wanglab/gogpt-training-data huggingface dataset:
Protein: DDB1- and CUL4-associated factor 16 (Q9NXF7)
Organism: Homo sapiens (Human)
Function: Functions as a substrate recognition component for CUL4-DDB1 E3 ubiquitin-protein ligase complex, which mediates ubiquitination and proteasome-dependent degradation of nuclear proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:31209349}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- DDB1- and CUL4-associated factor 15
- Protein cereblon
- Cullin-4B
- DDB1- and CUL4-associated factor 5
- DET1 homolog
- DET1- and DDB1-associated protein 1
- DDB1- and CUL4-associated factor 12
- Denticleless protein homolog
Sequence:
MGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKCLLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLASCGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCCCGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL
Protein: Prostaglandin E2 receptor EP4 subtype (Prostanoid EP4 receptor) (C0HB24)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSGMNNGTMTSGPREPTIPVIMFIFGVVGNVIAIVVLRKSRKEQKETTFYTLVCGLAVTDLLGTLLASPVTIATYVQGKWPGGESLCQYSGFILLFFFLVGLSIICAMSIERYLAINHAYFYNHYVDQRLAALTLAGIYISNVLFCALPAMGLGKVNKQFPGTWCFIDWRTNDSAHAAFSYMYAGVSSFLILATVICNVLVCGALIMMHKRFIRRTSLGTDQGGRIADLRRRRSFQRLAGAEIQMVILLIATSVVVLICSIPLVLRIFVNQLSRVEFDARSTPIEKNPDLHAIRIASVNPILDPWIYILLRKTVLLKLVEKIKYLFCRLGSHGRGSGVSGQFCCGGESHQNSSIVSLDSPSLVSRELKDVISTSQTFLYLPEGTKGGLGGFRGTGGEGRPILPAVERSLLQDQQTQAGKGMQKDPKKGPRISMRSEGTVDPSRLNRVQLDRKDKTLHVTFTDETLNLQEKCI
Protein: Proteinase A (Q59U59)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Carboxypeptidase
- Proteinase B
Sequence:
MQLSLSALTTVALALTSSLVDAKAHSIKLSKLSNEETLDASNFQEYTNSLANKYLNLFNTAHGNPSNFGLQHVLTNQEAEIPFVTPKKGGKYDAPLTNYLNAQYFTEIQIGTPGQPFKVILDTGSSNLWVPSQDCTSLACFLHAKYDHDASSTYKVNGSEFSIQYGSGSMEGYISQDVLTIGDLVIPGQDFAEATSEPGLAFAFGKFDGILGLAYDTISVNHIVPPIYNAINQGLLEKPQFGFYLGSTDKDENDGGLATFGGYDASLFQGKITWLPIRRKAYWEVLFEGIGLGDEYAELHKTGAAIDTGTSLITLPSSLAEIINAKIGATKSWSGQYQVDCAKRDSLPDLTLTFAGYNFTLTPYDYILEVSGSCISVFTPMDFPQPIGDLAIVGDAFLRKYYSIYDLDKNAVGLAPSKV
Protein: Centrosomal protein of 104 kDa (Cep104) (O60308)
Organism: Homo sapiens (Human)
Function: Required for ciliogenesis and for structural integrity at the ciliary tip.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:23970417, ECO:0000269|PubMed:36606424}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, spindle pole. Note=In interphase non-ciliated cells, localizes to the distal ends of both the mother and daughter centrioles. In ciliated cells, present at the distal end of the daughter centriole, but not on the mother centriole, and at the tip of primary cilium. Localization at the ciliary tip is also observed in motile cilia. Throughout S phase, associated with both mother and daughter centrioles in each centrosome. During metaphase and telophase, present at both spindle poles. {ECO:0000269|PubMed:23970417}.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 97 kDa
- Leucine-rich repeat-containing protein 47
Sequence:
MPHKIGFVVVSSSGHEDGFSARELMIHAPTVSGWRSPRFCQFPQEIVLQMVERCRIRKLQLLAHQYMISSKIEFYISESLPEYFAPYQAERFRRLGYVSLCDNEKTGCKARELKSVYVDAVGQFLKLIFHQNHVNKYNIYNQVALVAINIIGDPADFSDESNTASREKLIDHYLGHNSEDPALEGTYARKSDYISPLDDLAFDMYQDPEVAQIIRKLDERKREAVQKERYDYAKKLKQAIADLQKVGERLGRYEVEKRCAVEKEDYDLAKEKKQQMEQYRAEVYEQLELHSLLDAELMRRPFDLPLQPLARSGSPCHQKPMPSLPQLEERGTENQFAEPFLQEKPSSYSLTISPQHSAVDPLLPATDPHPKINAESLPYDERPLPAIRKHYGEAVVEPEMSNADISDARRGGMLGEPEPLTEKALREASSAIDVLGETLVAEAYCKTWSYREDALLALSKKLMEMPVGTPKEDLKNTLRASVFLVRRAIKDIVTSVFQASLKLLKMIITQYIPKHKLSKLETAHCVERTIPVLLTRTGDSSARLRVTAANFIQEMALFKEVKSLQIIPSYLVQPLKANSSVHLAMSQMGLLARLLKDLGTGSSGFTIDNVMKFSVSALEHRVYEVRETAVRIILDMYRQHQASILEYLPPDDSNTRRNILYKTIFEGFAKIDGRATDAEMRARRKAATEEAEKQKKEEIKALQGQLAALKEIQAEVQEKESDAVKPKNQDIQGGKAAPAEALGIPDEHYLDNLCIFCGERSESFTEEGLDLHYWKHCLMLTRCDHCKQVVEISSLTEHLLTECDKKDGFGKCYRCSEAVFKEELPRHIKHKDCNPAKPEKLANRCPLCHENFSPGEEAWKAHLMGPAGCTMNLRKTHILQKAPALQPGKSSAVAASGPLGSKAGSKIPTPKGGLSKSSSRTYAKR
Protein: Transient receptor potential protein (P19334)
Organism: Drosophila melanogaster (Fruit fly)
Function: A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Ca(2+) influx may then feed back and inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in the light response, though it is unclear whether as heteromultimers or as distinct units, and are activated by fatty acids and metabolic stress. Also required for olfactory adaptation and may be involved in olfactory system development.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10995445, ECO:0000305|PubMed:2516726, ECO:0000305|PubMed:7751943, ECO:0000305|PubMed:9010208}; Multi-pass membrane protein {ECO:0000305|PubMed:10995445, ECO:0000305|PubMed:2516726, ECO:0000305|PubMed:7751943, ECO:0000305|PubMed:9010208}. Cell projection, rhabdomere membrane {ECO:0000305|PubMed:10995445, ECO:0000305|PubMed:2516726, ECO:0000305|PubMed:7751943, ECO:0000305|PubMed:9010208}; Multi-pass membrane protein {ECO:0000305|PubMed:10995445, ECO:0000305|PubMed:2516726, ECO:0000305|PubMed:7751943, ECO:0000305|PubMed:9010208}. Note=Localized on plasma membrane loops found at the base of the rhabdomere, in close proximity to the calcium stores.
Interaction partners:
- Inactivation-no-after-potential D protein
- Protein kinase C, eye isozyme
- Transient-receptor-potential-like protein
- Opsin Rh1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Calmodulin
- Neither inactivation nor afterpotential protein C
- Protein kinase C, brain isozyme
- Transient receptor potential-gamma protein
- Opsin Rh3
Sequence:
MGSNTESDAEKALGSRLDYDLMMAEEYILSDVEKNFILSCERGDLPGVKKILEEYQGTDKFNINCTDPMNRSALISAIENENFDLMVILLEHNIEVGDALLHAISEEYVEAVEELLQWEETNHKEGQPYSWEAVDRSKSTFTVDITPLILAAHRNNYEILKILLDRGATLPMPHDVKCGCDECVTSQMTDSLRHSQSRINAYRALSASSLIALSSRDPVLTAFQLSWELKRLQAMESEFRAEYTEMRQMVQDFGTSLLDHARTSMELEVMLNFNHEPSHDIWCLGQRQTLERLKLAIRYKQKTFVAHPNVQQLLAAIWYDGLPGFRRKQASQQLMDVVKLGCSFPIYSLKYILAPDSEGAKFMRKPFVKFITHSCSYMFFLMLLGAASLRVVQITFELLAFPWMLTMLEDWRKHERGSLPGPIELAIITYIMALIFEELKSLYSDGLFEYIMDLWNIVDYISNMFYVTWILCRATAWVIVHRDLWFRGIDPYFPREHWHPFDPMLLSEGAFAAGMVFSYLKLVHIFSINPHLGPLQVSLGRMIIDIIKFFFIYTLVLFAFGCGLNQLLWYYAELEKNKCYHLHPDVADFDDQEKACTIWRRFSNLFETSQSLFWASFGLVDLVSFDLAGIKSFTRFWALLMFGSYSVINIIVLLNMLIAMMSNSYQIISERADTEWKFARSQLWMSYFEDGGTIPPPFNLCPNMKMLRKTLGRKRPSRTKSFMRKSMERAQTLHDKVMKLLVRRYITAEQRRRDDYGITEDDIIEVRQDISSLRFELLEIFTNNNWDVPDIEKKSQGVARTTKGKVMERRILKDFQIGFVENLKQEMSESESGRDIFSSLAKVIGRKKTQKGDKDWNAIARKNTFASDPIGSKRSSMQRHSQRSLRRKIIEQANEGLQMNQTQLIEFNPNLGDVTRATRVAYVKFMRKKMAADEVSLADDEGAPNGEGEKKPLDASGSKKSITSGGTGGGASMLAAAALRASVKNVDEKSGADGKPGTMGKPTDDKKAGDDKDKQQPPKDSKPSAGGPKPGDQKPTPGAGAPKPQAAGTISKPGESQKKDAPAPPTKPGDTKPAAPKPGESAKPEAAAKKEESSKTEASKPAATNGAAKSAAPSAPSDAKPDSKLKPGAAGAPEATKATNGASKPDEKKSGPEEPKKAAGDSKPGDDAKDKDKKPGDDKDKKPGDDKDKKPADNNDKKPADDKDKKPGDDKDKKPGDDKDKKPSDDKDKKPADDKDKKPAAAPLKPAIKVGQSSAAAGGERGKSTVTGRMISGWL
Protein: Krueppel homolog 2 (Protein Kr-h2) (Q9V447)
Organism: Drosophila melanogaster (Fruit fly)
Function: Member of the dosage-dependent hierarchy effective upon white gene expression.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Krueppel homolog 1
- Surfeit locus protein 4 homolog
- Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
Sequence:
MSAPTDQPPRSEGAQTNSSERSSQQQEQPQQSQSQNVPAKLLQHFQTNRIDSALWALRLLVIFFTVSYVLPIFTSQQSAFSKVMLANAAISALRLHQRLPAFAFSREFLARLFAEDSCHYMMYSLIFFNIRPSLLVLIPVLLYSVLHASSYSLKLLDLIGQNSWWGARFIISIVEFQAANILKATAFCEIFIMPYAIVLAFMNHAGLMTPVIYYHYLVMRYSSRRNPYPRNAFAELRITFEALAARSPPAFAKIIRGGIGFVNRLAPQLQPAAAQE
Protein: Uncoordinated 115b, isoform C (Q8INN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trio, isoform A
- Protein hu-li tai shao
- Netrin receptor unc-5
Sequence:
MYILIYISIPKHPQTDKTRPIYPSTLGTELRTELGKTGQGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFGVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMYIRSRTPSFNGSLYSSSRKHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNAIHSYRSPPKPGYGFKTTTLPYIRNGFSSDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSIISCANAKL
Protein: Inositol polyphosphate 5-phosphatase (EC 3.1.3.-) (Ciliary localization protein 1) (P34370)
Organism: Caenorhabditis elegans
Function: Dephosphorylates a number of phosphatidylinositols. Controls the cellular levels and subcellular distribution of phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has a role in sperm activation and motility. Influences the localization of the transient receptor potential polycystin (TRPP) complex proteins lov-1 and pkd-2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19781942}. Note=Observed in reticular structures.
Interaction partners:
- Probable type I inositol 1,4,5-trisphosphate 5-phosphatase
- BTB and MATH domain-containing protein 42
- Pre-mRNA-processing factor 19
Sequence:
MDWKITIFTYNLAMKASDSEAVHNMLNGMIDDHTHLVAIGLQEVAHSETIGGAVLTWATTIASWMNTNGRMVLLAKTFQATNQVLIFGRKQLIGQIKRIDYRFQRNTMGGLTGHKGSIGVRLQLASPYSIVFVDSHFIHGPENYGKRVEQYHTNRNCSFPEDKSVRAAFWFGDFNFRVEEDVNTVIRKIKNGTHLELLDTREQLKRALVERDAFIGFHEQPVTFEPTYRVTVGTTEQDGKRVPSWTDRILYKGDGITGLSYTNNKKAVASDHLPVVAMFRVTAPAAPKPQWEVIFEHLPTWYTSIPLVGRFQVNELYYKENGSYRDWIGVFPSSINDCTTATNWIYAATCFEQVIEGSKFLACEFNNIPAGNYRLGYFSCHLHCLVGLSKVFQIVEQP
Protein: V-type proton ATPase subunit B1 (V-ATPase subunit B1) (V-ATPase 57 kDa subunit) (Vacuolar H(+)-ATPase subunit B isoform 1) (Vacuolar proton pump subunit B1) (P11574)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d1
- Vacuolar ATP synthase catalytic subunit-related / V-ATPase-related / vacuolar proton pump-like protein
- V-type proton ATPase subunit c5
- V-type proton ATPase subunit c''1
Sequence:
MGTNDLDIEEGTLEIGMEYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGSTRRGQVLEVDGEKAVVQVFEGTSGIDNKFTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLVKRLEKTVDLLEDHGEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVMQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFYSRDSTS
Protein: Uncharacterized protein C24B10.19c (Q9P7I7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C16E8.12c
- Meiotically up-regulated gene 165 protein
- Histone deacetylase clr6
- Transcriptional regulatory protein sds3
- Paired amphipathic helix protein pst1
- Transcriptional regulatory protein rxt3
- SWIRM domain-containing protein laf2
- Paired amphipathic helix protein pst3
- SWIRM domain-containing protein laf1
- RbAp48-related WD40 repeat-containing protein prw1
Sequence:
MVKSCQKKPDIDEFFSFLQSAFHPLQTEELDTFVRNIFEYDDRGRLYNCLLTLVPYERLPIDAEDLSSRKTYARPVLIRQYRSLRFANKEENICRLTPNSAFVPVRDSAVASISTSKVQDFNSYATLTEAQKKTATPVEEKNFLNQIVIQCLDSLETDVETNTTHATLLAVDPTWLIRVSQHTCDRKAVANLCIQYGSQIFYDPSFRNAYELWSNPSVLLAFLKAQRVLVVSDIFTSSTLRSTQGTPMSFPNLALESADNVENVSKPINPRMERFSSEVKSSSILKQQIAAVVEKINYDIRPQRDQIPEENIVPRISYLTSTTTSTKSSPVPESTTTNTTEVLKELNDIQENKSRKNVEKATAATEEMLRGHHKPVEGTTATSEKESIKEEVDLEVNGDGKVEAEERIELESSDSEKELSELIDFLKREHPPEDTPEKRVKIKRIRTLLDTWQQEWRILNKAISNAESNSGRGQNSKTKTTSVNLSRNKRTRT
Protein: Probable endoribonuclease HigB1 (EC 3.1.-.-) (Toxin HigB1) (P9WJA5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endoribonuclease; also degrades E.coli and M-smegmatis tmRNA. Its toxic effect is neutralized by coexpression with antitoxin HigA. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system.
Interaction partners:
- Antitoxin HigA1
- SecB-like chaperone Rv1957
- Toxin RelE
- Putative toxin HigB2
Sequence:
MPPPDPAAMGTWKFFRASVDGRPVFKKEFDKLPDQARAALIVLMQRYLVGDLAAGSIKPIRGDILELRWHEANNHFRVLFFRWGQHPVALTAFYKNQQKTPKTKIETALDRQKIWKRAFGDTPPI
Protein: Metal-independent phosphoserine phosphatase (iPSP) (EC 3.1.3.3) (Phosphoglycerate mutase-like protein 3) (F4KI56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphoglycerate mutase-like protein lacking PGM activity, but having a low metal-independent phosphoserine phosphatase activity in vitro. May be involved in serine biosynthesis.
Interaction partners:
- Thioredoxin-like 3-2, chloroplastic
- Transmembrane protein
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, chloroplastic
- Cofactor-independent phosphoglycerate mutase
- F-box/kelch-repeat protein At5g49000
- Enolase 1, chloroplastic
- Phosphoglycerate mutase-like protein 2
- Cytosolic enolase 3
- Bifunctional enolase 2/transcriptional activator
Sequence:
MGHEWIDAEREFKWSEDVKVESEVTEIVLVRHGETTWNAAGRIQGQIESDLNEVGLKQAVAIAERLGKEERPVAVYSSDLKRAKDTALMIAKTCFCPEVIEVPDLKERHVGSLQGLYWKEGAEKEPEAYSAFFSSQNDLEIPGGGESFDQLADRSMDALEQIAKKHKGERVIVVTHGGVLRAIYLRITQASSAGKLLNASVNVVHLRDQKWIIDSWSDVSHLSSVGFLQRGFDGDAKP
Protein: Altered inheritance of mitochondria protein 20 (P40451)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell cycle progression and surviving DNA damage.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Sugar utilization regulatory protein IMP2
Sequence:
MGNVSVAVGTAVGIPIAVGVIIALIFWCKLQRRYKKEEIRDADLEKMVMEEVAVSVYDGFKAEINSSSEASTINEKEANQDLKPCQEKTAKAGYTPAYRRQLNASMGTLRPKKQSTAYTNVPVIFSGEKVNYGMVRDPSYSFMYPLTLSRKETSSLRSASTSNLSSSTENTALHEEIKLDDPYENDFTNYTVNKREFIDSLRPH
Protein: U18-myrmicitoxin-Mri1a (U18-MYRTX-Mri1a) (A0A6G9KJM3)
Organism: Manica rubida (European giant red ant)
Subcellular location: Secreted {ECO:0000269|PubMed:32182430}.
Interaction partners:
Sequence:
MKNNYNRINTFIVYLMVTFSLISIISITECTPNHDPCPPQYAEALCLNGGTCFSVTIMGSDNYNCICAPGFRGWRCQEKDLDHPVNQ
Protein: Autophagy protein 5 (APG5-like) (Apoptosis-specific protein) (Q9H1Y0)
Organism: Homo sapiens (Human)
Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17709747}. Preautophagosomal structure membrane; Peripheral membrane protein. Note=Colocalizes with nonmuscle actin. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed (By similarity). Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- Ubiquitin-like-conjugating enzyme ATG3
- Tectonin beta-propeller repeat-containing protein 1
- GABA type A receptor associated protein like 1
- Ubiquitin-like protein ATG12
- Autophagy-related protein 16-1
- Ubiquitin-like modifier-activating enzyme ATG7
- Protein Atg16l2
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Mitochondrial antiviral-signaling protein
Sequence:
MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAIEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGEKKNQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
Protein: Berberine bridge enzyme-like 16 (AtBBE-like 16) (EC 1.1.1.-) (O64745)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
- MACPF domain-containing protein CAD1
- Vesicle-associated protein 1-4
- Similarity to disease resistance protein domain family protein)
- Defensin-like protein 127
- Putative defensin-like protein 126
- Alkaline-phosphatase-like family protein
- Protein CONTINUOUS VASCULAR RING 1
- Heavy metal-associated isoprenylated plant protein 22
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MKFWSRPLTFLIIIIYLIIQQVNSSPPSLSIPEHFLRCLDTQPSDHGSPNSRTAVIPTNSSFSTNLMNGVRNLRFASVSTRKPEVIVAAVTETHIRATISCCKLLNLELRIRSGGHDYEGFSYTSPVPFVILDMYNFNKIDINMKDETVWIQSGASLGQLYYNIASKSKVHAFPAGVCPKVGAGGHFSGGGFGNLMRKYGLSIDHIIDAQIMDANGKVYRNRQAMGEDVFWAIRGGGGGSYGVILAWKIKLVRVPEKVTVFKLERTVREGAVDLVHKWQQVAPVIDRDLFIRLEIKPINRKISKGKTIKVSFIGMFLGLPERLLNITKQSFPELHLTKEDCMVKKWIESSVFWANYPEKAPIELLLKRVSTNEYYWKRTSDFVQAPISKQGLAKIFQTMIDHSPLPRRVWMQWNPWGGKMAEIASDATAFVHRGGNVFMIEHFMNWYRPGDELEEKFLAIARSFKEAMAPFVSKNPREAFFNYRDVDIGITTPGYNATYEGAKVYGDSYFKGNYLRLVKIKARFDRTNFFRSQQGIPVLA
Protein: CCAAT/enhancer-binding protein (Q8UVZ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005879}.
Interaction partners:
- Cyclin-dependent kinase 4
- cyclin-dependent kinase
- Cyclin-dependent kinase inhibitor 1
- Peroxisome proliferator-activated receptor gamma
- SI:bY184L24.2.1
- Runt-related transcription factor
- GATA-binding protein 1a.
Sequence:
MEQANLYEVAPRPLMTSLVQNQQNPYIYKDTAGDLSEICENENSIDISAYIDPSAFNDEFLADLFHNSSKQEKLKLASGDYDYHHGANGAPGAPQMYGCLNGYMDSSKLEPIYDSQARMRPVAIKQEPREEDELGDSMPPTYHHSQHHAPHLSYLQHQIAHCAQTTMHLQPGHPTPPPTPVPSPHHQHSHLPGGSMKIGDRGKSKKHVDKNSTEYRLRRERNNIAVRKSRDKAKMRNVETQQKVIELSADNDRLRKRVEHLTRELETLRGIFRQLPDGSFVKAMGNCA
Protein: Choline/ethanolamine kinase (B3GWD5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVSLEVPTESPCISRRAPSEECEIAFSHDDPTLMWKDRTTDCVDLKKVFSKFDSSAPISGEILFRARFLCAKYLGGAWRKVKIEEFRIRAITGGMSNLLFLVELPAHLTPIQMEPEKALLRVHCQSDIDQLLSESVVFTLLSERNLGPKMLGVFPGGRFEQFIPSRALQCLEISKPGLSKLIAPIVARVHTLDAPIPKEPQTLQTARQWLERFKKTPAGERPIEMYLTQAKVPKSDYPSTITVAQLERELNFVEFFLQHSHSPVVFSHNDLQEGNFLLIDGYKLADDGTVLTPDGKPTNDDPLSLIDFEYCSYNYRGFDLGNHFCEYGYDYNEAEAPYYKIHQHYFEVEKERKVFCEAYLDEVYKMRACGDNPHFPSDLVTGDREKDLNKIIEESILFMPVSNIFWVCWSLINAEESSIAFDYGAYGRDRLALYFHQKKNLEKYLSNL
Protein: Non-classical export protein 102 (Q5ANE3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in membrane organization. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient (By similarity). Regulates actin organization and subsequent morphogenesis and pathogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19824013}; Multi-pass membrane protein {ECO:0000255}. Note=Accumulates in membrane domains at eisosomes. {ECO:0000250|UniProtKB:Q12207}.
Interaction partners:
- Lipid-binding protein
- Protein SUR7
Sequence:
MLAIGDVILRAFNFVFLVIALGLTGSLAATTITQHNPQINFAVFAAAFGLLTSSFYGVFAYFVAAFAWPVILFVFDFLNFVFTFAAATAIAAGIRAHSCSNQDYLDDNNIAQGSSGRCRKAQASTAFLYFSTFIFIASAIFSAISLSKGGLFGHSSRPAPRTGVPTMSQV
Protein: Serine/threonine-protein kinase 25 (EC 2.7.11.1) (Ste20-like kinase) (Sterile 20/oxidant stress-response kinase 1) (SOK-1) (Ste20/oxidant stress response kinase 1) (Q9Z2W1)
Organism: Mus musculus (Mouse)
Function: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localizes to the Golgi apparatus. {ECO:0000250}.
Interaction partners:
- Programmed cell death protein 10
- Striatin
- Striatin-interacting protein 1
- Striatin-4
- Serine/threonine-protein kinase 26
- Striatin-3
- Striatin-interacting proteins 2
- Serine/threonine-protein kinase 24
- MOB-like protein phocein
- Suppressor of IKBKE 1
Sequence:
MAHLRGFAHQHSRVDPEELFTKLDRIGKGSFGEVYKGIDNHTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYFGSYLKSTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNNPPTLEGHHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWKSEGHGEESSSEDSDIDGEAEDGEQGPIWTFPPTIRPSPHSKLHKGTALHSSQKPAEPIKRQPRSQCLSTLVRPVFGELKEKHKQSGGSVGALEELENAFSLAEESCPGISDKLMVHLVERVQRFSHSRNHLTSTR
Protein: Cytoadherence linked asexual protein 9 (Q8I2G2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MIIWFIQPTIFYIIFILARNIQCTYKGDNINEIKSILDNDELYNSLSNLENLLLQTLEQDELKIPIMKGDLDKYLNMSNFKILNELNADGAEKPYIIPTSNCSANDIVKYEHTLKTQITLEYKPEISDMLKRKNIVVRTLKIIKFMQTPMSAYKNTNNIKQSLLEMNKLFTNKEKKLNEHTINALRLRDRIFNTNNLTHRSIKKGISTYMPIDTKSDIIDYDDLLFTNHPSIELMENLDKLANYYHIGIFNMIGSHYIAVGHFITLKLALKNYKKYFEIGSLKYLNWQSILKFNQSDRFKVLDLICDESSWYEGQMKRREQYLKNNIFSTSEECSVLEFLIHHMNKYQMELYSKMHKLSLNVQIYLENKHLKEKFLQFMCRSRKECNIYESDRFKQEQEKGIEFHDNNNYKFSQENDPVSKVVDPFNLFTNYFYFIKYYSVFNSDHIIYMHLLNFVGVLNGNNNAYVSSLYLPGYYNAIQLSYKDQVGLKELYQNLVKCVEKCYIRNRKNRSFSHRIASIFRHKKFDSSKCSICEGTLLYINDQSQDKMSMAQKFYIFVTKILKVNNISSFITNMNIYEDYSNYLMHDLNWYTFLFLFRMTTYKDIPNYSISNAMYLNIKDEDDTKRTMVTFQWMPSTIKRMHNYRIRKYVSIYLLEELEKLIDNKLIEKLKKCITFLIHLNAFLQLDFFSYLNETPANLQHPFPISMMIEARFKDWFIQYLTGFFFINYDDANTRYNMPENMKRGTFIPPKYSKWNIHLKRFIDEAFLMYFNQKHALTLFKYHNPYNISNKIMLMRDTFELYTKNYDQLIFGADIMLLRKTFSCTPMSTKVWDRVKYYLHNIIGNPINFYKHGLIYAYTLNKAMLKEVVNDFFVIYKMNKDLFSETSFLQTVYLLFKKIQGTYFSHRRNDDVSMNNIFMFNVEKNYSKMSQADREKEIHESMASRFFAKNLFTVFQMMFVIQISNDVDKLDRIYGKADMLRLSVHDEPFLRFAYAYYGSMYDKLTNVFFPMNIKKPTIQLKYGKTFIMANLYYLCSVLFSMYNLNNLGLLCEYQAIGSANFHSYKKMSQFIDKKFIPLVFYTLKARTEGIIGKEWYKMVFNDFDGKSMANTWPYFGYYMGGNMLYRNILYFPNHLPEELRKQTKGVELQQPEYEPSVHSIDWQVGYAISHGLSLSFFTFGMMKAYAYFENVIFFLRNSIRIFDRFYSILENYVCMYIKRLFNKLTVDKLLKAMSRAYTSTKKEGAYEEAMVSRVRNKENVVQEVQEDKGTDITPLPTFDIMDSKQNTNYMYNDNEDYFDDLDDNEQFLNSKDLLYYDDGIDRTKRYELIPLQRYRYDPF