dbPTM

STOM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STOM_HUMAN
UniProt AC	P27105
Protein Name	Erythrocyte band 7 integral membrane protein
Gene Name	STOM
Organism	Homo sapiens (Human).
Sequence Length	288
Subcellular Localization	Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, cytoskeleton . Cell membrane Lipid-anchor Cytoplasmic side . Membrane raft . Melanosome . Cytoplasmic vesicle . Localizes to juxtanuclear structure probably derived from
Protein Description	Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity..
Protein Sequence	MAEKRHTRDSEAQRLPDSFKDSPSKGLGPCGWILVAFSFLFTVITFPISIWMCIKIIKEYERAIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEILTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNVLGTKNLSQILSDREEIAHNMQSTLDDATDAWGIKVERVEIKDVKLPVQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIIGAKHSHLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Ubiquitination	----MAEKRHTRDSE ----CCCCCCCCCHH	39.68	-
7	Phosphorylation	-MAEKRHTRDSEAQR -CCCCCCCCCHHHHC	39.96	30242111
10	Phosphorylation	EKRHTRDSEAQRLPD CCCCCCCHHHHCCCH	31.38	25159151
18	Phosphorylation	EAQRLPDSFKDSPSK HHHCCCHHHCCCCCC	32.05	22167270
20	Ubiquitination	QRLPDSFKDSPSKGL HCCCHHHCCCCCCCC	62.34	-
20	Acetylation	QRLPDSFKDSPSKGL HCCCHHHCCCCCCCC	62.34	27452117
22	Phosphorylation	LPDSFKDSPSKGLGP CCHHHCCCCCCCCCH	31.50	22167270
24	Phosphorylation	DSFKDSPSKGLGPCG HHHCCCCCCCCCHHH	43.22	22167270
30	S-palmitoylation	PSKGLGPCGWILVAF CCCCCCHHHHHHHHH	7.19	10338112
58	Acetylation	WMCIKIIKEYERAII HHHHHHHHHHHHHHH	58.69	27452117
58	2-Hydroxyisobutyrylation	WMCIKIIKEYERAII HHHHHHHHHHHHHHH	58.69	-
60	Phosphorylation	CIKIIKEYERAIIFR HHHHHHHHHHHHHHH	13.00	21951684
77	Ubiquitination	RILQGGAKGPGLFFI HHHHCCCCCCCEEEE	69.76	-
87	S-palmitoylation	GLFFILPCTDSFIKV CEEEEEECCCCEEEE	6.22	10338112
90	Phosphorylation	FILPCTDSFIKVDMR EEEECCCCEEEEEEE	15.66	24719451
93	Sumoylation	PCTDSFIKVDMRTIS ECCCCEEEEEEEEEE	30.12	-
115	Phosphorylation	ILTKDSVTISVDGVV HCCCCCEEEEECCEE	16.10	24719451
123	Phosphorylation	ISVDGVVYYRVQNAT EEECCEEEEEEECCE	5.33	21951684
124	Phosphorylation	SVDGVVYYRVQNATL EECCEEEEEEECCEE	7.84	21951684
137	Phosphorylation	TLAVANITNADSATR EEEEEECCCCHHHHH	24.94	20071362
157	Phosphorylation	TLRNVLGTKNLSQIL HHHHHHCCCCHHHHH	16.76	27174698
158	2-Hydroxyisobutyrylation	LRNVLGTKNLSQILS HHHHHCCCCHHHHHC	54.84	-
161	Phosphorylation	VLGTKNLSQILSDRE HHCCCCHHHHHCCHH	25.27	23025827
165	Phosphorylation	KNLSQILSDREEIAH CCHHHHHCCHHHHHH	35.93	27174698
188	Ubiquitination	ATDAWGIKVERVEIK HHHHCCCEEEEEEEE	33.82	-
188	Sumoylation	ATDAWGIKVERVEIK HHHHCCCEEEEEEEE	33.82	-
188	Sumoylation	ATDAWGIKVERVEIK HHHHCCCEEEEEEEE	33.82	-
195	2-Hydroxyisobutyrylation	KVERVEIKDVKLPVQ EEEEEEEECCCCCHH	42.85	-
198	Ubiquitination	RVEIKDVKLPVQLQR EEEEECCCCCHHHHH	58.15	-
198	2-Hydroxyisobutyrylation	RVEIKDVKLPVQLQR EEEEECCCCCHHHHH	58.15	-
220	Ubiquitination	ASREARAKVIAAEGE HHHHHHHHHHHHHHC	28.72	-
220	2-Hydroxyisobutyrylation	ASREARAKVIAAEGE HHHHHHHHHHHHHHC	28.72	-
228	Sulfoxidation	VIAAEGEMNASRALK HHHHHHCCCHHHHHH	8.15	21406390
231	Phosphorylation	AEGEMNASRALKEAS HHHCCCHHHHHHHHC	17.06	25159151
235	Ubiquitination	MNASRALKEASMVIT CCHHHHHHHHCEEEE	50.69	-
235	2-Hydroxyisobutyrylation	MNASRALKEASMVIT CCHHHHHHHHCEEEE	50.69	-
238	Phosphorylation	SRALKEASMVITESP HHHHHHHCEEEECCC	18.05	29214152
239	Sulfoxidation	RALKEASMVITESPA HHHHHHCEEEECCCH	3.05	21406390
242	Phosphorylation	KEASMVITESPAALQ HHHCEEEECCCHHHH	20.99	21815630
244	Phosphorylation	ASMVITESPAALQLR HCEEEECCCHHHHHH	15.93	25159151
252	Phosphorylation	PAALQLRYLQTLTTI CHHHHHHHHHHHHHH	16.26	28152594
255	Phosphorylation	LQLRYLQTLTTIAAE HHHHHHHHHHHHHHH	24.39	20860994
257	Phosphorylation	LRYLQTLTTIAAEKN HHHHHHHHHHHHHCC	21.39	20860994
258	Phosphorylation	RYLQTLTTIAAEKNS HHHHHHHHHHHHCCC	16.25	21406692
283	Ubiquitination	LQGIIGAKHSHLG-- HHHHHHCCCCCCC--	40.19	-

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
10	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
10	S	Phosphorylation	Kinase	PKA	-	Uniprot
10	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STOM_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 STOM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GTR1_HUMAN	SLC2A1	physical	10562431
STOM_HUMAN	STOM	physical	9642292
RUVB2_HUMAN	RUVBL2	physical	10524211
RUVB1_HUMAN	RUVBL1	physical	10524211
TCPQ_HUMAN	CCT8	physical	26344197
ASIC3_HUMAN	ASIC3	physical	15471860
ASIC2_HUMAN	ASIC2	physical	15471860
ASIC1_HUMAN	ASIC1	physical	15471860
SEPR_HUMAN	FAP	physical	26209915
CAND2_HUMAN	CAND2	physical	27173435

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STOM_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Cysteine 29 is the major palmitoylation site on stomatin."; Snyers L., Umlauf E., Prohaska R.; FEBS Lett. 449:101-104(1999). Cited for: PALMITOYLATION AT CYS-30 AND CYS-87.	10338112 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Identification of the phosphorylation site on human erythrocyte band7 integral membrane protein: implications for a monotopic proteinstructure."; Salzer U., Ahorn H., Prohaska R.; Biochim. Biophys. Acta 1151:149-152(1993). Cited for: PROTEIN SEQUENCE OF 5-25, AND PHOSPHORYLATION AT SER-10.	8373790 [Abstract]