wanglab/gogpt-training-data huggingface dataset:
Protein: Exonuclease domain-containing protein (Q9TZZ9)
Organism: Caenorhabditis elegans
Interaction partners:
- Enhanced RNAI
Sequence:
MSINFTRTPRLLLDTVAHYSSFLESTKLVKTREVKKPPRYPNFSLKKDTKNQKMSQHFDYLLVLDFEATCQDNWKGPMHPVQEIIEFPVVQLSTADWSEIRRFHQYVKPTECPRLTSFCTSLTGIIQEMVDEKPTLPQVLSEFDSWLKEDSRLEKGKFAFVTCGDWDLKVALPNEAKFKNIGIPEYFNQWINVKKASAEHTNHFAKGIAQLLAIYKLQHQGRHHSGIDDVANICEIVRCLGMNGHNYQITGSKDTMTRRVFRDARK
Protein: Uncharacterized N-acetyltransferase C663.13c (EC 2.3.1.-) (O74519)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-terminal acetyltransferase A complex subunit nat1
- N-terminal acetyltransferase A complex catalytic subunit ard1
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase A complex subunit-like protein C418.02
- N-terminal acetyltransferase B complex subunit arm1
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- SAGA complex subunit Sgf29
Sequence:
MIELDAINPNNLKILEVINEKCFDPEIIIFPTSFYKDTISVGPLAQYAYFNQVCVGAVRCKKETHNKSHKIQILSLAVLPAYRNRSIGTKLLEYACETAAEGKAKEIYIKLSPKLDVSEWFIHRGFIIDESSKTEDSVLLSKKL
Protein: Sex hormone-binding globulin (SHBG) (Sex steroid-binding protein) (SBP) (Testis-specific androgen-binding protein) (ABP) (Testosterone-estradiol-binding globulin) (TeBG) (Testosterone-estrogen-binding globulin) (P04278)
Organism: Homo sapiens (Human)
Function: Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration.
Subcellular location: Secreted {ECO:0000250}. Note=In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis. {ECO:0000250}.
Interaction partners:
- Albumin
- Corticosteroid-binding globulin
- Insulin
- Insulin-like growth factor 1
- Adiponectin
- Prolactin
- Neurexin-2
- Muellerian-inhibiting factor
- Thyroxine-binding globulin
- Aromatase
Sequence:
MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQSAHDPPAVHLSNGPGQEPIAVMTFDLTKITKTSSSFEVRTWDPEGVIFYGDTNPKDDWFMLGLRDGRPEIQLHNHWAQLTVGAGPRLDDGRWHQVEVKMEGDSVLLEVDGEEVLRLRQVSGPLTSKRHPIMRIALGGLLFPASNLRLPLVPALDGCLRRDSWLDKQAEISASAPTSLRSCDVESNPGIFLPPGTQAEFNLRDIPQPHAEPWAFSLDLGLKQAAGSGHLLALGTPENPSWLSLHLQDQKVVLSSGSGPGLDLPLVLGLPLQLKLSMSRVVLSQGSKMKALALPPLGLAPLLNLWAKPQGRLFLGALPGEDSSTSFCLNGLWAQGQRLDVDQALNRSHEIWTHSCPQSPGNGTDASH
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha) (Q6PD03)
Organism: Mus musculus (Mouse)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Shugoshin 1
- Apoptosis regulator Bcl-2
- Protein phosphatase 1 regulatory subunit 1A
- Meiotic recombination protein REC8 homolog
Sequence:
MSSPSPPAPVACAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCVLFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNQTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELQLKKALEKQNNAYNMHSIRSSTSAK
Protein: Bifunctional purine biosynthesis protein ADE17 [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)] (P38009)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10877846}.
Interaction partners:
- Bifunctional purine biosynthesis protein ADE16
- Adenylosuccinate lyase
- Adenylosuccinate synthetase
- Serine hydroxymethyltransferase, cytosolic
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthetic protein ADE5,7
- Amidophosphoribosyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Serine hydroxymethyltransferase, mitochondrial
- Phosphoribosylformylglycinamidine synthase
Sequence:
MANYTKTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILARDIDSDEKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGEISQDLRNRLALKAFEHTADYDAAISDFFRKQYSEGQAQITLRYGANPHQKPAQAYVSQQDSLPFKVLCGSPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGIPLSDVEKQVYFVADIENLSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKYCILQIDPNYVPEAVERRQVYGVTLEQKRNDAIINQSTFKEIVSQNKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKADNWWFRQHPRVLEIKWAKGVKRPEKSNAIDLFVTGQIPTEEPELSEYQSKFEEIPKPFTPEERKEWLSKLTNVSLSSDAFFPFPDNVYRAVKSGVKYIAAPSGSVMDKVVFSAADSFDLVYVENPIRLFHH
Protein: Uncharacterized protein C4H3.03c (Q10211)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C553.10
- Uncharacterized protein PB18E9.04c
Sequence:
MPPNARVSYGAEKYLPREIDNHGIVGNMHTSAMISLDGSVEMMCWPNFDSPSIFARILDARAGHFSITPIEQTSCKQMYEPSTNILHTKFYSERGVLRLLDFFHRPWEDYEPLYPWLIRRVSCIRGTSRIKLECFPALDYARQSHETRVSKITENYYQAEFVPASGDPKYILDCVPSGDQLKIDLELIYPAEHLIEGGGVISYLELEEGQEITFIFRQEGLGPNVDYVTPNLVDKLEDSTKRYWRAWIQQCVYTGRYREFVQRNALTLKLLIYEPTGAVIASPTFSLPEDLGGVRNWDYRFTWIRDSAFTIYALAQLGFRAEAVEYMSFIYHVLKKKNKDGGINIVYSIHGDSQNLEEVELTHLRGYYNSHPVRIGNAAVHHLQLDIYGELMDSIYIYDKKCQPIAYDLWLEVRQICDYVCANWKRPDKSIWEVRGQERNFLYSKIMLWVALDRALRIAFTRSLPCPKHMVWMDTRDEIYEAIMDSGYNMEKGFFAQSFENNDILDASVLVMPLVSFISPTDPRFLSTMDNIMKPLEKDGLMSNGLIFRYNNFVYEDGVGGDEGAFTMVCFWLVEALAMAGCSGYPKLLSTAVSMFEDLVRYSSHLQYYSEECSLSSESLGNSPQAFSSIAAIAAAHILDKALSIFNEI
Protein: Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1) (P49427)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes.
Subcellular location: Cytoplasm. Nucleus. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Polyubiquitin-C
- S-phase kinase-associated protein 1
- Cullin-1
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- F-box/WD repeat-containing protein 1A
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 R2
Sequence:
MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEEADSCFGDDEDDSGTEES
Protein: Protein phosphatase 1 regulatory subunit 12B isoform 2 (A0A0S2Z4Q8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAELEHLGGKRAESARMRRAEQLRRWRGSLTEQEPAERRGAGRQPLTRRGSPRVRFEDGAVFLAACSSGDTDEVRKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFINHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGAFP
Protein: Guanine deaminase (EC 3.5.4.3) (Dihydropterin deaminase) (EC 3.5.4.-) (Q9VMY9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. Also has 7,8-dihydropterin deaminase activity, which plays a role in synthesis of the red eye pigment aurodrosopterin.
Interaction partners:
- Xanthine dehydrogenase
- Adenine phosphoribosyltransferase
- purine-nucleoside phosphorylase
- Aldehyde oxidase 1
- Aldehyde oxidase 3, isoform A)
- Aldehyde oxidase 4
- Aldehyde oxidase 2
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MATVFLGTVVHTKSFSEFESFEGGFLAVDDAGKIIGVGQDYHAWASSNPAHAKGLTEVHLSDYQFLMPGFVDCHIHAPQFAQLGLGLDMPLLDWLNTYTFPLEAKFSNHQYAQQVYQGVVEATLRCGTTLASYFATNHLESTLTLAREAVRQGQRALIGKVCSNCNSPEFYVETAEESVSATLAFVEGVRKLGSPMVMPTITPRFALSCSKELLKSLGDIAKRFDLHIQSHISENLEEIEMVKGIFKTSYAGAYDEAGLLTNKTVLAHGVHLEDDEVALLKVRGCSVAHCPTSNTMLSSGLCDVQRLVSGGVSVGLGTDVSGGNSVSIQDVLLRALDVSKHLDFFKKQNIRGTGVSKTQDFNYHQLKYKQALYLATLGGAKALSLDHLTGNFALGKDFDALLVDVSVVDKPLRRLSVDELVEKFIYTGSDRNIVEVFVAGKRIKQGYQ
Protein: Pyrroline-5-carboxylate reductase 1, mitochondrial (P5C reductase 1) (P5CR 1) (EC 1.5.1.2) (Q922W5)
Organism: Mus musculus (Mouse)
Function: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P32322}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Proline dehydrogenase 1, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
- Hydroxyproline dehydrogenase
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-3
- Prolyl 4-hydroxylase subunit alpha-1
- Cytosol aminopeptidase
Sequence:
MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTRELQTMADQETISPAAIKKTVLDKVKLDSSAGASLSSDHVKPLP
Protein: BBSome-interacting protein 1 (BBSome-interacting protein of 10 kDa) (Q1L8Y6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for primary cilia assembly.
Subcellular location: Cell projection, cilium {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Bardet-Biedl syndrome 1.
- Bardet-Biedl syndrome 7 protein homolog
- BBSome complex member BBS2
- Bardet-Biedl syndrome 9.
- BBSome complex member BBS5
- Tetratricopeptide repeat domain 8.
- Bardet-Biedl syndrome 12
- Bardet-Biedl syndrome 10.
- Leucine zipper transcription factor-like 1.
Sequence:
MPEVKSMFREVLPKQGQLSMEDVPTMVLCKPKLLPLKSVTLEKLEKMQKDAQEIIRQQELALKEQPPSEKAE
Protein: Cyclic AMP-responsive element-binding protein 3-like protein 2 (cAMP-responsive element-binding protein 3-like protein 2) (SCI-related protein Ra69) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 2] (Q6QDP7)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes. In a neuroblastoma cell line, protects cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BH52}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8BH52}. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 2]: Nucleus {ECO:0000250|UniProtKB:Q8BH52}. Note=Upon ER stress, translocated into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Atf6b protein
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- cAMP-responsive element modulator
- Cyclic AMP-dependent transcription factor ATF-4
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- histone acetyltransferase
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Mitogen-activated protein kinase 3
- CREB-regulated transcription coactivator 2
Sequence:
MEVLESGEQSVLQWDRKLSELSEPGETEALMYHTHFSELLDEFSQNVLGQLLNDPFLSEKSVSMEVEPSPTSPAPLIQAEHSYSLSEEPRAQSPFTHVAASDGFNDEEVESEKWYLSTEFPSATIKTEPITEEQPPGLVPSVTLTITAISTPFEKEESPLDMSAGGDSSCQTLIPKIKLEPHEVDQFLNFSPKEASVDQLHLPPTPPSSHSSDSEGSLSPNPRLHPFSLSQAHSPGRAMPRGPSALSTSPLLTAPHKLQGSGPLVLTEEEKRTLIAEGYPIPTKLPLTKSEEKALKKIRRKIKNKISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNRTLLQQLQKLQTLVMGKVSRTCKLAGTQTGTCLMVVVLCFAVAFGSLFQGYGLYPSATKMALPSQHPLSEPYTASVVRSRNLLIYEEHSSLEESSSPASAGELGGWDRGSSLLRASSGLEALPEVDLPHFIISKETSLEKSVLLELQQHLVSSKLEGNETLKVVELERRVNATF
Protein: C-C motif chemokine ligand 9 (Ccl9-like protein) (Chemokine (C-C motif) ligand 9) (Chemokine CCL9) (Q5FVN3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Macrophage inflammatory protein-1 alpha receptor
- Chemokine
- C-C chemokine receptor type 5
- C-C motif chemokine 2
- C-X-C chemokine receptor type 3
- C-C chemokine receptor type 3
- C-C motif chemokine receptor 8
- C-C motif chemokine receptor 7
- C-C motif chemokine
- CX3C chemokine receptor 1
Sequence:
MKPFHTALSFLIFAATLGIQAQIVHATETREVLKAEQGHQLFSLGFQDSSDCCLSYTSRVHCSRYKNYFPTSGGCTKPAIIFVSKKGTLVCANPSDLRVQKCIKRLEQNSQPQIYKQ
Protein: C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Pre-B-cell-derived chemokine receptor) (PB-CKR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184) (P70658)
Organism: Mus musculus (Mouse)
Function: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8962122, ECO:0000269|PubMed:9295051}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (By similarity). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (By similarity). {ECO:0000250}.
Interaction partners:
- Stromal cell-derived factor 1
- C-C motif chemokine 5
- C-C motif chemokine 2
- T-cell surface glycoprotein CD4
- C-X-C motif chemokine 10
- Growth-regulated alpha protein
- C-X-C motif chemokine 13
- C-C motif chemokine 19
- Fractalkine
- CD44 antigen
Sequence:
MEPISVSIYTSDNYSEEVGSGDYDSNKEPCFRDENVHFNRIFLPTIYFIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAMADWYFGKFLCKAVHIIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKAVYVGVWIPALLLTIPDFIFADVSQGDISQGDDRYICDRLYPDSLWMVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYVGISIDSFILLGVIKQGCDFESIVHKWISITEALAFFHCCLNPILYAFLGAKFKSSAQHALNSMSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
Protein: Antimicrobial peptide 2 (Cn-AMP2) (P86706)
Organism: Cocos nucifera (Coconut palm)
Function: Has antimicrobial activity against Gram-positive bacteria B.subtilis (MIC=150 ug/ml) and S.aureus (MIC=170 ug/ml), and against Gram-negative bacteria E.coli (MIC=170 ug/ml) and P.aeruginosa (MIC=169 ug/ml).
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:19111587}.
Interaction partners:
Sequence:
TESYFVFSVGM
Protein: LD36294p (Q960T4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLGEGRYRGWHKPIPPSPSILFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAERVVCAGDSAGANLSIGVALKCIEQGVRVPDGLFLAYCPTLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPAQETLQQNAKQVEDAAQIRNVPKSNVGSLNSSRRTSMARSPLSPLEASMNPDDESSDTFASASASYHSQTVERTDLPHTEGDNSSCVSFEDDSQPIVHYPIEISADPPKDTASAAYIDNFLDKYLIDTATMEVTEETAPEAVQAQANGHAKISSDDDILVETGRDLVAIDTLQGRLQEAVNNITNTLTRCTQSYEIHGSNVMAQQDVRNMDALIARSPSEEFAFDVPKDPFLSPYWASDEWLSQLPETKILTLNMDPCLDDCVMFAKKLKRLGRQVDLEILEGLPHGFLNFTMLSNEAMEGSKKCIKSLQTLLQTDSKTKNIDKANSMDEEESSSPSASLAAS
Protein: Zinc finger homeobox protein 2 (Zinc finger homeodomain protein 5) (Q2MHN3)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that is critical for the regulation of pain perception and processing of noxious stimuli.
Subcellular location: Nucleus {ECO:0000269|PubMed:29253101}.
Interaction partners:
Sequence:
MATLNSASPSGTVPSPGHNVRSPPPETSSSSTSDPVTKDPPDAPSTSESIRSSEPGGERLESGSDLDPPKEIGEPQEEPGCGHIPPKDLGVAKEEEEILPLDLSSHLFFAAGGQAYLLANLPLPRGSELSLPKGFPWDEASAKEEPSLPLLTHFPSSHLTTLHIQHGFDPIQGFSSSDQMLSHDTSAPSLAACERRDGSFWSYQLVPNPTEDPKDGPLGSRREDHRAMFWICLLCRLGFGRLQTFIGHTLSHGVKLSPAHHQGLLGSPAVLQEGHDGGMALLSFLEPKFLTRPSPEVPDTSTVTVKTNGAQAEDGPPEADGQALVLPAEEVIALSPPSPPTALATWDPSPTQAKDSPVPRGEAGPDWFPEGQEEDGGLCLPLNQSSPTSKEVAVLPAPAGSPEDTSDPPPSCRLADDYTPAPAAFQGLSLSSHMSLLHSRNSCKTLKCPKCNWHYKYQQTLDVHMREKHPESNSHCSYCSAGGAHPRLARGESYNCGYKPYRCDVCNYSTTTKGNLSIHMQSDKHLANLQGFQAGPGGQASPPEASLPPTSVGDKEPKTKSSWQCKVCSYETNISRNLRIHMTSEKHMQNVLMLHQGLPLGLPPGLVGPGPPPPPGAAPTNPPELFQYFGPQALGQPQTPMPGPGLRPDKPLEAQLLLNGFHHLGAPARKFPTAAPGSLSPETHLPPSQLLGSSSDGLPTSPSPDDSPALKVFRCLVCQAFSTDSLELLLYHCSIGRSLPEAEWKEVAGDTHRCKLCCYGTQLKANFQLHLKTDKHTQKYQLAAHLREGGGAMGTPSLLALGDGASYGSISPLHLRCNICDFESNSKEKMQLHTRGSAHEENSQIYKFLLEMEGAEAGPEPGLYHCLLCAWDTPSRLALLQHLRTPAHRDAQAQRRLQLLQNGPAAEEGLSALQSILSFSHGRLQTPGKASDTPLAQPPTSEKDAQNKTEQQASEVTEDRSGPPRDSANQITVFCCPYCSFLSPECDQVRVHTLSQHAVQPKYRCPLCQEQLVGRPALHFHLSHLHNVVPECVEKLLLVATTVEMTFATKMLPGPTLNPVEDGLDHPAPGAEPTPNRDQVAESSNLAPEVSPDPPLEPPLAPVEGSREPSESPDQPPSPAPSPAPRLDAQVEELAPLPTMSEEEEGAMGEPRSAEPTPADSRHPLTYRKTTNFALDKFLDPARPYKCTVCKESFTQKNILLVHYNSVSHLHKMKKAAIDPSGPARGEAGIPPPAATASDKPFKCTVCRVSYNQSSTLEIHMRSVLHQTRSRGAKIDARAEGAERGQEEFKEGETEGEAGTEKKGPDPGGFMSGLPFLSPPPPPLDLHRFSAPLFTPPVLPPFPLVPESLLKLQQQQLLLPFYLHDLKVGPKLALASPTPMLSLPAANPPPLPAPPKAELAEQEWERPLMAEEGTEAGPSSPTHTSPNEAARTAAKALLENFGFELVIQYNEGKQAVPPPPTPPPPESLGGGDKLACGACGKLFSNMLILKTHEEHVHRRFLPFEALSRYAAQFRKSYDSLYPPPVEPPKPPDGCLESPPQLGPPFVVPEPEVGGIHTSEERSLSGGGPWPSEEEEGSRGSLPPAVPVGRRFSRTKFTEFQTQALQSFFETSAYPKDGEVERLASLLGLASRVVVVWFQNARQKARKNACEGGPVTAGGASGGASGCRRCHATFACVFELVRHLKKCYDDQPPEEEEEAERGEEEEEVEEEEAEERNLEPAAARPGGPSPEHADGEDLSQTEPTRPESKESEGKAPPSPPVYACDQCAASFPSQDLLTTHHRLHLLPSVQPSAPPPSQLLDLPLLVFGERNPVVSGTSSVTGTPLKRKHDDGSLSPTGSEAGGGGEGEPPKDKRLRTTILPEQLEILYRWYMQDSNPTRKMLDCISEEVGLKKRVVQVWFQNTRARERKGQFRSTPGGVAGPAVKPTVPPSPAPFPKFNLLLSKIEDETGKEAPKRDAPAFPYPTVTPAVGPLPFLPPGKEAAVPTPEPPPPLPPPALSEDEGPEEPSKASPESEACSPSAGDLSDSSASSLAEPESPGAGGTSGGPGGGTGVPDSMGQRRYRTQMSSLQLKIMKACYEAYRTPTMQECEVLGEEIGLPKRVIQVWFQNARAKEKKAKLQGTAPPGSGGSSEGTSAAQRTDCPYCDVKYDFYVSCRGHLFSRQHLAKLKEAVRAQLKSESKCYDLAPAPETPLAPKGPPATTPASSVPLGASPTLPRLAPVLLPGPTLAQPPLGSIASFNSGPAASSGLLGLATSVLPATTVVQTAGPGRPLPQRPVSNQTNSSTDPTPGPATEPSGDKVSGERKPVATLPNSSTDALKNLKALKATVPALLGGQFLPFPLPPAGGAAPPAVFGPQLQGAYFQQLYGMKKGLFPMNPVIPQTLIGLLPNALLQQPPQAPEPTATAPPKPPELPASGEGESSEADELLTGSTGISTVDVTHRYLCRQCKMAFDGEAPATAHQRSFCFFGRGSGASMPAPLRVPICTYHCLACEVLLSGREALASHLRSSAHRRKAAPPPGGPPITVTNSATAVPAAVAFAKEEARLPHTDPNPKTTTTSTLLAL
Protein: Antifungal protein ginkbilobin-2 (Antimicrobial protein Gnk2-1) (A4ZDL6)
Organism: Ginkgo biloba (Ginkgo) (Maidenhair tree)
Function: Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity. Exerts antifungal activity against S.cerevisiae and F.culmorum through its carbohydrate-binding specificity. Acts as a lectin that stricly recognizes alpha-1,2-linked mannose moieties and interacts with the yeast cell wall mannan polysaccharide. Can interfere with the fungal actin remodeling resulting to the activation of an actin-dependent cell death.
Subcellular location: Secreted {ECO:0000269|PubMed:26315821}.
Interaction partners:
Sequence:
MKTMRMNSAFILAFALAAAMLILTEAANTAFVSSACNTQKIPSGSPFNRNLRAMLADLRQNTAFSGYDYKTSRAGSGGAPTAYGRATCKQSISQSDCTACLSNLVNRIFSICNNAIGARVQLVDCFIQYEQRSF