wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome non-ATPase regulatory subunit 7 (Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)) (Proteasome 26S subunit, non-ATPase 7) (Psmd7 protein) (Q7ZYX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- 26S proteasome regulatory subunit 6B
- Proteasome 26S subunit, non-ATPase 14.
- Proteasome 26S subunit, non-ATPase 6.
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 12
- Proteasome subunit alpha type
Sequence:
MPDLAVERVVVHPLVLLSVVDHFNRIGKVGSQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKQYCSNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLRDIKDTTVGTLSQRITNQVHGLKGLNSKLLDIKSYLEKVATGKLPINHQIIYQLQDVFNLLPDVNLQEFVKAFYLKTNDQMLVVYLASLIRSVVALHNLINNKIANRDAEKKEGQEKDDSKKEKKDEKDKDKDKDKEKDASAKKEDKKDKK
Protein: Auxin response factor 10 (Q9SKN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Auxin-responsive protein IAA33
- Auxin transporter protein 1
- B3 domain-containing transcription factor ABI3
- Auxin-responsive protein IAA17
- Protein TRANSPORT INHIBITOR RESPONSE 1
- WUSCHEL-related homeobox 5
- Transcription factor MYB33
- Protein AUXIN SIGNALING F-BOX 2
- Auxin-responsive protein IAA32
- Protein AUXIN SIGNALING F-BOX 3
Sequence:
MEQEKSLDPQLWHACAGSMVQIPSLNSTVFYFAQGHTEHAHAPPDFHAPRVPPLILCRVVSVKFLADAETDEVFAKITLLPLPGNDLDLENDAVLGLTPPSSDGNGNGKEKPASFAKTLTQSDANNGGGFSVPRYCAETIFPRLDYSAEPPVQTVIAKDIHGETWKFRHIYRGTPRRHLLTTGWSTFVNQKKLIAGDSIVFLRSESGDLCVGIRRAKRGGLGSNAGSDNPYPGFSGFLRDDESTTTTSKLMMMKRNGNNDGNAAATGRVRVEAVAEAVARAACGQAFEVVYYPRASTPEFCVKAADVRSAMRIRWCSGMRFKMAFETEDSSRISWFMGTVSAVQVADPIRWPNSPWRLLQVAWDEPDLLQNVKRVSPWLVELVSNMPTIHLSPFSPRKKIRIPQPFEFPFHGTKFPIFSPGFANNGGGESMCYLSNDNNNAPAGIQGARQAQQLFGSPSPSLLSDLNLSSYTGNNKLHSPAMFLSSFNPRHHHYQARDSENSNNISCSLTMGNPAMVQDKKKSVGSVKTHQFVLFGQPILTEQQVMNRKRFLEEEAEAEEEKGLVARGLTWNYSLQGLETGHCKVFMESEDVGRTLDLSVIGSYQELYRKLAEMFHIEERSDLLTHVVYRDANGVIKRIGDEPFSDFMKATKRLTIKMDIGGDNVRKTWITGIRTGENGIDASTKTGPLSIFA
Protein: RNA-binding protein with multiple splicing 2 (Heart and RRM expressed sequence) (Hermes) (Q9W6I1)
Organism: Gallus gallus (Chicken)
Function: RNA-binding protein involved in the regulation of smooth muscle cell differentiation and proliferation in the gastrointestinal system. Binds NOG mRNA, the major inhibitor of the bone morphogenetic protein (BMP) pathway. Mediates an increase of NOG mRNA levels, thereby contributing to the negative regulation of BMP signaling pathway and promoting reversible dedifferentiation and proliferation of smooth muscle cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRY4}. Nucleus {ECO:0000250|UniProtKB:Q6ZRY4}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q6ZRY4}.
Interaction partners:
- Pleckstrin homology domain containing S1.
- Uncharacterized protein.
- Ligand of numb-protein X 2.
- NDRG family member 3
Sequence:
MSNLNKDTEHTNGGGNVEEEVRTLFVSGLPVDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVTFDSRAGAEAAKNALNGIRFDPENPQTLRLEFAKANTKMAKSKLMATPNPTNIHPALGAHFIARDPYDLTGAALIPASPEAWAPYPLYTTELTPAIPHAAFTYPAAAAAAAALHAQMRWYPPSEATQQGWKSRQFC
Protein: Temporin-1Tc (TC) (Temporin-C) (P56918)
Organism: Rana temporaria (European common frog)
Function: Has antibacterial activity against Gram-positive bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
LLPILGNLLNGLL
Protein: (S)-8-oxocitronellyl enol synthase CYC2 (EC 1.3.1.122) (Cyclase 2) (Iridoid synthase) (ISY) (A0A1C9CX66)
Organism: Camptotheca acuminata (Happy tree)
Function: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities.
Interaction partners:
Sequence:
MSWWWAGAIGAARKKFEEDDAPRDCQSVALIIGVTGIVGNSLAEILPISDTPGGPWKVYGVARRPRPAWNADHPVEYIQCDISDASDTHTKLSPLTDVTHIFWVTWANRPTESECCELNGTMLRNVLNALIPKAANLHHICLQTGHKHYIGPFEAFGKIKPHEPPFTEDMPRLNAPNFYYTLEDMLVEASEKKAGLNWSVHRPAVIFGFSPFSMMNIIGTLCVYAAICKHENTPLKFPGTKAAWNCYSVASDADLIAEHQIWAAVDPYAKNEAFNCSNGDLFKWKHLWKVLAEQFGVEYAEFDESEKPTSLVERMKDKGPVWEEIVRENGLHTTKLEGVATWWFADVILGGECLLDSMNKSKEHGYLGFRNTKNSLISVIDKMKAHKIVP
Protein: LD47668p (Q960J3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSKPREFAHLIKNKFGSADNINQMSEAELQGMQSANADVLGSERLQQVPGAGTSTGSGGGGQNNNTGGAGSGTGKFNSDNGSECSSVTSESIPGGSGKSQSGASQYHIVLKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQWPDVQDIGSGLVRHLKQSLVVK
Protein: Proteasome subunit beta type-3 (Proteasome subunit beta 3) (Q23237)
Organism: Caenorhabditis elegans
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-6
- Proteasome subunit pbs-5
- Proteasome subunit alpha type-3
Sequence:
MSIMSYTGGTVVAMAGDECVCIASDLRIGEQMTTIATDQKKVHKVTDKVYVGLAGFQSDARTVLEKIMFRKNLYELRENRNIKPQVLSEMISNLAYQHRFGSYFTEPLVAGLDDTNKPYICCMDTIGCVSAPRDFVAVGTGQEYLLGVCENFWRENMKPDELFEATAQSILSCLERDAASGWGAVVYTITKDKVNVSTIKARMD
Protein: E3 ubiquitin-protein ligase TRIM17 (EC 2.3.2.27) (RING finger protein 16) (RING-type E3 ubiquitin transferase TRIM17) (Testis RING finger protein) (Tripartite motif-containing protein 17) (Q9Y577)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase that plays important roles in the regulation of neuronal apoptosis, selective autophagy or cell proliferation. Stimulates the degradation of kinetochore ZW10 interacting protein ZWINT in a proteasome-dependent manner, leading to negative regulation of cell proliferation. Inhibits autophagic degradation of diverse known targets while contributing to autophagy of midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17 assembles into complexes with the key autophagy regulator BECN1. Controls neuronal apoptosis by mediating ubiquitination and degradation of MCL1 to initiate neuronal death. In addition, regulates NFAT transcription factors NFATC3 and NFATC4 activities by preventing their nuclear localization, thus inhibiting their transcriptional activities. Decreases TRIM41-mediated degradation of ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase activity of TRIM28 and its interaction with anti-apoptotic BCL2A1, blocking TRIM28 from ubiquitinating BCL2A1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27562068}. Lysosome {ECO:0000269|PubMed:27562068}.
Interaction partners:
- Gamma-butyrobetaine dioxygenase
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- T-cell receptor-associated transmembrane adapter 1
- Transcription intermediary factor 1-beta
- Transcription intermediary factor 1-alpha
- E3 ubiquitin-protein ligase TRIM9
- TERF1-interacting nuclear factor 2
- Tripartite motif-containing protein 66
- Tripartite motif-containing protein 44
- Tripartite motif-containing protein 67
Sequence:
MEAVELARKLQEEATCSICLDYFTDPVMTTCGHNFCRACIQLSWEKARGKKGRRKRKGSFPCPECREMSPQRNLLPNRLLTKVAEMAQQHPGLQKQDLCQEHHEPLKLFCQKDQSPICVVCRESREHRLHRVLPAEEAVQGYKLKLEEDMEYLREQITRTGNLQAREEQSLAEWQGKVKERRERIVLEFEKMNLYLVEEEQRLLQALETEEEETASRLRESVACLDRQGHSLELLLLQLEERSTQGPLQMLQDMKEPLSRKNNVSVQCPEVAPPTRPRTVCRVPGQIEVLRGFLEDVVPDATSAYPYLLLYESRQRRYLGSSPEGSGFCSKDRFVAYPCAVGQTAFSSGRHYWEVGMNITGDALWALGVCRDNVSRKDRVPKCPENGFWVVQLSKGTKYLSTFSALTPVMLMEPPSHMGIFLDFEAGEVSFYSVSDGSHLHTYSQATFPGPLQPFFCLGAPKSGQMVISTVTMWVKG
Protein: Coatomer subunit epsilon (Q9Y0Y5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}.
Interaction partners:
- Coatomer subunit zeta
- Coatomer subunit beta
- Coatomer subunit beta'
- Coatomer subunit gamma
- Coatomer subunit alpha
- Coatomer subunit delta
- Protein SEC13 homolog
- ADP-ribosylation factor 1
- Protein transport protein Sec31A
- BET1 homolog
Sequence:
MSRQQNEEDTNSVLFDARNEYYIGNFMGSINFVLPEQGTAGPELLSYMYLSYLAIDSGRIVASDIKEGNSTPLQALRLVHEAFEQPSRTEELLEKLTDKVAGEEDETNIWHLATAIVYCHDGQFENALKILHGSTNLESMALSVQCLLRLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALAQGTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVLRESLLKKHNDYDTLINLMVHAHLTGKPTEAITRNLEQLRQFYPKSDFVTDLDKKSAEFDRLCLQYDVEGGEKLLAV
Protein: Peptidoglycan-N-acetylmuramic acid deacetylase PdaA (Peptidoglycan MurNAc deacetylase) (EC 3.5.1.-) (O34928)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate.
Interaction partners:
- Probable glycosyltransferase YdaM
- Germination-specific N-acetylmuramoyl-L-alanine amidase
- Uncharacterized glycosylase YvbX
- Putative sporulation-specific glycosylase YdhD
Sequence:
MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYLGNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHIIGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRLGYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLKKQGYTFKSIDDLMFEKEMRLPSL
Protein: GDT1-like protein 4 (Q9C6M1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lysine histidine transporter-like 6
- Transcription factor HHO3
Sequence:
MSSVLQGFTKSLAMTFVSEIGDKTFFAAAILAMRYPRRLVLAGCLSALIVMTILSATLGWAAPNLISRKWTHHITTLLFFGFGLWSLWDGFKEGGGGSEELAEVEAELDADLKANGKSPKDSSKREDENKKQNRAFLTQFFSPIFLKAFSINFFGEWGDKSQLATIGLAADENPFGVVLGGVVAQFLCTTAAVIGGKSLASQISERIVALSGGMLFIIFGIQSYLTSVEA
Protein: TPR repeat-containing protein P27G11.02 (Q9P7N6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent zinc metalloprotease YME1 homolog
Sequence:
MRMQWIWKSRRSLQNVFIRRSSQYHKPFWRRPLPATLLGCAVLGVAAVYFAKPSPIDENYPRSVAKYLHEALYRQKGENNHDFQDAWKAYQSAIKQAESEKMDMESPPVQGIRLQMANLLASAGALHKAWSMYWDILERTSKLPDFLEQRVLIASKLIELSEPLGLQKDATKAADLIVKALLSKQFNGDDEQKSRLFEQSATLYFQAGTPSYAVPLYHEALNLTMANPSCHGLILMNNLATSLLAQTETVDKKHHETLMKQSQSWSQKAVDSYYFAYPKDRNQECHAGCAAAFYTLGQIAERQGNIDLALKHYKNSEALRKDDPYNDGSMLSHIAIDRLDKDAFIKKLDKSSSPTD
Protein: Golgi apyrase (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (Golgi nucleoside diphosphatase) (Q9USP2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Required for Golgi glycosylation and cell wall integrity. Involved in N-mannosylation of proteins in Golgi.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:12686557, ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- CTP synthase
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase large chain
- Bifunctional purine biosynthesis protein ade10
- Uridylate kinase
- Guanylate kinase
- Adenylate kinase
- Inosine triphosphate pyrophosphatase
- AMP deaminase
- Uracil phosphoribosyltransferase 1
Sequence:
MVRKYGIFIDAGSSGSRLLIYSWDYDTDSSLSDKVKKLPLIETGIGDGGKWSLKVQPGISSFANNPKHVGKKHLKELLDFAAHAIPKDVHKETPVFLSATAGMRLLGVDAQNKILSHACRYIKKNYDFDIPNCSNSIRVIDGKAEGMYGWLATNYLLKTLEEKDTSTVGFLDMGGASVQIAFELPPSQLKNYKDSISTVHIGLQNGQQLEYPLFVTTWLGFGANEAYRRYLGLLIESENGKVGNTLSDPCSLRGRTYDIDGIEFAGTGDLKQCLKLTYNLLNKDKPCSMDPCNFDGISIPPVDFANTEFVGVSEFWYTTNDVFDMGGSYHFPNFYKKVDEYCGTEWETMLSRLYNKELTPSTDENKLEKLCFKASWALNVLHEGFDVPKSNTSSNDAKDGLSVIPAYHSPFTSLEKIERTEVSWTLGQVLLYASNQQLLAKPEYANYYMDPYGKLIASPSKHWMRLFPNKLFFILSFIFCLFFLFSLVLFGYDPKRRQRFKKFLLRLQRRKAPYIMSANGSYEDIADFSDDLEMSSPSKWHGPPIRTTSSHVLADRLSFTASRERTPRSPFP
Protein: Parasitophorous vacuole membrane protein S16 (Sexual stage-specific protein S16) (Q6ZMA7)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Involved in male gametogenesis. Required for exflagellation of male gametocytes. May play a role in parasite transmission in the mosquito (By similarity). Binds to the mosquito vector midgut (By similarity).
Subcellular location: Parasitophorous vacuole membrane {ECO:0000269|PubMed:14698439, ECO:0000269|PubMed:17367781}; Single-pass type I membrane protein {ECO:0000305}. Vacuole {ECO:0000269|PubMed:17367781}. Note=Localizes to the multi-laminate membrane whorls of the circular clefts in the infected erythrocyte cytoplasm and food vacuole membrane of the gametocyte. {ECO:0000269|PubMed:17367781}.
Interaction partners:
Sequence:
MNIRKFIPSLALMLIFFAFANLVLSDANDKAKKPAGKGSPSTLQTPGSSSGASLHAVGPNQGGLSQGLSGKDSADKMPLETQLAIEEIKSLSNMLDKKTTVNRNLIISTAVTNMIMLIILSGIVGFKVKKTKNADDDKGDKDKDKDNTDEGDEGDDS
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (E7F716)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ethanolamine kinase
- Zinc finger protein 148
Sequence:
MMADRLSAEEEQATKQFLEEINKWTSQHGVSPLSWDVAVKFLMARKFDVLRAIELFHSYRETRLREGIVKLQPHKEPLRSELLSGKFTVLGVRDPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSNYTNFELDLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMADLRQHLPRDCLPEHLGGCLPLDVHNWNLQLLSEQNGRVDPVDELVGIPLENTSIHTPGAEAMSLAELMAHLNRAQRSGIYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEHAQRQGLLSANQ
Protein: Testis-expressed sequence 2-like protein (DUF2404) (Q9CAT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
- Protein ARV 1
Sequence:
MVSFTGFAFVFGILLGILAIVTAEVVGFLYLLKRLNRKRDRQESNSSSDPNFKSFDPRQSIDFSLNKQGVIWILELDENVKDWMKEKLPKEQKKKRVDLLEVHPVRRFARIKDHKLILSDSLDGPQTPITLKGCFVDAVSGSGPTRKWAKRFPIQVESKTSVLYKGNRVFYIFLETSWEKESWCKALRLAACENQERFIWSTKLKEDFRNYLASLNAAYPSFMKPSAGFSFESLDKGLKADGPSSKVRLIWKKFSKKCSTKVNFPPSIRDDKKTSSRSYQDSQSTGSSGKSTSARRMQDNIPEETDVQVISRSWSHSSHASDVDSEDKSFDEGTLALNVVLSRLFFDVKQNTVLKNLVRERIQRIMSNMRIPSYIGELICCDVDIGNLPPYIHGTRILPMEMNGVWAFEIDIEYTGGAGLEVETRVDAREEDLQKGIAEGKLQPNSAGDVPPDLLEGLADFEKQLNVPGGTVDAQDVKSGGTDKADESKGPKGTKTGSSNGSKWKSMLKNIVEQVSQVPITLSIGVSSLRGTLCVHMKPPPSDQLWFGFTSMPDIEFNLVSSVGEHKITNSHVAMFLVNRFKTAIRDVMVLPNCESVTIPWMTAEKDDWVERNVAPFMWLNQDSTSDRENLEAAEAKSKADKPPTSEQMQKTVNIPQKPRIEEESVSADTAPSANSIALLVESDKSLEELKTPLLESSEKHDTIARGGSAGDIIPGIGQSPSMSTVSGEEDDSNSKGKKMGAAKARMFDFRKKVGEKFEEKKRHVEEKSRQIVEKMRGP
Protein: Killer cell lectin-like receptor, subfamily A, member 5 (E9PTN0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTYSSVRFSKSSGLQNQVKPEETKGPKEAGHRECYVPWHLIVIALGILCTLLLLTVAVLVTIIFQYSQEKHELQETLNHHHNCSAMQRDIDLKEEMLRKISIDCSPGNDLLESFNRSKNRWYSKTKAVVNSSQHKGSEIETYWFCYGIKCYYVIKDGKSWDECKQTCQNSSLFLLKIDDEDERKFLQQQLIPDNYWIGFSYDKEKKEWAWIENGPSKLASNTMKFNKKLGGCVFLSKTRLDHTDCINLYSCICGKKLNKFPDLLSN
Protein: Microtubule interacting and trafficking domain containing 1 (B8ZZL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKSGLRQDPQSTAAATVLKRAVELDSESRYPQALVCYQEGIDLLLQVLKGTKDNTKRCNLREKISKYMDRAENIKKYLDQEKEDGKYHKQIKIEENATGFSYESLFREYLNETVTEVWIEDPYIRHTHQGIEQVQQSRGLQEIEESLRSHGVLLEVQYSSSIHDREIRFNNGWMIKIGRGLDYFKKPQSRFSLGYC
Protein: DUF1707 domain-containing protein (O33344)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTETGGDMVALRVSDADRNGTMRRLHNAVALGLINIDEFEQRSSRVSFACTRSELDGLVGDLPRPGAIVTSAADRVELRGWAGSLKRHGEWIVPTRLALVRRLGSIELDLVKARFAGPVVVIELDMMFGSLEVRLPNGASASIDDVEVYVGSASDRRKDAPAEGTPHVVLTGRMVCGSVVIKGPRRALLRRHRG
Protein: Putative uncharacterized protein BUD26 (Q03783)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative uncharacterized protein YLR232W
- Increased recombination centers protein 13
Sequence:
MILIFFAYISRRETVSQRQTSTIVYNITLMFSTLRCALKILAQIKKRLQQTSSNHENKKYEEVIKDHVGVKIQNIICLLAFVLVVYYQMRCKKMT
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (O26013)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- DNA 3'-5' helicase
- Bifunctional DNA-directed RNA polymerase subunit beta-beta'
- UvrABC system protein B
- Anaphase-promoting protein
- Protein RecA
- Beta sliding clamp
- Amidophosphoribosyltransferase
- CN hydrolase domain-containing protein
- Phosphopantetheine adenylyltransferase
- Serine--tRNA ligase
Sequence:
MMDFEKSILDHLNGAQKIAASHIQGPLLILAGAGSGKTKTLTSRLAYLIGVCGVPSENTLTLTFTNKASKEMQERALKLLKNQALIPPLLCTFHRFGLLFLRQHMNLLKRACDFSVLDSDEVKTLCKQLKISNFRASISQIKNGMMDLSMQDSECYKAYELYQNALKKDNLVDFDDLLFLSLKILQDNETIAKETSERYHYIMVDEYQDTNALQLEFLKKLSFTHHNLCVVGDDDQSIYGFRGADISNILNFSKHFKGAKIVKLETNYRSSAEILACANSLISHNQHRHIKTLQSFKGSHKSVVCKEYLTQKEESLDVAYQIKALLKKGENLENIAILYRLNGLSRSIEESLNALNIPYRLIGALSFYERAEIKDALAFMHLVAKKDDRFFIKRVLNKPPRGLGKITQEWIFSLLDEEGLNLEEALKLGAFKDKLNPKNEYALKQFIAMIGRLREAFEISVEEFCSRFLEETNLLKSYEKEDNYEEREGFVKELLTLVKEYFKTNPTHSLLDFLNESVLDAHNTENAQKVSCMSVHMSKGLEFKHVFVIGLEEGFFPHRGFNQESDLEEERRLAYVAITRAKEELQLSYVKERSYFGRKISCSPSVFLEEAQLLNQDNPPKQDHQKDAPIKVGDLIRHKIFGTGRVLGVEKGLSGLCLKINCGGNVYDKISEKFVEKVDNGF
Protein: Type 1 encapsulin shell protein (O07181)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Encapsulin nanocompartment {ECO:0000256|ARBA:ARBA00033738}.
Interaction partners:
Sequence:
MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH
Protein: SD04793p (Q8MQX3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDDLDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLNELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG
Protein: CCAAT/enhancer-binding protein epsilon (C/EBP epsilon) (Q6PZD9)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- CCAAT/enhancer-binding protein alpha
- Transcription factor PU.1
Sequence:
MSHGTYYECEPRGGQQPLEFSGGRAGPGELGDMCEHEASIDLSAYIESGEEQLLSDLFAMKPTPEARSLKGPGAPSFPHYLPADPRPFAYPSHTFGPDRKALGPGIYSNPGSYDPRAVAVKEEPRGPEGNRGTSRGSYNPLQYQVAHCGQTAVHLPPTLAAPGQPLRVLKAPVAAAAPPCSPLLKAPSPAGPSHKGKKAVNKDSLEYRLRRERNNIAVRKSRDKAKRRIMETQQKVLEYMAENERLRNRVDQLTQELDTLRNLFRQIPEAASLIKGVGGCS
Protein: E3 ubiquitin-protein ligase RNF170 (EC 2.3.2.27) (Putative LAG1-interacting protein) (RING finger protein 170) (RING-type E3 ubiquitin transferase RNF170) (Q96K19)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21610068, ECO:0000269|PubMed:31076723}; Multi-pass membrane protein {ECO:0000269|PubMed:21610068}.
Interaction partners:
- Erlin-2
- Erlin-1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Transmembrane and ubiquitin-like domain-containing protein 1
Sequence:
MAKYQGEVQSLKLDDDSVIEGVSDQVLVAVVVSFALIATLVYALFRNVHQNIHPENQELVRVLREQLQTEQDAPAATRQQFYTDMYCPICLHQASFPVETNCGHLFCGACIIAYWRYGSWLGAISCPICRQTVTLLLTVFGEDDQSQDVLRLHQDINDYNRRFSGQPRSIMERIMDLPTLLRHAFREMFSVGGLFWMFRIRIILCLMGAFFYLISPLDFVPEALFGILGFLDDFFVIFLLLIYISIMYREVITQRLTR
Protein: Arylsulfatase B (ASB) (EC 3.1.6.12) (N-acetylgalactosamine-4-sulfatase) (G4S) (P50430)
Organism: Rattus norvegicus (Rat)
Function: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation. In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels. Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity).
Subcellular location: Lysosome. Cell surface {ECO:0000269|PubMed:19536613}.
Interaction partners:
- Alpha-L-iduronidase
- Arylsulfatase A
- Arylsulfatase G
- Hyaluronidase-1
- Hyaluronidase-2
- Hyaluronidase
- Hyaluronidase
- Hyaluronidase.
- Hyaluronidase PH-20
- Formylglycine-generating enzyme
Sequence:
MGELSGCTGGSRAGGPGPRLPLLLLLLLWPARASDAAPPPHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHMGLQHYLIMTCQPNCVPLDEKLLPQLLKDAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIECLNGTRCALDLRDGEEPAKEYTDIYSTNIFTKRATTLIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYDFIQDKHRRIYAGMVSLLDEAVGNVTKALKSRGLWNNTVLIFSTDNGGQTRSGGNNWPLRGRKGTLWEGGIRGAGFVASPLLKQKGVKSRELMHITDWLPTLVNLAGGSTHGTKPLDGFDVWETISEGSPSPRVELLLNIDPDFFDGLPCPGKNTTPEKNDSFPLEHSAFNTSIHAGIRYKNWKLLTGYPGCGYWFPPPSQSNISEVPSVDSPTKTLWLFDINRDPEERHDVSREHPHIVQNLLSRLQYYHEHSVPSYFPPLDPRCDPKGTGVWSPWM