WHRN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: WHRN_HUMAN
• UniProt AC: Q9P202
• Protein Name: Whirlin {ECO:0000305}
• Gene Name: WHRN {ECO:0000312|HGNC:HGNC:16361}
• Organism: Homo sapiens (Human).
• Sequence Length: 907
• Subcellular Localization: Cytoplasm. Cell projection, stereocilium. Cell projection, growth cone. Detected at the level of stereocilia in inner outer hair cells of the cochlea and vestibule. Colocalizes with the growing ends of actin filaments (By similarity). Colocalizes wit
• Protein Description: Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear..
• Protein Sequence: MNAPLDGLSVSSSSTGSLGSAAGAGGGGGAGLRLLSANVRQLHQALTALLSEAEREQFTHCLNAYHARRNVFDLVRTLRVLLDSPVKRRLLPMLRLVIPRSDQLLFDQYTAEGLYLPATTPYRQPAWGGPDSAGPGEVRLVSLRRAKAHEGLGFSIRGGSEHGVGIYVSLVEPGSLAEKEGLRVGDQILRVNDKSLARVTHAEAVKALKGSKKLVLSVYSAGRIPGGYVTNHIYTWVDPQGRSISPPSGLPQPHGGALRQQEGDRRSTLHLLQGGDEKKVNLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAEGSGLKVGDQILEVNGRSFLNILHDEAVRLLKSSRHLILTVKDVGRLPHARTTVDETKWIASSRIRETMANSAGFLGDLTTEGINKPGFYKGPAGSQVTLSSLGNQTRVLLEEQARHLLNEQEHATMAYYLDEYRGGSVSVEALVMALFKLLNTHAKFSLLSEVRGTISPQDLERFDHLVLRREIESMKARQPPGPGAGDTYSMVSYSDTGSSTGSHGTSTTVSSARNTLDLEETGEAVQGNINALPDVSVDDVRSTSQGLSSFKPLPRPPPLAQGNDLPLGQPRKLGREDLQPPSSMPSCSGTVFSAPQNRSPPAGTAPTPGTSSAQDLPSSPIYASVSPANPSSKRPLDAHLALVNQHPIGPFPRVQSPPHLKSPSAEATVAGGCLLPPSPSGHPDQTGTNQHFVMVEVHRPDSEPDVNEVRALPQTRTASTLSQLSDSGQTLSEDSGVDAGEAEASAPGRGRQSVSTKSRSSKELPRNERPTDGANKPPGLLEPTSTLVRVKKSAATLGIAIEGGANTRQPLPRIVTIQRGGSAHNCGQLKVGHVILEVNGLTLRGKEHREAARIIAEAFKTKDRDYIDFLVTEFNVML

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
84	Phosphorylation	TLRVLLDSPVKRRLL HHHHHHCCHHHHHHH	31.40	28674419
101	Phosphorylation	LRLVIPRSDQLLFDQ HHHEECCCHHEECCE	25.10	24043423
109	Phosphorylation	DQLLFDQYTAEGLYL HHEECCEECCCCEEE	15.12	24043423
110	Phosphorylation	QLLFDQYTAEGLYLP HEECCEECCCCEEEC	16.76	24043423
115	Phosphorylation	QYTAEGLYLPATTPY EECCCCEEECCCCCC	22.84	24043423
119	Phosphorylation	EGLYLPATTPYRQPA CCEEECCCCCCCCCC	26.77	22210691
120	Phosphorylation	GLYLPATTPYRQPAW CEEECCCCCCCCCCC	22.04	24043423
122	Phosphorylation	YLPATTPYRQPAWGG EECCCCCCCCCCCCC	21.56	22210691
142	Phosphorylation	PGEVRLVSLRRAKAH CCCEEEEEEEECCCC	22.28	24719451
206	Ubiquitination	VTHAEAVKALKGSKK CCHHHHHHHHCCCCE	55.86	-
211	Phosphorylation	AVKALKGSKKLVLSV HHHHHCCCCEEEEEE	25.65	24719451
217	Phosphorylation	GSKKLVLSVYSAGRI CCCEEEEEEEECCCC	16.13	25072903
219	Phosphorylation	KKLVLSVYSAGRIPG CEEEEEEEECCCCCC	6.88	24719451
220	Phosphorylation	KLVLSVYSAGRIPGG EEEEEEEECCCCCCC	23.30	24719451
234	Phosphorylation	GYVTNHIYTWVDPQG CEECCEEEEEECCCC	6.23	27642862
243	Phosphorylation	WVDPQGRSISPPSGL EECCCCCCCCCCCCC	33.95	23663014
245	Phosphorylation	DPQGRSISPPSGLPQ CCCCCCCCCCCCCCC	31.82	23663014
248	Phosphorylation	GRSISPPSGLPQPHG CCCCCCCCCCCCCCC	57.24	23312004
372	O-linked_Glycosylation	ARTTVDETKWIASSR CCCCCCHHHHHHHHH	27.50	31492838
373	Ubiquitination	RTTVDETKWIASSRI CCCCCHHHHHHHHHH	34.26	-
387	Phosphorylation	IRETMANSAGFLGDL HHHHHHHCCCHHHCC	21.89	23532336
395	Phosphorylation	AGFLGDLTTEGINKP CCHHHCCCCCCCCCC	27.78	29978859
396	Phosphorylation	GFLGDLTTEGINKPG CHHHCCCCCCCCCCC	39.24	29978859
405	Phosphorylation	GINKPGFYKGPAGSQ CCCCCCCCCCCCCCC	22.43	23532336
411	Phosphorylation	FYKGPAGSQVTLSSL CCCCCCCCCEEEHHH	24.47	-
482	Phosphorylation	LLSEVRGTISPQDLE HHHHHCCCCCHHHHH	14.02	28842319
517	Phosphorylation	GPGAGDTYSMVSYSD CCCCCCCEEEEEEEC	10.25	-
521	Phosphorylation	GDTYSMVSYSDTGSS CCCEEEEEEECCCCC	15.41	-
525	Phosphorylation	SMVSYSDTGSSTGSH EEEEEECCCCCCCCC	32.78	-
529	Phosphorylation	YSDTGSSTGSHGTST EECCCCCCCCCCCCC	44.38	-
572	Phosphorylation	SVDDVRSTSQGLSSF CHHHHHHCCCCHHCC	17.95	-
577	Phosphorylation	RSTSQGLSSFKPLPR HHCCCCHHCCCCCCC	40.32	-
647	Phosphorylation	SSAQDLPSSPIYASV CCCHHCCCCCCEEEC	56.92	27642862
648	Phosphorylation	SAQDLPSSPIYASVS CCHHCCCCCCEEECC	17.24	27642862
651	Phosphorylation	DLPSSPIYASVSPAN HCCCCCCEEECCCCC	9.01	27642862
685	Phosphorylation	GPFPRVQSPPHLKSP CCCCCCCCCCCCCCC	37.23	25159151
746	Phosphorylation	RALPQTRTASTLSQL HCCCCCCCHHHHHHH	28.48	25954137
751	Phosphorylation	TRTASTLSQLSDSGQ CCCHHHHHHHHHCCC	23.59	25954137
754	Phosphorylation	ASTLSQLSDSGQTLS HHHHHHHHHCCCCCC	25.06	25954137
759	Phosphorylation	QLSDSGQTLSEDSGV HHHHCCCCCCCCCCC	35.46	25954137
787	Phosphorylation	RQSVSTKSRSSKELP CCCCCCCCCCCCCCC	37.17	22817900
875	Acetylation	NGLTLRGKEHREAAR CCEEECCHHHHHHHH	43.86	7365163
901	Phosphorylation	DYIDFLVTEFNVML- HHHHEEEEEEECCC-	36.69	30619164

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of WHRN_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
245	Phosphorylation	255 (10)	G ⇒ D	rs79509430	Obesity-related traits	23251661

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBK1_HUMAN	TBK1	physical	27173435
TBKB1_HUMAN	TBKBP1	physical	27173435
CRCM_HUMAN	MCC	physical	27173435
PAXI_HUMAN	PXN	physical	27173435
WDTC1_HUMAN	WDTC1	physical	27173435
ANR28_HUMAN	ANKRD28	physical	27173435
XPP3_HUMAN	XPNPEP3	physical	27173435
VIME_HUMAN	VIM	physical	27173435

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 607084: Deafness, autosomal recessive, 31 (DFNB31)
• 611383: Usher syndrome 2D (USH2D)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND MASSSPECTROMETRY.
PubMed: 18187866