Q9NRX5 (SERC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine incorporator 1

Alternative name(s):
Tumor differentially expressed protein 1-like
Tumor differentially expressed protein 2

Gene names

Name:	SERINC1
Synonyms:	KIAA1253, TDE1L, TDE2
ORF Names:	UNQ396/PRO732

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Enhances the incorporation of serine into phosphatidylserine and sphingolipids By similarity.
Subunit structure	Interacts with SPTLC1 By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the TDE1 family.
Sequence caution	The sequence BAA86567.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylserine metabolic process Inferred from sequence or structural similarity. Source: HGNC phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transferase activity Inferred from sequence or structural similarity. Source: HGNC sphingolipid metabolic process Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: HGNC integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from sequence or structural similarity. Source: HGNC
Molecular_function	L-serine transmembrane transporter activity Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAX8	Q06710	2	EBI-2683145,EBI-2683132

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	Serine incorporator 1		PRO_0000218966
Regions
	Topological domain	1 – 39	39	Cytoplasmic Potential
	Transmembrane	40 – 60	21	Helical; Potential
	Topological domain	61 – 88	28	Lumenal Potential
	Transmembrane	89 – 109	21	Helical; Potential
	Topological domain	110 – 123	14	Cytoplasmic Potential
	Transmembrane	124 – 144	21	Helical; Potential
	Topological domain	145 – 151	7	Lumenal Potential
	Transmembrane	152 – 172	21	Helical; Potential
	Topological domain	173 – 197	25	Cytoplasmic Potential
	Transmembrane	198 – 218	21	Helical; Potential
	Topological domain	219 – 231	13	Lumenal Potential
	Transmembrane	232 – 252	21	Helical; Potential
	Topological domain	253 – 259	7	Cytoplasmic Potential
	Transmembrane	260 – 280	21	Helical; Potential
	Topological domain	281 – 309	29	Lumenal Potential
	Transmembrane	310 – 330	21	Helical; Potential
	Topological domain	331 – 387	57	Cytoplasmic Potential
	Transmembrane	388 – 408	21	Helical; Potential
	Topological domain	409 – 426	18	Lumenal Potential
	Transmembrane	427 – 447	21	Helical; Potential
	Topological domain	448 – 453	6	Cytoplasmic Potential
Amino acid modifications
	Modified residue	351	1	Phosphoserine Ref.11
	Modified residue	352	1	Phosphothreonine Ref.11
	Modified residue	361	1	Phosphoserine Ref.10 Ref.11
	Modified residue	364	1	Phosphoserine Ref.11
	Lipidation	2	1	N-myristoyl glycine Ref.14
	Glycosylation	298	1	N-linked (GlcNAc...) Ref.12
Natural variations
	Natural variant	199	1	L → V. Corresponds to variant rs13210569 [ dbSNP | Ensembl ].		VAR_052275
	Natural variant	216	1	F → V. Corresponds to variant rs13210446 [ dbSNP | Ensembl ].		VAR_052276
	Natural variant	225	1	S → G. Corresponds to variant rs17260829 [ dbSNP | Ensembl ].		VAR_052277
Experimental info
	Sequence conflict	89	1	A → S in AAH28607. Ref.9
	Sequence conflict	247	1	S → F in AAP97200. Ref.1
	Sequence conflict	247	1	S → F in AAP97211. Ref.1
	Sequence conflict	408	1	Y → S in AAQ88795. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9NRX5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3868DBF38165B78C	FASTA	453	50,495
	10 20 30 40 50 60 MGSVLGLCSM ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG 70 80 90 100 110 120 MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA 130 140 150 160 170 180 VHNGFWFFKF AAAIAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE 190 200 210 220 230 240 SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIVLFFVYY THPASCSENK AFISVNMLLC 250 260 270 280 290 300 VGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGYNTT 310 320 330 340 350 360 STVPKEGQSV QWWHAQGIIG LILFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGGAR 370 380 390 400 410 420 SDGSLEDGDD VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW 430 440 450 TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of TDE2, a plasma-membrane protein with 11 transmembrane helices, and its variable expression in human lung cancer and liver cancer tissues." Zhang M., Yu L., Wu Q., Zheng L.H., Wei Y.H., Wan B., Zhao S.Y. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[5]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Subthalamic nucleus.
[7]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Testis.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; THR-352; SER-361 AND SER-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-298, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[14]	"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system." Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T. Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF087902 mRNA. Translation: AAP97200.1. AF092436 Genomic DNA. Translation: AAP97211.1. AB033079 mRNA. Translation: BAA86567.1. Different initiation. AL137261 mRNA. Translation: CAB70662.2. AF164794 mRNA. Translation: AAF80758.1. AY358429 mRNA. Translation: AAQ88795.1. AK128781 mRNA. Translation: BAG54731.1. Z99129 Genomic DNA. Translation: CAD92585.1. CH471051 Genomic DNA. Translation: EAW48172.1. CH471051 Genomic DNA. Translation: EAW48173.1. BC028607 mRNA. Translation: AAH28607.1. BC033029 mRNA. Translation: AAH33029.1.
IPI	IPI00413817.
RefSeq	NP_065806.1. NM_020755.2.
UniGene	Hs.146668.
3D structure databases
ProteinModelPortal	Q9NRX5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRX5. 8 interactions.
STRING	9606.ENSP00000342962.
PTM databases
PhosphoSite	Q9NRX5.
Polymorphism databases
DMDM	25453298.
Proteomic databases
PaxDb	Q9NRX5.
PRIDE	Q9NRX5.
Protocols and materials databases
DNASU	57515.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339697; ENSP00000342962; ENSG00000111897. ENST00000368454; ENSP00000357439; ENSG00000111897.
GeneID	57515.
KEGG	hsa:57515.
UCSC	uc003pyy.1. human.
Organism-specific databases
CTD	57515.
GeneCards	GC06M122807.
HGNC	HGNC:13464. SERINC1.
HPA	HPA035738. HPA035739.
MIM	614548. gene.
neXtProt	NX_Q9NRX5.
PharmGKB	PA134973249.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG308011.
HOVERGEN	HBG025699.
InParanoid	Q9NRX5.
OMA	HVNCDVL.
OrthoDB	EOG4S4PGF.
PhylomeDB	Q9NRX5.
Gene expression databases
Bgee	Q9NRX5.
CleanEx	HS_SERINC1.
Genevestigator	Q9NRX5.
GermOnline	ENSG00000111897. Homo sapiens.
Family and domain databases
InterPro	IPR005016. TMS_TDE. [Graphical view]
PANTHER	PTHR10383. PTHR10383. 1 hit.
Pfam	PF03348. Serinc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SERINC1. human.
GenomeRNAi	57515.
NextBio	63885.
SOURCE	Search...

Entry information

Entry name

SERC1_HUMAN

Accession

Primary (citable) accession number: Q9NRX5
Secondary accession number(s): B3KY69 , E1P565, O75655, Q7Z2F5, Q8TAG1, Q9NTH8, Q9ULG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.