wanglab/gogpt-training-data huggingface dataset:
Protein: Calreticulin (CALBP) (CRP55) (Calcium-binding protein 3) (CABP3) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (P18418)
Organism: Rattus norvegicus (Rat)
Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12782144}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule {ECO:0000250|UniProtKB:P27797}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.
Interaction partners:
- Protein disulfide-isomerase A3
- TAP binding protein
- Endoplasmin
- Calnexin
- Beta-2-microglobulin
- Endoplasmic reticulum chaperone BiP
- Prolow-density lipoprotein receptor-related protein 1
- Thrombospondin-1
- Antigen peptide transporter 1
- Antigen peptide transporter 2
Sequence:
MLLSVPLLLGLLGLAAADPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPGGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDEDDRDEDEDEEDEKEEDEEDATGQAKDEL
Protein: Dolichol-phosphate mannose synthase subunit 3 (DPM synthase subunit 3) (Dol-P-Man synthase1) (Dolichol phosphate-mannose biosynthesis regulatory protein) (Q8LEQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPMS1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21558543}; Multi-pass membrane protein {ECO:0000255}. Note=May serve as regulatory subunit and membrane anchor for DPMS1. {ECO:0000269|PubMed:21558543}.
Interaction partners:
- Dolichol-phosphate mannose synthase subunit 2
- Dolichol-phosphate mannosyltransferase subunit 1
- dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
- UDP-glycosyltransferase TURAN
- Lipid phosphate phosphatase gamma
- At3g57220
- Dolichol kinase EVAN
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Phosphatidylinositol-glycan biosynthesis class X-like protein
Sequence:
MKHIVKILSLLVAISAFWIGLLQAAIIPRSHTWLLPIYFVVSLGCYGLLMVGVGLMQFPTCPQEAVLLQKDIAEAKDFFKHKGVDVGSN
Protein: ATP-dependent Clp protease proteolytic subunit-related protein 4, chloroplastic (ClpR4) (Protein HAPPY ON NORFLURAZON 5) (Q8LB10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plastid protein homeostasis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14593120}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit-related protein 2, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- Chloroplastic ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- CLP protease regulatory subunit CLPX1
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- ATP-dependent Clp protease ATP-binding subunit CLPT2
- Chaperone protein ClpC1, chloroplastic
Sequence:
MEVAAATATSFTTLRARTSAIIPSSTRNLRSKPRFSSSSSLRASLSNGFLSPYTGGSISSDLCGAKLRAESLNPLNFSSSKPKRGVVTMVIPFSKGSAHEQPPPDLASYLFKNRIVYLGMSLVPSVTELILAEFLYLQYEDEEKPIYLYINSTGTTKNGEKLGYDTEAFAIYDVMGYVKPPIFTLCVGNAWGEAALLLTAGAKGNRSALPSSTIMIKQPIARFQGQATDVEIARKEIKHIKTEMVKLYSKHIGKSPEQIEADMKRPKYFSPTEAVEYGIIDKVVYNERGSQDRGVVSDLKKAQLI
Protein: CRISPR-associated protein Cas5 (D4GQN7)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly. This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas5 and Cas6 are also required for optimal crRNA processing and/or stability.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MSPHIDANGVPIDCLSFTVRSTWGHFKRVGRSVTKQTYRIPPRTTVAGMLAAIVGADRDSYYDVFGADNSAIAITPLSDLRTVNIPTTGLGTDPKQDVTETAGSWRTYKLTYQNTTGDRQLHSYEVLADPAYRIDVALENEEFYDSLREHLVNGTSIYPPSLGKSEYLAVIEDVEVDREPEVQDIDETLDIDSVVPISLSEAVPQGKVTYGVERSPAVMVRESGGRRTTRFDDYVYAQQASNPVRIGEQTDVAPVQVGDRTVVFR
Protein: Chloride intracellular channel protein 5 (Glutaredoxin-like oxidoreductase CLIC5) (EC 1.8.-.-) (Q9NZA1)
Organism: Homo sapiens (Human)
Function: Required for normal hearing. It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti (By similarity). Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture. Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:15184393}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15184393}. Membrane {ECO:0000269|PubMed:15184393, ECO:0000305|PubMed:18028448}; Single-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:20335315}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Mitochondrion {ECO:0000250|UniProtKB:Q9EPT8}. Cell projection, stereocilium {ECO:0000269|PubMed:24285636}. Note=Associates with the cortical actin cytoskeleton (PubMed:10793131, PubMed:15184393). Localizes to the apical region of cochlear hair cells, at the base of the actin-rich hair bundle (By similarity). Colocalizes with podocalyxin at the apical cell membrane in renal glomeruli (PubMed:20335315). May localize to the centrosome in lens epithelial cells (By similarity). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q8BXK9, ECO:0000250|UniProtKB:Q9EPT8, ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:15184393, ECO:0000269|PubMed:20335315}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus {ECO:0000269|PubMed:12163479}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12163479}. Note=Colocalizes with AKAP9 at the Golgi apparatus as well as, to a lesser extent, the centrosome. {ECO:0000269|PubMed:12163479}.
Interaction partners:
- Taperin
- Ezrin
- Radixin
- Glutaredoxin domain-containing cysteine-rich protein 2
- Unconventional myosin-VIIa
- Plastin-1
- Chloride intracellular channel protein 4
- Chloride intracellular channel protein 2
- Rho family-interacting cell polarization regulator 2
- Moesin
Sequence:
MNDEDYSTIYDTIQNERTYEVPDQPEENESPHYDDVHEYLRPENDLYATQLNTHEYDFVSVYTIKGEETSLASVQSEDRGYLLPDEIYSELQEAHPGEPQEDRGISMEGLYSSTQDQQLCAAELQENGSVMKEDLPSPSSFTIQHSKAFSTTKYSCYSDAEGLEEKEGAHMNPEIYLFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTPEKYPKLAAKHRESNTAGIDIFSKFSAYIKNTKQQNNAALERGLTKALKKLDDYLNTPLPEEIDANTCGEDKGSRRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVAKRLSRS
Protein: E3 ubiquitin-protein ligase Hakai (EC 2.3.2.27) (M9PBE2)
Organism: Drosophila melanogaster (Fruit fly)
Function: E3 ubiquitin-protein ligase required during early development. E3 ubiquitin-protein ligases mediate ubiquitination of target proteins. Required for epithelial integrity and midgut morphogenesis. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Its function in the WMM complex is unknown.
Subcellular location: Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}.
Interaction partners:
- Protein virilizer
- Pre-mRNA-splicing regulator female-lethal
- N
- Fl
- RNA-binding protein spenito
- N
- DE-cadherin
- YTH domain-containing protein 1
- Adherens junction protein p120
Sequence:
MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIASRPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESVADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR
Protein: Toll-like receptor 5 (G3V6F8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 4
- Toll-like receptor 2
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- High mobility group protein B1
- High mobility group protein B1
- Toll/interleukin-1 receptor domain-containing adapter protein
- T-cell surface glycoprotein CD4
- Toll-like receptor 1
Sequence:
MWCFYSLFSHRIMAYQLDLLIGVVFMASPVLEMSPCFSDGRIALFRGCNLTQIPWVLNTTERLLLSFNYISTVVTTSFPLLEQLLLLELGTQYARLTIGQEAFRNLPNLRILDLGQSQIEVLNPDAFQGLPHLFELRLFDCGLSNAVLRDAYFRNLNSLARLDLSANEIHSLHLHSSFQELSSLSDINFSFNRIFTLCEDELQPLQGRTLSFFGLKSTSLFSRVFVDWEACRNPLRGIRLETLDLSENGWTAAILGNFSHTIQGSHISSLILTYHIMGSGFGFQNIKDPDQSTFASLARSSVLQLDLSHGYIFSLNPRLFETLKDLKKLNLAFNKINKISDYAFHGLDSLQILNLSYNLLGELYNSNFYGLPSIAYLDLQRNHIGIIQDRTFRLLKKLQTLDLRDNALKTIGFIPSVQMVLLGSNKLTHLPHVRFTANFIELSENGLENLSDLYFLLRIPGLQFLILNQNRLSSCSNVDYAPSQNLSLEQLFLAENMLQLAWETGLCWDIFKGLSRLQILYLNNNYLNFLPPGIFNGLVALRMLSLSANRLTMLSPGSLPANLEILDISRNQLFSPDPGLFSSLRALDITHNEFICDCELSTFIVWLNQTNVTLFGSPADVYCMYPNSLLGSSLYNISTKDCDEEEAVRSLNFSLFILCTVTLTLFLVITLIVTKFRGICFLCFKTIQKLMFKGKFRNPEPSAYRYDAYFCFSSKDFEWAQNALLKHLDAQYSSQNRLRLCFEERDFIPGENHISNIQAAVWGSRKTVCLVSRHFLKDGWCLEAFRYAQSRCLSDLKRVLIVVVVGSLPQYQLMRHETIRGFLQKQQYLRWPEDLQDVDWFLDKLSGCILKEEKGKKRSSPIQLRTIRTVS
Protein: Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (MOCO1-B) (Molybdenum cofactor synthesis protein 2 large subunit) (Molybdenum cofactor synthesis protein 2B) (MOCS2B) (Molybdopterin-synthase large subunit) (MPT synthase large subunit) (O96007)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:15073332}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase MOCS3
- Molybdenum cofactor biosynthesis protein 1
- Gephyrin
- Sulfite oxidase, mitochondrial
- SAGA-associated factor 29
- Aldehyde oxidase
- Thiosulfate sulfurtransferase
- Mitochondrial amidoxime reducing component 2
- 3-mercaptopyruvate sulfurtransferase
- Thiosulfate:glutathione sulfurtransferase
Sequence:
MSSLEISSSCFSLETKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVISPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKWPVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPIWKKEIYEESSTWKGNKECFWASNS
Protein: Uncharacterized protein (Q585A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GST N-terminal domain-containing protein
- 50S ribosomal protein L13, putative
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- KOW domain-containing protein
- Large ribosomal subunit protein uL3m
- Ribosomal protein L11, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S25
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S26
Sequence:
MWSKVFTPLLTHRLTPAEKFPQLQLRVGQQRRVTCGRQLSIPLSSFDSHSLDFARREIEPGSVVELRDADHRKLLALAFYEPALLRVDIFHHTPKVVTDLPRISEDFFVNRVKEAWGRRQSVFRHVRTGSTNAYRVVNGYADGVPSLYVDLFSSSFARVVATSAGAERIVPAVTELLRQHGVEEVLLDTPHLKDHEKLTLITPTITLPETYMENGASNMWLPRDEYPTTSSNRWLINTAHRRIRAVLRDLCHGKRVLCVNDRGGAAALQAVMTAKSVVFAESDESLLNRVRENLVANHASAVFNTCETTNSPIEELSMRQQDVVFLEHRFDTLSSPEQWQNLLKVMLFRGVCGKGSIVVVAQEVALLGMHDYVASGGGVAASVVRATRSEMFNVFNRVTAEHGLRARLLRFFGPSIDYPTLPAVEAGCYSYAFLLELAS
Protein: Uncharacterized protein (Q388G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEEVQRRSSAIPTSQGIANAVPVPKKNPYLLRIATCYAHIPMGFREFVLAGPLLLLALGIAYFAPTLAPMDKLTQGLQPNTAPMSSYRLEPIHNEKGELKGYRRIFIKQDKEAKTSHES
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (J3KPD6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
LGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
Protein: DASH complex subunit ASK1 (Associated with spindles and kinetochores protein 1) (Outer kinetochore protein ASK1) (P35734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25236177}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17620411, ECO:0000269|PubMed:18079178, ECO:0000269|PubMed:25236177}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25236177}. Chromosome {ECO:0000269|PubMed:36701236}. Note=Associates with the mitotic spindle and the kinetochore (PubMed:14562095, PubMed:17620411, PubMed:25236177). Localizes to microtubule plus-ends (PubMed:17620411). Associates with origin of replication (ORI) sites during interphase (PubMed:36701236). {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17620411, ECO:0000269|PubMed:25236177, ECO:0000269|PubMed:36701236}.
Interaction partners:
- DASH complex subunit DAD2
- DASH complex subunit SPC34
- DASH complex subunit DAM1
- DASH complex subunit DAD1
- DASH complex subunit SPC19
- DASH complex subunit DAD3
- DASH complex subunit DAD4
- DASH complex subunit DUO1
- DASH complex subunit HSK3
- Spindle pole body component SPC98
Sequence:
MDSASKEETLEKLDQEITVNLQKIDSNLSFCFHKITQDIIPHVATYSEICERIMDSTEWLGTMFQETGLVNLQANAAAPVGNAPVKSLVSNNVGIFPTSAEEASRQSQTDNGPNEADSAVHVNRDVHSMFNNDSIDDFHTANITSTGQILKLPDSSDEDTGSEAVPSREQTDLTGEGHGGADDEQDESTIQRQSRKRKISLLLQQQYGSSSSMVPSPIVPNKMRKQLAHEEHINNDGDNDDENSNNIESSPLKQGHHHPKGQADDNNEGPDEEESTKEVPKPGTIIHFSTNR
Protein: Kinase (EC 2.7.-.-) (Q38DG0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLNICQNLSSVAKPDLIVVSGHKCNIQRGPQTSIGTPTITKRVTAWEALIYLEMLLAEDEAFAILATFVPPLVALLPPENFASDNWVYVHDPASRPLLKSIFAQLKQMSADTHGYNEVMDTTRWEIILVDVTATFHKPCVLDIKLGYVRHSPHTLPDKVERIHKRQLRRSQPIRFCGAHHQFCRQNNDIGECFELEEFTKDMGYALETEESHRRALRSFFTTASLMTTSNTNETTIIDDRHAMARSRCCRQRVQKLVDFLKGHLGQMLLERIAFVSASLLIVYDATGCCGRNVTVSEGINSMNDMVNVYLIDFSRSGDRRLHFPEEVVGFVQGLEKIIFLLS
Protein: Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2) (O35632)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Beta-glucuronidase
- Alpha-L-iduronidase
- Arylsulfatase B
- CD44 antigen
- Hyaluronan mediated motility receptor
- Hyaluronan synthase 2
- Lymphatic vessel endothelial hyaluronic acid receptor 1
- Hyaluronan synthase 1
- Transforming growth factor beta-1 proprotein
- Hyaluronan synthase 3
Sequence:
MRAGLGPIITLALVLEVAWAGELKPTAPPIFTGRPFVVAWNVPTQECAPRHKVPLDLRAFDVKATPNEGFFNQNITTFYYDRLGLYPRFDAAGTSVHGGVPQNGSLCAHLPMLKESVERYIQTQEPGGLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPSDRVMKQAQYEFEFAARQFMLNTLRYVKAVRPQHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSVHSRNFVSFRVREALRVAHTHHANHALPVYVFTRPTYTRGLTGLSQVDLISTIGESAALGSAGVIFWGDSEDASSMETCQYLKNYLTQLLVPYIVNVSWATQYCSWTQCHGHGRCVRRNPSANTFLHLNASSFRLVPGHTPSEPQLRPEGQLSEADLNYLQKHFRCQCYLGWGGEQCQRNYKGAAGNASRAWAGSHLTSLLGLVAVALTWTL
Protein: Plasmepsin IV (EC 3.4.23.39) (Plasmepsin 4) (Q17SB3)
Organism: Plasmodium falciparum (isolate HB3)
Function: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Vacuole lumen {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:12850260}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:11782538, ECO:0000269|PubMed:12850260}.
Interaction partners:
Sequence:
MALTVKEEEFSNTLIKNASAFDRLKLGNLKNLKIQKKLQFLYLILFVLITGVFFFFLIGNFYSHRKLYQVIKNTKHTTIGFKIDRPHDKVLSSVLKNKLSTYVKESFKFFKSGYAQKGYLGSENDSIELDDVANLMFYGEGQIGTNKQPFMFIFDTGSANLWVPSVNCDSIGCSTKHLYDASASKSYEKDGTKVEISYGSGTVRGYFSKDVISLGDLSLPYKFIEVTDADDLEPIYSGSEFDGILGLGWKDLSIGSIDPVVVELKKQNKIDNALFTFYLPVHDKHVGYLTIGGIESDFYEGPLTYEKLNHDLYWQIDLDIHFGKYVMQKANAVVDSGTSTITAPTSFLNKFFTDMNVIKVPFLPLYVTTCDNDDLPTLEFHSRNNKYTLEPEFYMDPLSDIDPALCMLYILPVDIDDNTFILGDPFMRKYFTVFDYEKESVGFAVAKNL
Protein: WD40 repeat-containing protein (Q551N8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DNA damage-binding protein 1
- SNF2-related domain-containing protein
- Cullin-4
- UV-stimulated scaffold protein A C-terminal domain-containing protein
- RING-type domain-containing protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit rpabc1
- DNA-directed RNA polymerase II subunit rpb7
- DNA-directed RNA polymerases I, II, and III subunit rpabc2
- DNA-directed RNA polymerases I, II, and III subunit rpabc5
Sequence:
MNKFLLKRELGICNERREIIDEIKRSIRHLDLSVYKQIINYNKGPINHLDIDVAENRYLLSVSGDGIIQIYDLFENLLNNKKNNEIKTEFQPILKINRKSNNNNNNNNSNSEGILLKGISSVQWYPIDTGIFFIGGVNGNVEVWDTNLGQVSQTFYLENCVNSISYSQVNCTNLLIAAATTDPKVRLCDMRTNSSVHCLTGHRESVLSIKWSPFSPNLIATASKDKTIRLWDIRRGDTFLFALDQYNGSGIGIGVGGGSGGESNDDVGNDIGGGNKNDLKQSKRYRQKLHKPKSLQTSSSSIIEKRNIGGGGGGIGGSANLTLKKEVPTAHNGTITSIAWTPDGNYLVSTGADSKIRLWDIQKGGANTMINYPNAHNVHKIPNQICLSTNGQYLFHPNGRAIHVYETATGNLVRQLKGHFEKVNCCVFNHCDQALISGSNDRLTLYWDNSNDDQIDDQQFLNEEKQNNQNNDDDNNNFQVTTNTTTKTSTTTTTSTTISPPTTLEDVDNWSDD
Protein: Transcriptional regulator (A4FQD5)
Organism: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Interaction partners:
- Circadian input-output histidine kinase CikA
- NADH-quinone oxidoreductase chain F
- Mycothiol acetyltransferase
Sequence:
MSSELLLLTSDRDCEAVLPALGLLPHRVRVLPPEPGAILSAGTHDVVLVDARTDLAGARDLCRVLAVGDAPVLAVVNEGGLVTVSAEWGVDDILLPTAGPAEIDARLRLLTTRRGADAGEGDGMLTVGDLVIEESTYTARLKGRALELTYKEFELLKYLAQHAGRVFTRAQLLQEVWGYDFFGGTRTVDVHVRRLRAKLGPEYDSMIGTVRNVGYKFVRPSRSSQPASPIVAEERQDAATQADAPAQRSAESAVVR
Protein: Regulator of gene activity (Protein regena) (CCR4-NOT transcription complex subunit 2 homolog) (CNOT2) (Not2) (Q94547)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Essential for viability. Acts as a suppressor of position effect variegation (PEV) at the white locus and regulates the expression of several unrelated genes. Plays a role in germline stem cell differentiation in the ovaries.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23303381}.
Interaction partners:
- Not1, isoform H
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 9
- poly
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 10
- CCR4-NOT transcription complex subunit 4
- Protein associated with topo II related - 1, isoform A
- poly
- FI22161p1
Sequence:
MANLNFQQPPRSIANAALAGRTTGGFGGSSLAGHVTPTSGMFQTDFANSYPGTANYGQAPQQQQQQQQQPQLSPNRNAQLSVGGPAISSGNRNANLFGQRQFVERRAMQGLGSGPMSNMGNFMQTGRGGYGTGGGGGGPLNNFHVFGGGGGSDTSTPALLDPTEFPSLTNARGQNDQTLPQSNPLQPPGSKPYGNFFTSFGMVKQPTSEQSEFTMSNEDFPALPGTQNSDGTTNAVGSVAGTGGSGGASTENHLDGTEKPMNSIVVSGSASGSSGSNVGVVGGNGLGAVGSGIGGLAVGGGGGAGSSGGGGVGGNAASGVVGGSHVGLVGSNSGIGGVNSVPNSNAMMGVGGGLGSGSGSSGSGAGGEHLNDNSSNDKLVKSGVQTSPDGKVTNIPATMVNNQFGMVGLLTFIRAAETDPNLVTLSLGTDLTGLGLNLNSQESLHTTFAGPFVAQPCRAQDVEFNVPPEYLINFAIRDKLTAPVLKKLQEDLLFFLFYTNIGDMMQLMAAAELHSREWRYHVEEKIWITRIPGIDQYEKNGTKERGTFYYFDAQSWKRLSKVFQIDPEKLDKCPNISAFMNGQSV