydrolase
Sequence:
MRIGMVCPYSFDVPGGVQSHVLQLAEVLRDAGHEVSVLAPASPHVKLPDYVVSGGKAVPIPYNGSVARLRFGPATHRKVKKWIAEGDFDVLHIHEPNAPSLSMLALQAAEGPIVATFHTSTTKSLTLSVFQGILRPYHEKIIGRIAVSDLARRWQMEALGSDAVEIPNGVDVASFADAPLLDGYPREGRTVLFLGRYDEPRKGMAVLLAALPKLVARFPDVEILIVGRGDEDELREQAGDLAGHLRFLGQVDDATKASAMRSADVYCAPHLGGESFGIVLVEAMAAGTAVVASDLDAFRRVLADGDAGRLVPVDDADGMAAALIGILEDDQLRAGYVARASERVHRYDWSVVSAQIMRVYETVSGAGIKVQVSGAANRDETAGESV
Protein: PON (Paraoxonase) and MEC-6 Like (Q21427)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- Metallo-beta-lactamase domain-containing protein
- Uncharacterized protein F46C5.2
- Neuropeptide-Like Protein
Sequence:
MLQLSPFASNCLFFTSFAIVTTLFGKLLLHIDINKRTYNHVPGECGVIPNLPGILGLTTSTTGRLYMTTNSKDINTDQTHLFTFYSDNRTAREIEIRGGPPKWRLTPGALSINSETSNPNVFVHNKRTNNIDVFETNEQNDAWQYRKTFKDEQFEGLTDISAAGLNSFFFVKSSIFGTNFALNIIERVVPIPTGYIYFVSGNNIQQISRVSFPTGIVYDSVKKSIFVTSSTRNSIYRMKVQVKNGIEIVSSKEYDLGCSPSSIWKDFDGSFLITCHPVKFRYLLSLFNVITSSPSLILRVAVPTDKDKPLTITQLYSNDGATISNANVTVRAGRSLLISDGTKILNCHL
Protein: Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (F4JCI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable galactinol--sucrose galactosyltransferase 5
- Probable galactinol--sucrose galactosyltransferase 2
- Probable galactinol--sucrose galactosyltransferase 1
- Probable galactinol--sucrose galactosyltransferase 6
- alpha-D-xyloside xylohydrolase
- Galactokinase
- UDP-glucose 4-epimerase
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
- UDP-glucose 4-epimerase 5
- UDP-glucose 4-epimerase 2
Sequence:
MTGLSVEKTGSTRSTVFFIIFNLSIFSLSIEARSRQQHASFPPRGWNSYDSFCWTISEAEFLQSAEIVSKRLLPHGYQYVVVDYLWYRKKVEGAYVDSLGFDVIDEWGRLHPDPGRWPSSRGGKGFTEVAEKVHRMGLKFGIHVMGGISTQAYNANSLVMDSVKGGAYEESGRQWRAKDIGIKERACVWMSHGFMSVNTKLGAGKAFLRSLYRQYAEWGVDFIKHDCVFGTDFNIEEITYVSEVLKELDRPVLYSISPGTSVTPTMAKEVSQLVNMYRITGDDWDTWKDVTAHFDISRDLSASSMIGARGLQGKSWPDLDMLPLGWLTDQGSNVGPHRACNLNLEEQKSQMTLWSIAKSPLMFGGDVRNLDATTYNLITNPTLLEINSYSSNNKEFPYITATRVSRNKHKGYPHHPTGKNISTKHAFGLTSCKEQKANTWFIVDKNRGQICWNQHSSEKLEKPFCLYNRKALLASDKKLKHNQLYQGKLHLHTNDKAQSCLAASSQQKLTSKDYSQGALSPCKLDANQMWELHSNGTLENSYSGLCAVLNPVKAAEASSNGVRSWIATGRRGEVYVAFFNLNQEKTKISAKISDIATALRGKKNLVGASCTSHELWSGKDFGPTKDSVSIQVEPHGPALFVLHCSNA
Protein: UBX domain protein 1 (A0A087WTZ5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWMLELVAQKQREREEREEREALERERQRRRQGQELSAARQRLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSQPPPVAPEPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEELGGGQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS
Protein: ERO1-like protein beta (ERO1-L-beta) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase beta) (Endoplasmic reticulum oxidoreductin-1-like protein B) (Oxidoreductin-1-L-beta) (Q8R2E9)
Organism: Mus musculus (Mouse)
Function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2, PDIA3, PDIA4, PDIA6 and NXNDC12. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). Involved in oxidative proinsulin folding in pancreatic cells, hence required for glucose homeostasis in vivo.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Note=The association with ERP44 may be essential for its retention in the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- Protein disulfide-isomerase A4
- Protein disulfide-isomerase
- Protein disulfide-isomerase A6
- Thioredoxin domain-containing protein 5
- ERO1-like protein alpha
- Endoplasmic reticulum resident protein 29
- Endoplasmic reticulum resident protein 44
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A2
- Protein disulfide-isomerase A3
Sequence:
MSPGFRRAVTGQGAAAAVQLLVTLSFLSSLVKTQVTGVLDDCLCDIDSIDKFNTYKIFPKIKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGRSNKYSQAANSTKELDDCEQANKLGAINSTLSNESKEAFIDWARYDDSQDHFCELDDERSPAAQYVDLLLNPERYTGYKGSSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLCLEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFRRRFDPVETKGEGPRRLKNLYFLYLIELRALSKVAPYFERSIVDLYTGNVEDDADTKTLLLSIFQDTKSFPMHFDEKSMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEIQNLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRELQNFKALLQHRR
Protein: Amine oxidase domain-containing protein (Q5BBP2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MLTAFLFVAGALVACVRPQQFDPSAYAAEDVIERDFAIIGGGAAGTYAAISLADQNKTFTVVEMTGRLGGHTRTFRDEATGASIDIGVQLHENIPIVRDFFKRLNSPLAAFKPTDFGNPKYYDFTKKVALPNHTRPTIESDYVAVLNKYPFLDDLNNLPDNVPEELLLTWPDFAEKQNLSAASTEAGLLWPATPGNPLDTTALAIFNDGNHIELAEYAGAAVRSAAHYNSQIYDNALAELKEHVLLKSSIIAAQRGSSRKDGVRLIAETPSGRKLIKAKQLIIAMPPVLDNVKYFALDQQEHSILSKLSGKHYYAGVVNNTGLEAGVAYTNVGQNTPYHVASLPGVVEIAGSASPGYFFYWYNSVDPQTQAEIEEATRCTIKWLQSESGTEAVEPTFQDFADYSPFHLSPSTSDVADGWYGKMKGLQGHRNTWYISSLFVVGSTQVWNNTRNILPEIIDAARS
Protein: FYN-binding protein 2 (Activation-dependent, raft-recruited ADAP-like phosphoprotein) (Q5VWT5)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays a role in T-cell receptor (TCR)-mediated activation of signaling pathways. Required for T-cell activation and integrin-mediated T-cell adhesion in response to TCR stimulation.
Subcellular location: Membrane raft {ECO:0000269|PubMed:27335501}. Note=Recruited to membrane rafts and immunological synapse after TCR stimulation. {ECO:0000269|PubMed:27335501}.
Interaction partners:
Sequence:
MEGEGVRNFKELRAKFQNLDAPPLPGPIKFPAGVSPKGDIGGTQSTQILANGKPLSSNHKQRTPYCSSSESQPLQPQKIKLAQKSEIPKCSNSPGPLGKSTVCSATSSQKASLLLEVTQSNVEIITKEKVMVANSFRNKLWNWEKVSSQKSEMSSALLLANYGSKAIHLEGQKGMGLTPEEPRKKLETKGAQTLPSQKHVVAPKILHNVSEDPSFVISQHIRKSWENPPPERSPASSPCQPIYECELASQAPEKQPDVRHHHLPKTKPLPSIDSLGPPPPKPSRPPIVNLQAFQRQPAAVPKTQGEVTVEEGSLSPERLFNAEFEEPHNYEATISYLRHSGNSINLCTAKEIADPTYEVGIEELQKPGKNFPYPEPSAKHEDKKMKEKQPCELKPKNTEKEPYSNHVFKVDACEGTPEKIQMTNVHTGRRNMLAGKQEAMIDIIQTNPCPEGPKLARHSQGHCGHLEVLESTKETPDLGVSKTSSISEEIYDDVEYSRKEVPKLNYSSSLASSSEENRELYEDVYKTKNNYPKIDLDGKEALKRLQQFFKKEKDRFKIKKTKSKENLSAFSILLPDLELKSQEVIIYDDVDLSEKESKDEDKLKMWKPKFLTPKEKKEKNGAEESESFSPRNFFKTKKQNLEKNRMKREEKLFRERFKYDKEIIVINTAVACSNNSRNGIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHLDFKHQSWSP
Protein: Resistance to glucose repression protein 1 (Protein HEX2) (Second-site suppressor of the rna1-1 mutation 1) (Q00816)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in RNA processing and negative regulation of glucose repression. Regulates the level of two antigens, P43 and P70. Binds to protein phosphatase type 1. Functions with REG2 and SNF1 protein kinase to regulate growth. Might regulate SNF1 directly or indirectly.
Subcellular location: Nucleus.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-2
- Carbon catabolite-derepressing protein kinase
- Protein phosphatase 1 regulatory subunit SDS22
- SNF1 protein kinase subunit beta-3
- Serine/threonine-protein phosphatase 1 regulatory subunit GAC1
- Protein REG2
- 5'-AMP-activated protein kinase subunit gamma
- Hexokinase-2
- Protein BMH1
- Protein BMH2
Sequence:
MSTNLANYFAGKKDIENEHVNRNASHESNSKSDVKISGNDNDNDEDMGPSVSMAVQAKNDDDFHKSTFNLKRTRSMGLLDEYIDPTKKLLGRSDDLYDNDNEYYDNSSNNSSSNSSDDDYDDGYQEHSTSVSPPPADNDSYLIPQDDNDVVVEPERHVDYLSHEWKESEISNSWKYIILKKKKRDVDLVNAARLENASWRTWAKARNNLKTVSPEVVNWSKDSDVTWLYGPIVRDSEGNAQSEEEHDLERGYGSDDENSKRISMPTKNSKSIAAAPKPILKKRTVTEIIEDNALWKLNEARKHMTEMKHASVIMDPNGNKNVHDDFDALAAQVNAQYYHYPKESNSSVSLKSQHSDKKDNSTIPNPVGENSNGGGDKGEEDLHLKSALHVQNNRSTAQSNKSILENSTNDRKANLDQNLNSPDNNRFPSSTSSSNRDNENNSMGLSSILTSNPSEKSNKPTKNRHIHFNDRVEQCMALRYPASQSEDDESDDENKQYVDVNNNANVTTINNNRTPLLAIQHKSIPINSATEHLNKNTSDDDTSSQSSSSSHSDDEEHGGLYINARFSRRSDSGVHSPITDNSSVASSTTSRAHVRPIIKLLPDTTLNYGSDEESDNGEFNGYGNAVSHNVNTSRGYDYIYDYNSVYTGDTSSFLPVDSCDIVDVPEGMDLQTAIADDNASNYEFNNAVESKEKHVPQLHKASANNTTRQHGSHMLLYDDDNYSSSSDSEQQFIEDSQYNSSDDEEEEDDDDQEVDDNHDEGLSLRRTLSLGKSGSTNSLYDLAQPSLSSATPQQKNPTNFTGGKTDVDKDAQLAVRPYPLKRNSSSGNFIFNSDSEEESSSEEEQRPLPANSQLVNRSVLKGSVTPANISSQKKKALPKQPKASDSSQSFRIVNNTPSPAEVGASDVAIEGYFSPRNESIKSVVSGGNMMDHQDHSEMDTLAKGFENCHINNASKLKDKKVDSVQTTRKEASLTDSSNESLHKVVQNARGMASKYLHSWKKSDVKPQENGNDSS
Protein: Piwi-like protein 1 (EC 3.1.26.-) (Q8UVX0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a central role during gametogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Has a strong preference for piRNAs with a uridine nucleotide at their 5'-end (g1U preference, also named 1U-bias) and binds piRNAs in an opposite direction compared to piwil2/zili. Participates in a piRNA amplification loop with piwil2/zili. Not involved in the piRNA amplification loop, also named ping-pong amplification cycle. Acts as an endoribonuclease that cleaves transposon messenger RNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17418787}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:17418787}.
Interaction partners:
- Tudor domain-containing protein 1
- Tudor domain-containing 6
- RING finger protein 17
- ATP-dependent RNA helicase TDRD9
- Tudor domain-containing protein 7A
- Deleted in azoospermia-like
- DEAD
- Nanos homolog 3
- Dead end protein 1
- Tudor and KH domain-containing
Sequence:
MTGRARARSRGRGRGQEPAAPGAQPPVSQEAAKPVVSTPSEGQLVGRGRQKPAPGAMSEEAMLQISAGFQQVKIGERGGRRRDFHDSGVHTRQLMEHVKESKTGVSGTAIELRANFMRLLSRPMWALYQYHVDYKPPMESRRLRSALLFQHEETLGKAHTFDGAILFLPNKLRNAETVLCSETRNGEKVEITVTLTNELPPSSPVCLQFYNILFRRILRILNMQQIGRHYYNPDDPFNIPQHRLTIWPGFMTTILQYESSIMLCSDVSHKVLRSETVLDFMYSLRQQCGDQRFPEACTKELVGLIILTKYNNKTYRIDDIAWDHTPNNTFKKGDTEISFKNYFKSQYGLDITDGNQVLLVSHVKRLGPSGRPPPGPAMLVPEFCYLTGLTDKMRADFNIMKDLASHTRLSPEQREGRINRLISNINRNGDVQNELTTWGLSFENKLLSLNGRVLPSERIIQGGRAFEYNPWTADWSKEMRGLPLISCMSLDNWLMFYTRRNADVAQSLLQTLNKVSGPMGIRMQRAVMIEYEDRQESLLRALQQNVARETQMVVVILPTNRKDKYDCVKKYLCVDCPTPSQCVVSRTISKPQALMTVATKIALQMNCKMGGELWSVEIPLRQLMIVGIDCYHDTAAGKRSIGAMVASLNQGMSRWFSKCVLQNRGQEIIDALKGSLQGALKAYLKYNNSLPSRIIVYRDGVGDGMLQSVVDYEVPQIMQSIKTMGQDYEPKLSVVVVKKRISSRFFARIDGKIANPPPGTVIDTEVTRPEWYDFFIVSQAVRFGCVAPTHYNVVFDNSGLKPDHMQRLTYKLCHMYYNWQGIVRVPAPCQYAHKLAFLVGQSIHKEPNMNLDDFLYYL
Protein: RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (Heme-oxidized IRP2 ubiquitin transferase 1 homolog) (A9JTG5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (By similarity). LUBAC conjugates linear polyubiquitin to ikbkg and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (By similarity). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (By similarity). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) to conjugate linear polyubiquitin to ikbkg and possibly other components contributing to the stability of the complex (By similarity). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (By similarity). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (By similarity). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (By similarity). Binds polyubiquitin of different linkage types (By similarity).
Interaction partners:
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Uncharacterized protein.
- Receptor
- Receptor-interacting serine-threonine kinase 2.
- X-linked inhibitor of apoptosis.
- TNF receptor-associated factor
- TNF receptor-associated factor
- RING-type E3 ubiquitin transferase
- Tnf receptor-associated factor 5.
- RanBP-type and C3HC4-type zinc finger-containing protein 1
Sequence:
MSLSSGGWTRASPPAQSSSSHLGHEASQSACSTVLMSVKVSVCHSGIRPLCLPGAGDESLRLQLSMDPGKAGEFRLALRDISATAAGRSVFIAEFDLKTVQYEVKTPLCHELSLATPPHDRISFKFRCEQEAQEWATVVMSSLREAHRVAISSSTEEGRLPPPPLATQSKAPMPRTEEICAELVSAIEAGDVRSASVCASSLAKQKAALSIQPSKRNYTDSEVCLAVVVEDASSSCCVSVKVFPHSTIGALKQQVFSDYGFHPRVQRWVIGQSLCSDHRSLASYGVQRDGDTAFLYLISARQARLSRGIYQQDQESALLMVPTTHQAHQEAVSNGPAALNTASRPYSTLPTRLHNSHNTLSNNAGGSERLGLSDIRDLINLELPQLNEALGPNRTSIQPGWACPTCTYINKPTRPGCEMCSADRPEGYTVPGNYRPDALELRRIQQEKEAIRQYQQARETERRENFARLVQMDGQDLVPNPERVECRICYVELESGEGVLLRECLHCFCKECLRSVILMSEDPQVACPYRDESYACDCVLQEREIRALVSVDDYQHWLQRGLSVAESRCEGSYHCATADCPGWCVYEDTVNTFHCPVCKKQNCLLCKAIHEGMNCKQYQDDLTARAINDSAARRTRDLLKTLVNSGEAMHCPQCGIIVQKKEGCDWLRCTVCHTEICWVTRGPRWGPKGPGDISGGCRCNVNKQRCHPKCQNCH
Protein: GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I) (P0A6T5)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- Dihydroneopterin triphosphate 2'-epimerase
- Dihydropteroate synthase
- GTP cyclohydrolase-2
- Dihydroneopterin aldolase
- Dihydroneopterin triphosphate diphosphatase
- 7-carboxy-7-deazaguanine synthase
- Dihydrofolate synthase/folylpolyglutamate synthase
- 7-cyano-7-deazaguanine synthase
Sequence:
MPSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN
Protein: Conserved protein (O05900)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Calcium-transporting ATPase CtpE
- D-alanyl-D-alanine carboxypeptidase DacB2
- D-alanyl-D-alanine carboxypeptidase DacB1
- Beta lactamase like protein
- Hydrolase
- Protein Rv1367c
- Carboxypeptidase Rv3627c
- Possible conserved lipoprotein LpqK
Sequence:
MATICGHDQTSGNGRHGDVADVNGCGSTHQALGPPSGLPDASPNERSAIQIPAGRIDDAVAKVDGLVGELMQNTGIPGMAVAIVHGGKTLYAKGFGVRDVGKGGGPDNKVDADTVFQLASVSKSVGATVVAHAVTDNVVTWDTPVVSKLPWFALRDPYVTGQVTIADLYSHRSGLPDHAGDLLEDLGYDRRQVLQRLKYLPLAPFRISYAYTNFGVTAAAEAVAAAAGQSWEDLSDEVLYRPLGMGSTSSRFTDFLARPNHAVNHVKVADRWEARYQRDPDAQSPAGGVSSSLNDMTHWLAMVLADGVYNGRRITSPEALLPVYTPQVISRHPVSPRARASFYGYGFNVGVTSSGRTEYSHSGAFGLGAAANFVVLPSEDLAIIALTNAGPIGVPETLTAEFMDLVQYGQVREDWAALYKKAFAPLNELAGSLVGKQSPANPAPSRPLNDYVGVYANDYWGPATVTYHDGQLRLSLGPKNQTFDLTHWDGDTFTFTLSTENALPGSISKATFAGDTLNLEYYDADKLGTFTR
Protein: Altered inheritance of mitochondria protein 6 (Q5ASC2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Uncharacterized protein
Sequence:
MALFRFLVTAASAMFLAVPTEALEGTSELQSILKNTHRSSEYKYPTDFTRGILPIPVHSHNDYWRDVPFYTGWLFFVLSFIKPFIKKSFPALSLGCISVEADVWLYNGTLHVGHDESSLTDERTFESLYINPILDVLERQNPKSKFLTAPTHNGVFDTSTDQTLYLWVDSKTSGPETFEAVIAALEPLRRKGYLTTVKNNETLIQGPVTVIGTGNTPYDMVGPVADRDYFYDGPLAALNESGNEGITSLISPIASTSFTSAIGELTLGVDSVLSDEQLDTLRSQISNAKEKGIKARYWGAPSWPIRARNILWTTLINEGVGLLNADDLAAAAEYF
Protein: Histone acetyltransferase of the MYST family 2 (EC 2.3.1.48) (Histone acetyltransferase of the GNAT/MYST superfamily 5) (MYST-like histone acetyltransferase 2) (Q9LXD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone acetyltransferase which may be involved in transcriptional activation. Acetylates 'Lys-5' of histone H4 (H4K5ac). Essential for gametophyte development. Negative regulator of flowering controlling the H4K5ac levels in the FLC chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:17877703}.
Interaction partners:
- Histone acetyltransferase subunit NuA4-domain protein
- Histone H4
- Protein MRG2
- SWR1-complex protein 4
- Phosphotransferases/inositol or phosphatidylinositol kinase
- RuvB-like protein 1
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Protein MRG1
- Histone acetyltransferase GCN5
- Actin-related protein 4
Sequence:
MGSSANTETNGNAPPPSSNQKPPATNGVDGSHPPPPPLTPDQAIIESDPSKKRKMGMLPLEVGTRVMCRWRDGKHHPVKVIERRRIHNGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDKVTSLKMTRHQKRKIDETHIEGHEELDAASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPGDEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACILTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNISIKELSDVTAIKAEDILSTLQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPYKDQS
Protein: BART domain-containing protein (Q38DY6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQGEGNELLERLDAFFGEGANTDAIGNFFSEEYNIVQRLEAANDSSEALEFFSLFKRYGALVNTILETFGEREAASGSAVSLEQLAEAVMKEWQQPQDFCRYLCTGYIAGALDFDSFKQLVADVVALTTYPVGDEISEDEAVSVSGSIEEDDNEEEDA
Protein: GDNF family receptor alpha (B0S6A6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Neurturin
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Glial cell line-derived neurotrophic factor
- Neurturin
- TGF_BETA_2 domain-containing protein.
Sequence:
MTARAAPFYARGFLSRNRNMYIYIGFLLFLDELVFSMSGSSSLSESGNQDSMDCLKATEKCNQDQKCSHRFRIMRQCLAGKDRNTMLANRDCQVALEVLQEMALFDCRCKRGMKKEMQCLQSYWSINIGLTEGEDFYEPSPYEPMTPHRHSDAFRLASIISGMHSGTSKGQPHCTDPSRPCNPCLDATKACNLNENCKRQRSNYISTCTRAQTQGQQPSQTQTQEGCNRKRCHKALRQFFERVDTQYSYGLLFCACKDQACAERRRQTIVPSCSYQDKNKPNCLQLRNTCRLDVHCRSRLADFHTNCQMTPHSISSCLNDDYQACLASYTRLIGTDMTPNYLDSGHSNFTISPWCTCKGSGNLEEECEKFLQDFRENTCLRNAIQAFGYGSLPKPDPQPTTGSVKPDLEPTATVAKTTMEPGEDPCIISPCSNLNELDCYPSKDYNCESAEMKLSKPESPLNTRVEDPRNTSPGVKALTEAMMQSLLFALVTLVM
Protein: Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.147) (Core 3 synthase) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6) (BGnT-6) (Beta-1,3-Gn-T6) (Beta-1,3-N-acetylglucosaminyltransferase 6) (Beta3Gn-T6) (Q6ZMB0)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the core 3 structure of the O-glycan, an important precursor in the biosynthesis of mucin-type glycoproteins. Plays an important role in the synthesis of mucin-type O-glycans in digestive organs.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15755813}; Single-pass type II membrane protein {ECO:0000269|PubMed:15755813}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Polypeptide N-acetylgalactosaminyltransferase 6
- C1GALT1-specific chaperone 1-like protein
- Polypeptide N-acetylgalactosaminyltransferase 2
- Polypeptide N-acetylgalactosaminyltransferase 3
- Polypeptide N-acetylgalactosaminyltransferase 5
Sequence:
MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEPPSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLLLAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAREHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQPPGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAARHTPLFPIDDAYMGMCLERAGLAPSGHEGIRPFGVQLPGAQQSSFDPCMYRELLLVHRFAPYEMLLMWKALHSPALSCDRGHRVS