wanglab/gogpt-training-data huggingface dataset:
Protein: Rieske domain-containing protein (Q57Z95)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGEPVRIHVGSAHLFKDKSRQLIKCGERNIVVCLYNNQFYAIDNACYHHGGPLLEGDIEDMGGHPCIVCPWHQYRITLDTGEGLYWALQMTPSGTIDRNGKQVVRSKGRKQRIHTVTVEHGEVYVTLNTSGPALDSDAYAEMALANKDRPMTKPISNDGIRSKTFHSSLRSGQVLEMLGSSGSQLLPCGFTQGKVVYCARTEHVCDDTKEFFFSSCRGVLDLFPQPGQFVDLELPIRGPSGRFLRRRWTVVETDKEGCLFTLIIKEAKGSRGGSTWMLKNGLQQRFPLLLVGGRFTLSHNIRRLLELEGRVVVLSAGIGLTAPYALLKRLFDGSQSPVPTDEGNIAMMQVVHLHVDGKESLLPRCDDLVRWCSHQGDRFMYRFHCYLTKQDPSAMSNHLLLPHTTCGRRPTLWDVEEFMGEFVRTSPPLAFVSGPTEFVTMGKNALLSLGVLESDVVTDDPDNLGP
Protein: Carboxypeptidase Q (EC 3.4.17.-) (Lysosomal dipeptidase) (Plasma glutamate carboxypeptidase) (Q9Y646)
Organism: Homo sapiens (Human)
Function: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:10206990}. Golgi apparatus {ECO:0000269|PubMed:10206990}. Lysosome {ECO:0000250}. Secreted {ECO:0000269|PubMed:10206990}. Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. {ECO:0000250}.
Interaction partners:
Sequence:
MKFLIFAFFGGVHLLSLCSGKAICKNGISKRTFEEIKEEIASCGDVAKAIINLAVYGKAQNRSYERLALLVDTVGPRLSGSKNLEKAIQIMYQNLQQDGLEKVHLEPVRIPHWERGEESAVMLEPRIHKIAILGLGSSIGTPPEGITAEVLVVTSFDELQRRASEARGKIVVYNQPYINYSRTVQYRTQGAVEAAKVGALASLIRSVASFSIYSPHTGIQEYQDGVPKIPTACITVEDAEMMSRMASHGIKIVIQLKMGAKTYPDTDSFNTVAEITGSKYPEQVVLVSGHLDSWDVGQGAMDDGGGAFISWEALSLIKDLGLRPKRTLRLVLWTAEEQGGVGAFQYYQLHKVNISNYSLVMESDAGTFLPTGLQFTGSEKARAIMEEVMSLLQPLNITQVLSHGEGTDINFWIQAGVPGASLLDDLYKYFFFHHSHGDTMTVMDPKQMNVAAAVWAVVSYVVADMEEMLPRS
Protein: 3-ketosteroid oxygenase (EC 1.14.14.-) (Cytochrome P450 daf-9) (DAF-9) (H2KYS3)
Organism: Caenorhabditis elegans
Function: Converts the 3-keto steroids 4-cholesten-3-one and lathosterone into the carboxylic metabolites 3-keto-4-cholestenate (Delta(4)-dafachronic acid, Delta(4)-DA) and 3-keto-7,(5a)-cholestenate (Delta(7)-dafachronic acid, Delta(7)-DA) respectively, by catalyzing successive oxidations at C-26. Dafachronic acids bind directly to the nuclear hormone receptor (NHR) DAF-12, suppressing dauer formation and inducing reproductive growth. In a non-cell autonomous manner, negatively regulates body wall muscle arm extensions to motor neurons probably by preventing daf-12 isoform b activation. May be involved in thermotolerance.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to dendrite-like structure in XXXL/R cells. {ECO:0000269|PubMed:12783794}.
Interaction partners:
- Nuclear hormone receptor family member daf-12
- Cholesterol 7-desaturase
- 3beta-hydroxysteroid dehydrogenase/Delta
- 3beta-hydroxysteroid dehydrogenase dhs-16
- Daf-12-interacting protein 1
- Sterol 4-C-methyltransferase strm-1
- Insulin-like receptor
- Forkhead box protein O
- FERM domain-containing protein
- Dauer larva development regulatory growth factor daf-7
Sequence:
MHLENRVLSSVLDYASKFYKRMSSLVFFSANSIQVQMNISQSSWIKCRDWMAFALSHHIIMGIYLLILRNFLPQVVPDFEWQHYFMRVFIVHIIYIIISYFIRITRYPPGPPPMAVFGNSPFVNILTPEQTFLEYREIYGPIFTLHLSQPTIILAEYKTIQEALVKNGQQTSGRSSAESFVLFTGDRLNGDGVILAMRQKWKDMRHEISRFMNKWYGAPMDELVLHHTRCLEQELAKIAETKSLIDLRDPLAGAIANVIQQITIGRNYMYQDQEFQTQLRDINAVVKEIMTAEVFFVNCYPWLRYLPEGILRKWTNYKRSGFRLQQWFRTILEEHHVNRHQGDFMSHMIDLQESKQEQFRDLSIILTCGDMWTGGMETTVTTLRWGIIYLLNNPEVQAKCQMEILDVFGNDIPDMGKMNQTPYVRATLSEIQRLANVLPWAIPHKTIEECNIGGYDIPVNTEIIPALGAVLFDPNVFESPKQFKPERFLDEEGKYRVMEEFRPFGLGPRVCLGERIARTELYLIFASLLQNFRFYLNRGDPIPVAERVIGGITAPPKPYATRVEYLGNRLIN
Protein: Conserved oligomeric Golgi complex subunit 3 (COG complex subunit 3) (Component of oligomeric Golgi complex 3) (Q9Y7Z4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis- Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes at the barrier septum. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 5
- Vacuolar protein sorting-associated protein 52
- Protein transport protein tip20
- Protein transport protein sec20
- Vacuolar protein sorting-associated protein 54
Sequence:
MFDQLEFYPAVNYEDNETQNDIKLPEVAKLENIETVHSISKERRDSLTEILNDSSSLPARPFSLPNPNNSTVEKQSLFPFEEKMNPIWIISRPTFSIEQDAEKKINELQTFTNIIDQILGQTNNIESTLLSMKEKFESSEKKLSEFSEMCENLSTDEMRFSEIADGIRKGLTIFAPLKELTRVFRHPPPDFAGKVSFKEHITQLNTCIMFLEENLDFQESPHYLGQYKKLLSQAMDIFKPYFIRIIKQTTDQVLKDSKKMDVHKQLHSSLFYARFSAVGHNLCPTITELCKLCSKESLDAFLPAFYDVYFQCRTRLLKPVLDYHLKSFFMEKSISSYIQKSLALLQLTFFDENKLFREILIMDDFRFMHYWNNLCQSFFENSRSLILHEKNLTELCEVCSYIQSFQNAILEGEREDVDKKVVEFLNPLVLELQERLLFVVQTAIETDIQRYSPTEEDLNPIADDKSLLFDLEKLRLNNDEEKLDPDVPQKLAMAQGWYPVVQKSLIILSKIYRLVNSQVFDEIALELVHSCIRSLVDAYRYFSRNNDKQLARLFLIKNFLVLKDQLNSFDIHYACIEAGVDLRKVWDSVREWRSNLRGVLQLVYETFPKFITNAVDTRQELNQQLRVAVNGYIETAVIHYTECLSIGNLESITEFQNRIQKFPELRQQISLYLSETWIIELFLQAIREEVVSKFQNFYESIVANEDITGSDHNKSGTTSLKHLNEYVEDIYSVMS
Protein: Probable E3 ubiquitin-protein ligase rbrA (EC 2.3.2.31) (Ariadne-like ubiquitin ligase) (Q6T486)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Might act as an E3 ubiquitin-protein ligase. Appears to be required for normal cell-type proportioning and cell sorting during multicellular development. In addition to being necessary for a normal percentage of prestalk cells and the organization of the slug, rbrA is also necessary for spore cell viability.
Interaction partners:
Sequence:
MTDDEMYEDYDVDDDSAEESGNESLDDTEYDDAATQEFDFDENQPQRSLGKLTRQKSFEVLNKDDLFSESHKIIKEVKDVLSIPSEAAVSTLLRHMKWNKEKLIERYMENPEKLCIDAGVPNVMKLNATIVEKSGNVSCLICLEDYPPTQTFALICNHRYCLPCYKNYLEIKVSEGPECIYTPCPAPKCKVIVHQDAFKQIVSPEVFERFNNFILKSYVDDNPQVKWCPAPGCIYSIRCDRKERKEAVNCKCGFQYCFNCNDYEIGDHMPCPCSQVDKWLQKASDESENVTWMLANTKKCPECRSPIEKNGGCMHMTCRKNAGGCGFEFCWLCRGPWTEHGSTTGGYYNCNKYDKSKAKEDDDKAHDAKTELEAYMFYYHRYESHRNAMKIADEQRRNAHLKEQQILSKFDVRSADTKFLMEATEQLLKNRRVLQYSYVYGYYLDKKSQERNLFEYLQEDLEKHTNLLSTQYEQSLDKLEDYQAFIKWKEQVTNYTRITKKFLDNFVDGVAGGLVNTQIN
Protein: EWS RNA-binding protein 1 (A0A0G2K850)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASTDYSTYSQAAAQQGYSAYTAQPTQGYAQTTQAYGQQSYGTYGQPTDVSYTQAQSTATYGQTAYATSYGQPPTGYTTPTAPQAYSQPVQGYGTGAYDTTTATVTTTQASYAAQSAYGTQPAYPAYGQQPAATAPTRPQDGNKPAETSQPQSSTGGYNQPSLGYGQSNYSYPQVPGSYPMQPVTAPPSYPPTSYSSSQPTSYDQSSYSQQNTYGQPSSYGQQSSYGQQSSYGQQPPTSYPPQTGSYSQAPSQYSQQSSSYGQQSSFRQDHPSSMGVYGQESGGFSGPGENRSLSGPDNRGRGRGGFDRGGMSRDPDEDSDNSAVYVQGLNDSVTLDDLADFFKQCGVVKMNKRTGQPMIHIYLDKETGKPKGDATVSYEDPPTAKAAVEWFDGKDFQGSKLKVSLARKKPPLNSMRGGMPPREGRGMPPPLRGGPGGPGGPGGPMGRMGGRGGDRGGFPPRGPRGSRGNPSGGGNVQHRAGDWQCPNPGCGNQNFAWRTECNQCKAPKPEGFLPPPFPPPGGDRGRGGPGGMRGGRGGLMDRGGPGGMFRGGRGGDRGGFRGGRGMDRGGFGGGRRGGPGGPPGPLMEQMGGRRGGRGGPGKMDKGEHRQERRDRPY
Protein: Adhesin YadA (Type 5 secretion system autotransporter YadA) (P31489)
Organism: Yersinia enterocolitica
Function: Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance.
Subcellular location: Cell surface {ECO:0000269|PubMed:22155776}. Cell outer membrane {ECO:0000269|PubMed:22155776}. Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface. {ECO:0000269|PubMed:22155776}.
Interaction partners:
Sequence:
MTKDFKISVSAALISALFSSPYAFADDYDGIPNLTAVQISPNADPALGLEYPVRPPVPGAGGLNASAKGIHSIAIGATAEAAKGAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARASTSDTGVAVGFNSKADAKNSVAIGHSSHVAANHGYSIAIGDRSKTDRENSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQENTNKRSAELLANANAYADNKSSSVLGIANNYTDSKSAETLENARKEAFAQSKDVLNMAKAHSNSVARTTLETAEEHANSVARTTLETAEEHANKKSAEALASANVYADSKSSHTLKTANSYTDVTVSNSTKKAIRESNQYTDHKFRQLDNRLDKLDTRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNENVALKAGVAYAGSSDVMYNASFNIEW
Protein: Pre-mRNA-splicing factor cwf28 (Complexed with cdc5 protein 28) (O43031)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in spliceosome maturation and the first step of pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28
- Pre-mRNA-splicing factor cwf2
- Pre-mRNA-processing factor 19
- ATP-dependent RNA helicase uap56
- Pre-mRNA-splicing factor cwf26
- Pre-mRNA-splicing factor cwf24
- Uncharacterized protein P25A2.03
- THO complex subunit Tho3
- THO complex subunit tho5
Sequence:
MKRKAVLEAFSDSEDEDEKKLKGPQLITGFSAEEGVHYQNETIQRIHEKKRAPKIIHIASDENWMEKRKARFKKKETEVHEKPSQLPDSGLNYGLNIRVASSSAADNEIVDWKANNSNEKAQNKIATNKESTDILPEEVQLVLNDLNDDVKSANSANLQPITTNVVNEKDAYRKDIDELPEPSNMKDYSEIPVEEFGAAMLRGMGWNGQLSSKDAFDVNQRPTFLGMGAKPVDSELTELDIWKNPKKTMFLPVKPLESNSALNSQNEHTEVQKKSNSIDNLTPSSELFRKRSRDNNLSRESSVSSKHLDYNSRNYNKRDRDPDRTKYREYHSERRKQHRTDRYSDDYYQGRSYSYKKRSHRSDRYTERENPDRSYRSTRTL
Protein: Zinc finger protein JAGGED-like (Zinc finger protein NUBBIN) (Q6S592)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts with JAG to promote growth and patterning in stamens and carpels. Promotes the growth of the abaxial and adaxial sides of floral organs. Promotes the growth of the pollen-bearing microsporangia in anthers, the carpel walls of the gynoecium and the establishment of the correct number of cell layers in carpel walls. Promotes leaf blade growth and trichome development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Axial regulator YABBY 1
- Mediator of RNA polymerase II transcription subunit 10b
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB4
- Zinc finger protein KNUCKLES
Sequence:
MRADENNTLDLNNLPDDPSRDIFPFFEEGFSSSSSSGGFREKQTKDGKEYECRFCSLKFFKSQALGGHMNRHRQERETESLNKARELVLRNDSFPPHQGPPSFSYHQGDVHIGDLTQFKPMMYPPRHFSLPGSSSILQLQPPYLYPPLSSPFPQHNTNIGNNGTRHQTLTNSVCGGRALPDSSYTFIGAPVANGSRVAPHLPPHHGL
Protein: DNA polymerase kappa (AtPOLK) (EC 2.7.7.7) (Q6JDV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Template-directed low-fidelity DNA polymerase specifically involved in DNA repair. Able to extend primer-terminal mispairs, and to insert nucleotides opposite to a single 7,8-dihydro-8-oxoGuanine (8-oxoG) lesion and moderately extend from the resulting primer end, thus leading to both error-free and error-prone bypass of 8-oxoG DNA lesions. Probably involved in consecutive DNA replication cycles in the absence of mitosis. Binds preferentially template-primer DNA substrates or single-stranded DNA. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UBT6, ECO:0000255|PROSITE-ProRule:PRU00768}. Note=Detected throughout the nucleus and at replication foci. {ECO:0000250|UniProtKB:Q9UBT6}.
Interaction partners:
- DNA repair protein REV1
- DNA polymerase zeta processivity subunit
- Proliferating cellular nuclear antigen 1
- Proliferating cell nuclear antigen 2
- DNA polymerase zeta catalytic subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase eta
- Cell cycle checkpoint protein RAD17
- ATP-dependent DNA helicase Q-like 3
- At1g09815
Sequence:
MDNGESSSTNNSSRPWESYNTVFTNAKAGMEGVDKEKVQRVVYEMSKGSKYFQNEERKEALMKQKIEHMRDRCAKLSSLDLSNYQKVVDKRILELEATRDLSRIWLHVDMDAFYAAVETLSDPSIKGKPMAVGGLSMISTANYEARKFGVRAAMPGFIARKLCPDLIFVPVDFTKYTHYSDLTRKVFRNYDPHFIAGSLDEAYLDITEVCRERGLSGGEIAEELRSSVYSETGLTCSAGVAANRLLAKVCSDINKPNGQFVLQNDRSTVMTFVSFLPVRKIGGIGKVTEHILKDALGIKTCEEMVQKGSLLYALFSQSSADFFLSVGLGLGGTNTPQVRSRKSISSERTFAATGDERLLYSKLDELAEMLSHDMKKEGLTARTLTLKLKTASFEIRSRAVSLQRYTCSSDDILKHATKLLKAELPVSVRLIGLRMSQFVEEIRNSDPSQGTITKFIVQKDSSRQAQDLDDNDSFDLDANKNCLSNDESGNVSFGSHETSSAHLKDVVEYEERSQIDSGKVIPNQECMKKEERLQILEGDSLLKKYKECKPDTSHSMNDNSNATEAVSVFPQTEPLYWIDGYKCVLCGIELPPSFVEERQEHSDFHLAQRLQNEETGSSSSTTPSKRRILGKEKVNSKPKKQKPDQKDSSKHIPIHAFFTKSNQNSNETQRK
Protein: Large ribosomal subunit protein eL20B (60S ribosomal protein L20-B) (SP-L17) (P0CT69)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL30B
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL6A
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL21A
Sequence:
MALKEYQVVGRKVPTEHEPVPKLFRMRLFAPNESVAKSRYWYFLKMINKVKKATGEIVAINEISEPKPLKAKVFGIWIRYDSRSGTHNMYKEFRDTTRVGAVEAMYADMAARHRARFRSIRILKVVEVEKKEDVRRNYVKQLLNPHLKFPLPHRRTGVVGLAGKKVFAPHRPSTFY
Protein: Elongation factor 1-alpha (EF-1-alpha) (42Sp50) (Thesaurin A) (P17506)
Organism: Xenopus laevis (African clawed frog)
Function: This protein is one of two protein components of a 42S RNP particle that is very abundant in previtellogenic oocytes. A major function served by 42sp50 appears to be the storage of tRNAs for later use in oogenesis and early embryogenesis. Purified 42S particles can directly transfer aminoacyl tRNA to ribosomes.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MTDKAPQKTHLNIVIIGHVDSGKSTTTGHLIYKCGGFDPRALEKVEAAAAQLGKSSFKFAWILDKLKAERERGITIDISLWKFQTNRFTITIIDAPGHRDFIKNMITGTSQADVALLVVSAATGEFEAGVSRNGQTREHALLAYTMGVKQLIVCVNKMDLTDPPYSHKRFDEVVRNVMVYLKKIGYNPATIPFVPVSGWTGENISSPSQKMGWFKGWKVKRKDGFTKGQSLLEVLDALVPPVRPANKPLRLPLQDVYKIGGIGTVPVGKIETGILKPGMTISFAPSGFSAEVKSIEMHHEPLQMAFPGFNIGFNVKNIAVKSLKRGNVAGNSKSDPPTEASSFTAQVIILNHPGFIKAGYSPVIDCHTAHITCQFAELQEKIDRRTGKKLEDNPGLLKSGDAAIITLKPIKPFCVERFFDYPPLGRFAARDLKQTVAVGVVKSVEHKAGAAARRQVQKPVLVK
Protein: Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Isopeptidase T-3) (ISOT-3) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13) (Q92995)
Organism: Homo sapiens (Human)
Function: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36585612}.
Interaction partners:
- E3 ubiquitin-protein ligase SIAH2
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Beclin-1
- Ubiquitin carboxyl-terminal hydrolase 10
- Polyubiquitin-C
- Ubiquitin carboxyl-terminal hydrolase 25
- E3 ubiquitin-protein ligase AMFR
- S-phase kinase-associated protein 2
- Ubiquitin carboxyl-terminal hydrolase 22
Sequence:
MQRRGALFGMPGGSGGRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKIFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEEPVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKLRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAEANRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSIDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIIVHMEEPDFAEPLTMPGYGGAASAGASVFGASGLDNQPPEEIVAIITSMGFQRNQAIQALRATNNNLERALDWIFSHPEFEEDSDFVIEMENNANANIISEAKPEGPRVKDGSGTYELFAFISHMGTSTMSGHYICHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS
Protein: Rho guanine nucleotide exchange factor gef2 (Q09733)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the control of cell polarity and cytokinesis. Involved in bipolar growth and septum formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Septum.
Interaction partners:
- Uncharacterized protein C12B10.10
- Mitosis inducer protein blt1
- Anillin-related medial ring protein mid1
- Kinesin-like protein 8
- GTP-binding protein rho5
- Serine/threonine-protein kinase plo1
- Mitosis inducer protein kinase cdr2
- GTP-binding protein rho1
- Rho guanine nucleotide exchange factor gef3
- Cell division control protein 15
Sequence:
MDVGTMGSRAELLAISIQFGGLWVFRDLLQMNPLFEQDHVFCTFNHPNMGLVLISFAKVDGHILAAYALSKLGPDTFSICYPFSSKLDAFAQTLDLEWQIASMHKEAAACVYEFLCVESVCLHTGENWRESVIEPEYASYIFDTINVFQSSSLTRELYSLGEPNGVREFVVDAIFDIKVDNSWWEDPSNSYWKTVIGSREMFEDSRKKTSSPSPSFASSKDAGTIPAIQKKKSLLIEMMETESTYVERLRHLVNDYALPLRDLAKSSKKLLGLYELNTLFPPCLNKLIQLNSAFLDEFEAIMSDLNFEDIDEKKFEEIDLRLACCFESHFFAFSQHYPRYLEQSNDFGNVLKMASKIPKFVEFHDQVKLNANMNVGLSQLIMEPVQRIPRYSLFLDQIILLTQEGECQHTYVRSVEIIKNIAEMPTVDAEERSRIFAGLQHIIPDLAPNMISNSRNFIDCIDVTREFLKNGQLHLIPYTLILFNDRICLVQRRSKSSIASTILDLRKQNPRNSYSKEKRAQYIGSNMNEAVELTRSMVEENTIFLISKYASSPSFFNEYPILKFRCDFENVRTMDRFYQSFQKALSMNKSQPSCLSFSKLNDFVVFFNNYSRFEYEKESKRSDIVCICTNDANVDKHKFLQDGNIVITFFQQDEDFHLSFDSWLGVSLPTEAVIAKEDLREACLNYLINIKRLLLCPFSNRNFSSLDLYSNLIQHLLSANSSPRKSRLSFGGRPGSPSKISLSLNRFYNQGGLSKSCATLPSQMYNLDHNNISQKSLKFNTHNTSKASAEKTVEHLEAFKGGFKYHTDLKNLLYPLSEKEKIEGDELYDNILKETFNEELLSHYPPNIIYATFQKYLSSFINRKFGVLLSSSFIQQLNTVENLNLSFNSTDAVYHLKKILQDLPESSLKILENIFSIASDLLLRLPLKDQCDFVTKQLAIALAPSMFGSNAVELVYYLAYHSDRIFGTVEELPTPVSPANSNNDKQLDESKFQAIAMKEMPERHPKEILPGQIEREAYEDLRRKYHLTLARLAQMTRLNEDSKKSIPLLYDRFNHDLKLIKQSVQASLIRKQCELDTAKWTLEEYESKLNAKEGCQTNIFI
Protein: F-box only protein 43 (Endogenous meiotic inhibitor 2) (Q4G163)
Organism: Homo sapiens (Human)
Function: Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Plays a vital role in modulating the ubiquitilation of CCNB1 and CDK1 during gametogenesis.
Interaction partners:
- Serine/threonine-protein kinase PLK1
- Cell division cycle protein 20 homolog
- S-phase kinase-associated protein 1
- F-box/WD repeat-containing protein 1A
- Cyclin-dependent kinase 1
- Cullin-1
- G2/mitotic-specific cyclin-B1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- E3 ubiquitin-protein ligase RBX1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
Sequence:
MSFKDKDERISCLEAYVTLTSKSSRFTDETEILKMSQRHSGQAGTEAGNGADSPPIVNSKYSTFRDFCSTSSFQDSGYNELKSCSFDNIDKEYLGKKEKGPTLLYEHPETSGLGLTHPLESPTQKKKCILPRKEKDKTPELCETPKISGKKCLPRRRLNVSFALLKGDFESQNSSLESSISQVINLEKNIPSSASGFSRANNFSPLVTSTLKTEEVTSCSQKLRLNFSQQKTSTIDDSKDDCSLFEVECISPIQGNNFKDSITHDFSDSSLCINDENACPELLGSSVSGTTCGTDEDIFVTPISNLVANIRFNASQILSPSPEVRGSISTPEDSGFNSLSLEKSEDSLSDQEGSFQELLQKHKGTPKVGDTIRKTRHLGRSRRLSTLREQSSQSETEEEKQIVHPDSEKRAAAASAISEGQLSSDESGDLTFSLKNLSKTPALQLVHELFMKSKRKRLQENSGHEFLEQGDGEKIAVLQCILAGLIGKKMGIEKLDILTELKYRNLKHILAMVLESLTAESLCSVWKVSRNWREIVVQDKNANRRRKFYITQLKTDSEGAVLNVEDAATRLQLLNRSALRSVQAQARIPGSQREQGSTLSPWGEVLTPLASSSVTHLSSKQEEYVKVAKTLFTDEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRGAAKPRNRKDALPGSAQSKRNLKRL
Protein: Uncharacterized protein, isoform E (A0A0B4KEK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNSGRNHHRFDQTFLGATELDDELIKQLPKEVLLRVFSYLDVVSLCRCAQVCKYWNVLALDGSSWQKINLFDFQRDIEGPVIENISQRCRGFLKSLSLRGCQSVGDQSVRTLANHCHNIEHLDLSDCKKITDISTQSISRYCSKLTAINLHSCSNITDNSLKYLSDGCPNLMEINVSWCHLISENGVEALARGCVKLRKFSSKGCKQINDNAIMCLAKYCPDLMVLNLHSCETITDSSIRQLAANCHKLQKLCVSKCADLTDLTLLSLSQHNHLLNTLEVSGCRNFTDIGFQALGRNCKYLERMDLEECSQITDLTLAHLATGCPSLEKLTLSHCELITDDGIRHLTTGSCAAEILSVLELDNCPLITDRTLEHLVSCHNLQRIELFDCQLITRTAIRKLKNHLPNIKVHAYFAPGTPPAVTSGHRPRYCRCCEILXDTAIGFARKIMRKTATD
Protein: Stalk cross-band protein StpB (A0A0H3CAY8)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Interaction partners:
Sequence:
MRRLSRLLALWAALTLGAAVASAPELAVASPDAKIDQQIRPCFGLLLQPNLAHGCKVRDVRPKPCPRGTIRSKGRCVVPYNNGGYAYVSREINCDYAYPGQISDTLYRLYEGDVLTLTSTNGGACVDSLNITKAISIVVRDYSPSRTRPILIAGSGQPCIKIQPGVRYVVLDGLGIEATRAGAASCIVGRATEIAMRGVTVRYDGEGSAFDVGESRIELAQSTFIGRTRQPVVKATGTIMAADVEIAATAIGAALETSGDSRLRGVRVVRLGDWTGSSRTRNSAGFIIAGMNRQQLVQIDGLYVDGFSRGIYVGGGDETTLLRPVVRDSDWAVTLENANLRVVEGELEAVDVGIYAASGIVFASNNKIMGVMRSGIYADAGGQVRAVDNRVYARPEGCRALVTGFFNGELTCRPWFEAPELYRTPRDRARLDFDSYWPAPAIAAGVTAQAPAELSGPPPAGEPVPAPQQGGAPR
Protein: Spookier (EC 1.-.-.-, EC 1.14.-.-) (A8Y592)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Cholesterol 7-desaturase nvd
- Cytochrome P450 306a1
- Cytochrome P450 302a1, mitochondrial
- Cytochrome P450 315a1, mitochondrial
- Cytochrome P450 307a1
- Probable cytochrome P450 6t3
- Short-chain dehydrogenase/reductase)
- Prothoracicotropic hormone, isoform F
- Transcription factor Ouib
- Probable cytochrome P450 301a1, mitochondrial
Sequence:
MLTSVFYVLFAIAITIILISYVFLLLKCKQKAFVVIGLLYQEKKYQCFDQAPGPHPWPIIGNINLLGRFQYNPFYGFGTLTKKYGDIYSLSLGHTRCIVVNNVDLIKEVLNKNGKYFGGRPDFFRYHKLFGGDRNNSLALCDWSQLQQKRRNLARRHCSPRESSSYFSKMSEIGGLEVNQLLDQLTNISSGYPCDVKPLILAASANMFCQYMCSVRFNYSDKGFQKIIEYFDEIFWEINQGYSFDYIPWLVPFYCNHISRIVHWSASIRKFILERIVNHRESNININEPDKDFTDALLKSLKEDKNVSRNTIIFMLEDFIGGHSAVGNLVMLALAYIAKNPTIALHIRNEVDTVSAKGIRRICLYDMNVMPYTMASISEVLRYSSSPIVPHVAMEDTVIKGFGVRKGTIVFINNYVLNMSESFWNHPEQFDPERFLENNFTNNKESGLKCDDNKRTEFIRKNDNDGSTKSKKYGKQNLNNKLLKKSIPQFLPFSVGKRTCIGQSLVRGFGFLLLANIIQNYNVNSADFSKIKLEKSSIALPKKCFKLSLRPRT