DKKL1_HUMAN - dbPTM
DKKL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DKKL1_HUMAN
UniProt AC Q9UK85
Protein Name Dickkopf-like protein 1 {ECO:0000305}
Gene Name DKKL1 {ECO:0000312|HGNC:HGNC:16528}
Organism Homo sapiens (Human).
Sequence Length 242
Subcellular Localization Secreted . Cytoplasmic vesicle, secretory vesicle, acrosome . Localized specifically to the crescent shaped acrosome at the apex of the sperm head.
Protein Description Involved in fertilization by facilitating sperm penetration of the zona pellucida. May promotes spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduces testosterone synthesis in Leydig cells. Is not essential either for development or fertility..
Protein Sequence MGEASPPAPARRHLLVLLLLLSTLVIPSAAAPIHDADAQESSLGLTGLQSLLQGFSRLFLKGNLLRGIDSLFSAPMDFRGLPGNYHKEENQEHQLGNNTLSSHLQIDKMTDNKTGEVLISENVVASIQPAEGSFEGDLKVPRMEEKEALVPIQKATDSFHTELHPRVAFWIIKLPRRRSHQDALEGGHWLSEKRHRLQAIRDGLRKGTHKDVLEEGTESSSHSRLSPRKTHLLYILRPSRQL
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
5Phosphorylation---MGEASPPAPARR
---CCCCCCCHHHHH
27.4128122231
97N-linked_GlycosylationNQEHQLGNNTLSSHL
CCCCCCCCCHHHHHE
47.08UniProtKB CARBOHYD
110PhosphorylationHLQIDKMTDNKTGEV
HEEEEECCCCCCCCE
42.0122210691
112N-linked_GlycosylationQIDKMTDNKTGEVLI
EEEECCCCCCCCEEE
34.32UniProtKB CARBOHYD
114PhosphorylationDKMTDNKTGEVLISE
EECCCCCCCCEEEEC
44.8422210691
120PhosphorylationKTGEVLISENVVASI
CCCCEEEECCEEEEE
20.9622210691
126PhosphorylationISENVVASIQPAEGS
EECCEEEEEECCCCC
15.3322210691
158PhosphorylationPIQKATDSFHTELHP
EHHHHCCCCCCCCCH
17.9924719451
223PhosphorylationGTESSSHSRLSPRKT
CCCCCCCCCCCCCCE
36.5420068231
226PhosphorylationSSSHSRLSPRKTHLL
CCCCCCCCCCCEEEE
22.8821955146
230PhosphorylationSRLSPRKTHLLYILR
CCCCCCCEEEEEEEC
21.0227762562
234PhosphorylationPRKTHLLYILRPSRQ
CCCEEEEEEECCCCC
12.3125348772
239PhosphorylationLLYILRPSRQL----
EEEEECCCCCC----
26.6524719451

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 DKKL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DKKL1_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 DKKL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FJX1_HUMANFJX1physical
21988832
PCDGB_HUMANPCDHGA11physical
28514442
PEX6_HUMANPEX6physical
28514442
NUCB1_HUMANNUCB1physical
28514442
PCSK1_HUMANPCSK1Nphysical
28514442
ITIH2_HUMANITIH2physical
28514442
MGT4B_HUMANMGAT4Bphysical
28514442
FAT4_HUMANFAT4physical
28514442
RA51B_HUMANRAD51Bphysical
28514442
XRCC2_HUMANXRCC2physical
28514442
CELR2_HUMANCELSR2physical
28514442
LCHN_HUMANKIAA1147physical
28514442
CANT1_HUMANCANT1physical
28514442
ATS2_HUMANADAMTS2physical
28514442
ITA8_HUMANITGA8physical
28514442
RA51D_HUMANRAD51Dphysical
28514442
CELR3_HUMANCELSR3physical
28514442
DCAM_HUMANAMD1physical
28514442
FREM2_HUMANFREM2physical
28514442
NJMU_HUMANC17orf75physical
28514442
TGBR3_HUMANTGFBR3physical
28514442
LRP5_HUMANLRP5physical
28514442
NLGN2_HUMANNLGN2physical
28514442
HSP13_HUMANHSPA13physical
28514442
CBWD1_HUMANCBWD1physical
28514442
CELR1_HUMANCELSR1physical
28514442
FRAS1_HUMANFRAS1physical
28514442
INT2_HUMANINTS2physical
28514442
AMD_HUMANPAMphysical
28514442
ANM9_HUMANPRMT9physical
28514442
BMP7_HUMANBMP7physical
28514442
SYHM_HUMANHARS2physical
28514442
XPR1_HUMANXPR1physical
28514442
MDN1_HUMANMDN1physical
28514442
HS12A_HUMANHSPA12Aphysical
28514442
FAT3_HUMANFAT3physical
28514442
VWA8_HUMANVWA8physical
28514442
PEX1_HUMANPEX1physical
28514442
PCDH7_HUMANPCDH7physical
28514442
LARG2_HUMANGYLTL1Bphysical
28514442
DPOD2_HUMANPOLD2physical
28514442
ITA7_HUMANITGA7physical
28514442
CO6A2_HUMANCOL6A2physical
28514442
OAF_HUMANOAFphysical
28514442
PCD20_HUMANPCDH20physical
28514442
HTRA1_HUMANHTRA1physical
28514442
GT253_HUMANCERCAMphysical
28514442
SPAT5_HUMANSPATA5physical
28514442
EFTU_HUMANTUFMphysical
28514442
PDPR_HUMANPDPRphysical
28514442
KDIS_HUMANKIDINS220physical
28514442
CPSM_HUMANCPS1physical
28514442
CD109_HUMANCD109physical
28514442
TMPPE_HUMANTMPPEphysical
28514442
FAT1_HUMANFAT1physical
28514442
RPTOR_HUMANRPTORphysical
28514442
SPA5L_HUMANSPATA5L1physical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
INT12_HUMANINTS12physical
28514442
DPOE1_HUMANPOLEphysical
28514442
APLP2_HUMANAPLP2physical
28514442
XYLK_HUMANFAM20Bphysical
28514442
GPR98_HUMANGPR98physical
28514442
RA51C_HUMANRAD51Cphysical
28514442
LTN1_HUMANLTN1physical
28514442
DUSTY_HUMANDSTYKphysical
28514442
TBL3_HUMANTBL3physical
28514442
GALT7_HUMANGALNT7physical
28514442
LRP6_HUMANLRP6physical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
GPD1L_HUMANGPD1Lphysical
28514442
TBB3_HUMANTUBB3physical
28514442
UGDH_HUMANUGDHphysical
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 DKKL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-226, ANDMASS SPECTROMETRY.

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