dbPTM

S39AE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S39AE_HUMAN
UniProt AC	Q15043
Protein Name	Zinc transporter ZIP14
Gene Name	SLC39A14
Organism	Homo sapiens (Human).
Sequence Length	492
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cytoplasm . Cell projection, lamellipodium . Localized to the plasma membrane and also found colocalized with F-actin concentrated on lamellipodiae.
Protein Description	Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron..
Protein Sequence	MKLLLLHPAFQSCLLLTLLGLWRTTPEAHASSLGAPAISAASFLQDLIHRYGEGDSLTLQQLKALLNHLDVGVGRGNVTQHVQGHRNLSTCFSSGDLFTAHNFSEQSRIGSSELQEFCPTILQQLDSRACTSENQENEENEQTEEGRPSAVEVWGYGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPLEDYYVSKSAVVFGGFYLFFFTEKILKILLKQKNEHHHGHSHYASESLPSKKDQEEGVMEKLQNGDLDHMIPQHCSSELDGKAPMVDEKVIVGSLSVQDLQASQSACYWLKGVRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGLAFGILAGSHFSANWIFALAGGMFLYISLADMFPEMNEVCQEDERKGSILIPFIIQNLGLLTGFTIMVVLTMYSGQIQIG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63 (in isoform 1)	Ubiquitination	-	32.42	21906983
63 (in isoform 2)	Ubiquitination	-	32.42	21906983
63	Ubiquitination	SLTLQQLKALLNHLD CCCHHHHHHHHCCCC	32.42	21906983
77	N-linked_Glycosylation	DVGVGRGNVTQHVQG CCCCCCCCHHHHHCC	32.10	24927598
87	N-linked_Glycosylation	QHVQGHRNLSTCFSS HHHCCCCCHHHHCCC	32.44	24927598
99	Phosphorylation	FSSGDLFTAHNFSEQ CCCCCCEEECCCCCC	34.01	-
102	N-linked_Glycosylation	GDLFTAHNFSEQSRI CCCEEECCCCCCCCC	39.41	24927598
104	Phosphorylation	LFTAHNFSEQSRIGS CEEECCCCCCCCCCC	39.79	-
107	Phosphorylation	AHNFSEQSRIGSSEL ECCCCCCCCCCCHHH	23.09	-
256	Phosphorylation	NEHHHGHSHYASESL CCCCCCCCCCCCCCC	23.84	24719451
258	Phosphorylation	HHHGHSHYASESLPS CCCCCCCCCCCCCCC	18.16	24719451
260	Phosphorylation	HGHSHYASESLPSKK CCCCCCCCCCCCCHH	22.13	24719451
262	Phosphorylation	HSHYASESLPSKKDQ CCCCCCCCCCCHHHH	42.98	26657352
265	Phosphorylation	YASESLPSKKDQEEG CCCCCCCCHHHHHHC	58.60	26657352
267 (in isoform 1)	Ubiquitination	-	69.82	21906983
267 (in isoform 2)	Ubiquitination	-	69.82	21906983
267	Ubiquitination	SESLPSKKDQEEGVM CCCCCCHHHHHHCHH	69.82	2190698
276	Ubiquitination	QEEGVMEKLQNGDLD HHHCHHHHHHCCCCC	36.96	-
276 (in isoform 2)	Ubiquitination	-	36.96	-
291	Phosphorylation	HMIPQHCSSELDGKA CCCCHHHCCCCCCCC	25.40	28348404
292	Phosphorylation	MIPQHCSSELDGKAP CCCHHHCCCCCCCCC	47.80	28555341
297	Ubiquitination	CSSELDGKAPMVDEK HCCCCCCCCCCCCCE	49.32	-
297 (in isoform 2)	Ubiquitination	-	49.32	-
304	Ubiquitination	KAPMVDEKVIVGSLS CCCCCCCEEEEEEEC	32.56	-
304 (in isoform 2)	Ubiquitination	-	32.56	-
309	Phosphorylation	DEKVIVGSLSVQDLQ CCEEEEEEECHHHHH	13.43	23663014
311	Phosphorylation	KVIVGSLSVQDLQAS EEEEEEECHHHHHHH	21.30	22617229
318	Phosphorylation	SVQDLQASQSACYWL CHHHHHHHHHHHHHH	16.23	30108239
320	Phosphorylation	QDLQASQSACYWLKG HHHHHHHHHHHHHCC	20.15	27251275
322	S-palmitoylation	LQASQSACYWLKGVR HHHHHHHHHHHCCCC	2.80	29575903
326	Ubiquitination	QSACYWLKGVRYSDI HHHHHHHCCCCHHHH	41.01	-
326	Acetylation	QSACYWLKGVRYSDI HHHHHHHCCCCHHHH	41.01	20167786

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 S39AE_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
102	N	Glycosylation		19349973
N-glycosylation at Asn-102 is required for iron-regulated extraction of the transporter from membranes and subsequent proteasomal degradation.

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 S39AE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of S39AE_HUMAN !!

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 S39AE_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77 AND ASN-102, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77, AND MASS SPECTROMETRY.	19159218 [Abstract]

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