KHDR2_HUMAN - dbPTM
KHDR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KHDR2_HUMAN
UniProt AC Q5VWX1
Protein Name KH domain-containing, RNA-binding, signal transduction-associated protein 2
Gene Name KHDRBS2
Organism Homo sapiens (Human).
Sequence Length 349
Subcellular Localization Nucleus .
Protein Description RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability (By similarity). Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. Can regulate alternative splicing of NRXN1 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its phosphorylation by FYN inhibits its ability to regulate splice site selection. May function as an adapter protein for Src kinases during mitosis..
Protein Sequence MEEEKYLPELMAEKDSLDPSFVHASRLLAEEIEKFQGSDGKKEDEEKKYLDVISNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKAKEEELRKSGEAKYAHLSDELHVLIEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQLRELSYLNGSEDSGRGRGIRGRGIRIAPTAPSRGRGGAIPPPPPPGRGVLTPRGSTVTRGALPVPPVARGVPTPRARGAPTVPGYRAPPPPAHEAYEEYGYDDGYGGEYDDQTYETYDNSYATQTQSVPEYYDYGHGVSEDAYDSYAPEEWATTRSSLKAPPQRSARGGYREHPYGRY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MEEEKYLPELMAE
--CCHHHHHHHHHHC
30.6720068231
16PhosphorylationELMAEKDSLDPSFVH
HHHHCCCCCCHHHHH
45.8226074081
20PhosphorylationEKDSLDPSFVHASRL
CCCCCCHHHHHHHHH
39.3024719451
25PhosphorylationDPSFVHASRLLAEEI
CHHHHHHHHHHHHHH
14.4826074081
54O-linked_GlycosylationKKYLDVISNKNIKLS
HHHHHHHHCCCCCCC
41.4230379171
56AcetylationYLDVISNKNIKLSER
HHHHHHCCCCCCCCC
53.9430589657
69AcetylationERVLIPVKQYPKFNF
CCEEEEHHHCCCCCC
38.47163895
69UbiquitinationERVLIPVKQYPKFNF
CCEEEEHHHCCCCCC
38.4721890473
73UbiquitinationIPVKQYPKFNFVGKL
EEHHHCCCCCCHHHH
48.2673
73AcetylationIPVKQYPKFNFVGKL
EEHHHCCCCCCHHHH
48.2622647397
79MethylationPKFNFVGKLLGPRGN
CCCCCHHHHHCCCCH
34.9372622551
79AcetylationPKFNFVGKLLGPRGN
CCCCCHHHHHCCCCH
34.9372622551
95PhosphorylationLKRLQEETGAKMSIL
HHHHHHHHCCCEEHH
41.5120068231
100PhosphorylationEETGAKMSILGKGSM
HHHCCCEEHHCCCHH
17.6020068231
106PhosphorylationMSILGKGSMRDKAKE
EEHHCCCHHHHHHHH
17.7120068231
112AcetylationGSMRDKAKEEELRKS
CHHHHHHHHHHHHHH
71.9819818047
117MethylationKAKEEELRKSGEAKY
HHHHHHHHHHCCHHH
34.08-
119PhosphorylationKEEELRKSGEAKYAH
HHHHHHHHCCHHHHC
35.1224719451
128PhosphorylationEAKYAHLSDELHVLI
CHHHHCHHHCCEEEE
21.1224719451
146PhosphorylationAPPGEAYSRMSHALE
CCCCHHHHHHHHHHH
28.6724719451
163PhosphorylationKKFLVPDYNDEIRQE
HHHHCCCCCHHHHHH
20.60-
230MethylationPRGSTVTRGALPVPP
CCCCCCCCCCCCCCC
24.85-
240MethylationLPVPPVARGVPTPRA
CCCCCCCCCCCCCCC
47.04-
244PhosphorylationPVARGVPTPRARGAP
CCCCCCCCCCCCCCC
24.0124719451
346PhosphorylationGGYREHPYGRY----
CCCCCCCCCCC----
19.01-
348MethylationYREHPYGRY------
CCCCCCCCC------
28.30-
349PhosphorylationREHPYGRY-------
CCCCCCCC-------
20.6728112733

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KHDR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KHDR2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KHDR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX17_HUMANDDX17physical
17643375
DDX5_HUMANDDX5physical
17643375
ROA1_HUMANHNRNPA1physical
17643375
ROA2_HUMANHNRNPA2B1physical
17643375
HNRH1_HUMANHNRNPH1physical
17643375
HNRPK_HUMANHNRNPKphysical
17643375
HNRPR_HUMANHNRNPRphysical
17643375
HNRPQ_HUMANSYNCRIPphysical
17643375
HNRPC_HUMANHNRNPCphysical
17643375
IF2B1_HUMANIGF2BP1physical
17643375
ANM1_HUMANPRMT1physical
17643375
ILF2_HUMANILF2physical
17643375
KHDR1_HUMANKHDRBS1physical
17643375
RBMX_HUMANRBMXphysical
17643375
HNRDL_HUMANHNRNPDLphysical
17643375
EHBP1_HUMANEHBP1physical
17643375
ARID2_HUMANARID2physical
17643375
TAF3_HUMANTAF3physical
17643375
DSG1_HUMANDSG1physical
17643375
ROA0_HUMANHNRNPA0physical
17643375
IF2B3_HUMANIGF2BP3physical
17643375
HNRPL_HUMANHNRNPLphysical
17643375
HNRL2_HUMANHNRNPUL2physical
17643375
RBM39_HUMANRBM39physical
17643375
ILF3_HUMANILF3physical
17643375
HNRH3_HUMANHNRNPH3physical
17643375
ANM5_HUMANPRMT5physical
17643375
RS3_HUMANRPS3physical
17643375
FIBA_HUMANFGAphysical
17643375
YBOX1_HUMANYBX1physical
17643375
FIBG_HUMANFGGphysical
17643375
HNRPD_HUMANHNRNPDphysical
17643375
RT27_HUMANMRPS27physical
17643375
TADBP_HUMANTARDBPphysical
17643375
NUSAP_HUMANNUSAP1physical
17643375
SAFB1_HUMANSAFBphysical
17643375
MEP50_HUMANWDR77physical
17643375
MOV10_HUMANMOV10physical
17643375
HORN_HUMANHRNRphysical
17643375
KHDR3_HUMANKHDRBS3physical
17643375
FIBB_HUMANFGBphysical
17643375
DEK_HUMANDEKphysical
17643375
FBW1B_HUMANFBXW11physical
17643375
LRC15_HUMANLRRC15physical
17643375
HS90B_HUMANHSP90AB1physical
17643375
KHDR2_HUMANKHDRBS2physical
25416956
TYMOS_HUMANTYMSOSphysical
25416956
ATX2_HUMANATXN2physical
26344197
DDX43_HUMANDDX43physical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
HNRPQ_HUMANSYNCRIPphysical
26344197
KHDR2_HUMANKHDRBS2physical
21516116
TYK2_HUMANTYK2physical
21516116
TM14B_HUMANTMEM14Bphysical
21516116
KHDR3_HUMANKHDRBS3physical
28514442
FBW1B_HUMANFBXW11physical
28514442
FBW1A_HUMANBTRCphysical
28514442
ATG7_HUMANATG7physical
28514442
KHDR1_HUMANKHDRBS1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
YRDC_HUMANYRDCphysical
28514442
CRBN_HUMANCRBNphysical
28514442
PLCG1_HUMANPLCG1physical
28514442
PTER_HUMANPTERphysical
28514442
ACOX1_HUMANACOX1physical
28514442
RFWD2_HUMANRFWD2physical
28514442
CUL1_HUMANCUL1physical
28514442
SPT5H_HUMANSUPT5Hphysical
28514442
KLH42_HUMANKLHL42physical
28514442
UBP7_HUMANUSP7physical
28514442
CTC1_HUMANCTC1physical
28514442
ACD11_HUMANACAD11physical
28514442
NAGK_HUMANNAGKphysical
28514442
THIK_HUMANACAA1physical
28514442
MK03_HUMANMAPK3physical
28514442
AURKA_HUMANAURKAphysical
28514442
KIME_HUMANMVKphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KHDR2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND MASS SPECTROMETRY.

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