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Protein

Serologically defined colon cancer antigen 3

Gene

SDCCAG3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (By similarity). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1 (PubMed:23108400).By similarity2 Publications

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • protein transport Source: UniProtKB-KW
  • regulation of cytokinesis Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Serologically defined colon cancer antigen 3
Alternative name(s):
Antigen NY-CO-3
Gene namesi
Name:SDCCAG3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10667. SDCCAG3.

Subcellular locationi

  • Cytoplasm By similarity
  • Midbody 1 Publication
  • Early endosome 1 Publication
  • Recycling endosome 1 Publication

  • Note: During cytokinesis colocalized with PTPN13 at the midbody (PubMed:23108400). Colocalizes in a FAM21-dependent manner with the retromer CSC complex at endosomes (PubMed:25278552).

GO - Cellular componenti

  • early endosome Source: UniProtKB
  • endosome Source: UniProtKB
  • midbody Source: UniProtKB
  • recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901P → A: Disrupts interaction with PTPN13. 1 Publication
Mutagenesisi194 – 1941E → A: Disrupts interaction with PTPN13. 1 Publication

Organism-specific databases

PharmGKBiPA35597.

Polymorphism and mutation databases

BioMutaiSDCCAG3.
DMDMi172045853.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Serologically defined colon cancer antigen 3PRO_0000324285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei243 – 2431PhosphoserineCombined sources
Modified residuei247 – 2471PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96C92.
MaxQBiQ96C92.
PaxDbiQ96C92.
PRIDEiQ96C92.

PTM databases

iPTMnetiQ96C92.
PhosphoSiteiQ96C92.

Expressioni

Gene expression databases

BgeeiQ96C92.
CleanExiHS_SDCCAG3.
ExpressionAtlasiQ96C92. baseline and differential.
GenevisibleiQ96C92. HS.

Organism-specific databases

HPAiHPA029303.

Interactioni

Subunit structurei

Interacts with PTPN13, GIT1, VPS35 (PubMed:23108400, PubMed:25278552).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1M1Q9BXS53EBI-10178036,EBI-541426
DDX6P261963EBI-10178036,EBI-351257
SDCBPO005603EBI-10178036,EBI-727004
TFPTG5E9B53EBI-10178036,EBI-10178002

Protein-protein interaction databases

BioGridi116021. 52 interactions.
IntActiQ96C92. 42 interactions.
MINTiMINT-1375073.
STRINGi9606.ENSP00000349929.

Structurei

3D structure databases

ProteinModelPortaliQ96C92.
SMRiQ96C92. Positions 263-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 19826Required for interaction with PTPN131 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili261 – 371111Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SDCCAG3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHIY. Eukaryota.
ENOG4111TAC. LUCA.
GeneTreeiENSGT00390000000560.
HOVERGENiHBG058095.
InParanoidiQ96C92.
OMAiIRPAFMC.
OrthoDBiEOG7QK0BT.
PhylomeDBiQ96C92.
TreeFamiTF335840.

Family and domain databases

InterProiIPR026757. SDCCAG3.
[Graphical view]
PANTHERiPTHR31259. PTHR31259. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96C92-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGYQRRPGA TPLSRARSLA IPDAPAFYER RSCLPQLNCE RPHGRDLDSP
60 70 80 90 100
FFGIRPAFMC YVPSPVLASV GDTDFGYGKG KCSKQSPSGA HGTHFGDDRF
110 120 130 140 150
EDLEEANPFS FREFLKTKNL GLSKEDPASR IYAKEASRHS LGLDHNSPPS
160 170 180 190 200
QTGGYGLEYQ QPFFEDPTGA GDLLDEEEDE DTGWSGAYLP SAIEQTHPER
210 220 230 240 250
VPAGTSPCST YLSFFSTPSE LAGPESLPSW ALSDTDSRVS PASPAGSPSA
260 270 280 290 300
DFAVHGESLG DRHLRTLQIS YDALKDENSK LRRKLNEVQS FSEAQTEMVR
310 320 330 340 350
TLERKLEAKM IKEESDYHDL ESVVQQVEQN LELMTKRAVK AENHVVKLKQ
360 370 380 390 400
EISLLQAQVS NFQRENEALR CGQGASLTVV KQNADVALQN LRVVMNSAQA
410 420 430
SIKQLVSGAE TLNLVAEILK SIDRISEVKD EEEDS
Length:435
Mass (Da):47,961
Last modified:March 18, 2008 - v3
Checksum:i03EBD9512232B5E3
GO
Isoform 2 (identifier: Q96C92-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-97: Missing.

Show »
Length:412
Mass (Da):45,626
Checksum:iB246220F62D659E3
GO
Isoform 3 (identifier: Q96C92-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Show »
Length:377
Mass (Da):41,432
Checksum:i771C16B861EE61D1
GO
Isoform 4 (identifier: Q96C92-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-96: Missing.

Note: No experimental confirmation available.
Show »
Length:362
Mass (Da):40,058
Checksum:iEABA3B5233D003EB
GO

Sequence cautioni

The sequence BAA91607.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAI13936.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13942.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13943.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71R → H in AAH14515 (Ref. 4) Curated
Sequence conflicti343 – 3431N → T in AAQ56721 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571L → V.
Corresponds to variant rs7047681 [ dbSNP | Ensembl ].
VAR_039687
Natural varianti176 – 1761E → G.1 Publication
Corresponds to variant rs17851182 [ dbSNP | Ensembl ].
VAR_039688
Natural varianti304 – 3041R → Q.1 Publication
Corresponds to variant rs3812577 [ dbSNP | Ensembl ].
VAR_039689
Natural varianti379 – 3791V → M.1 Publication
Corresponds to variant rs1131992 [ dbSNP | Ensembl ].
VAR_039690
Natural varianti428 – 4281V → I.1 Publication
Corresponds to variant rs17855450 [ dbSNP | Ensembl ].
VAR_039691

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 3. 1 PublicationVSP_032176Add
BLAST
Alternative sequencei24 – 9673Missing in isoform 4. 1 PublicationVSP_040477Add
BLAST
Alternative sequencei75 – 9723Missing in isoform 2. 1 PublicationVSP_032177Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY349357 mRNA. Translation: AAQ56721.1.
CR597452 mRNA. No translation available.
AL592301 Genomic DNA. Translation: CAI13936.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13940.2.
AL592301 Genomic DNA. Translation: CAI13941.2.
AL592301 Genomic DNA. Translation: CAI13942.2. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13943.2. Sequence problems.
CH471090 Genomic DNA. Translation: EAW88230.1.
CH471090 Genomic DNA. Translation: EAW88231.1.
BC014515 mRNA. Translation: AAH14515.2.
AK001296 mRNA. Translation: BAA91607.1. Different initiation.
AF039688 mRNA. Translation: AAC18037.1.
CCDSiCCDS43903.1. [Q96C92-4]
CCDS43904.1. [Q96C92-1]
CCDS6999.2. [Q96C92-2]
RefSeqiNP_001034796.1. NM_001039707.1. [Q96C92-1]
NP_001034797.1. NM_001039708.1. [Q96C92-4]
NP_006634.3. NM_006643.3. [Q96C92-2]
UniGeneiHs.94300.

Genome annotation databases

EnsembliENST00000298537; ENSP00000298537; ENSG00000165689. [Q96C92-2]
ENST00000357365; ENSP00000349929; ENSG00000165689. [Q96C92-1]
ENST00000371725; ENSP00000360790; ENSG00000165689. [Q96C92-4]
GeneIDi10807.
KEGGihsa:10807.
UCSCiuc004chi.4. human. [Q96C92-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY349357 mRNA. Translation: AAQ56721.1.
CR597452 mRNA. No translation available.
AL592301 Genomic DNA. Translation: CAI13936.1. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13940.2.
AL592301 Genomic DNA. Translation: CAI13941.2.
AL592301 Genomic DNA. Translation: CAI13942.2. Sequence problems.
AL592301 Genomic DNA. Translation: CAI13943.2. Sequence problems.
CH471090 Genomic DNA. Translation: EAW88230.1.
CH471090 Genomic DNA. Translation: EAW88231.1.
BC014515 mRNA. Translation: AAH14515.2.
AK001296 mRNA. Translation: BAA91607.1. Different initiation.
AF039688 mRNA. Translation: AAC18037.1.
CCDSiCCDS43903.1. [Q96C92-4]
CCDS43904.1. [Q96C92-1]
CCDS6999.2. [Q96C92-2]
RefSeqiNP_001034796.1. NM_001039707.1. [Q96C92-1]
NP_001034797.1. NM_001039708.1. [Q96C92-4]
NP_006634.3. NM_006643.3. [Q96C92-2]
UniGeneiHs.94300.

3D structure databases

ProteinModelPortaliQ96C92.
SMRiQ96C92. Positions 263-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116021. 52 interactions.
IntActiQ96C92. 42 interactions.
MINTiMINT-1375073.
STRINGi9606.ENSP00000349929.

PTM databases

iPTMnetiQ96C92.
PhosphoSiteiQ96C92.

Polymorphism and mutation databases

BioMutaiSDCCAG3.
DMDMi172045853.

Proteomic databases

EPDiQ96C92.
MaxQBiQ96C92.
PaxDbiQ96C92.
PRIDEiQ96C92.

Protocols and materials databases

DNASUi10807.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298537; ENSP00000298537; ENSG00000165689. [Q96C92-2]
ENST00000357365; ENSP00000349929; ENSG00000165689. [Q96C92-1]
ENST00000371725; ENSP00000360790; ENSG00000165689. [Q96C92-4]
GeneIDi10807.
KEGGihsa:10807.
UCSCiuc004chi.4. human. [Q96C92-1]

Organism-specific databases

CTDi10807.
GeneCardsiSDCCAG3.
HGNCiHGNC:10667. SDCCAG3.
HPAiHPA029303.
neXtProtiNX_Q96C92.
PharmGKBiPA35597.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHIY. Eukaryota.
ENOG4111TAC. LUCA.
GeneTreeiENSGT00390000000560.
HOVERGENiHBG058095.
InParanoidiQ96C92.
OMAiIRPAFMC.
OrthoDBiEOG7QK0BT.
PhylomeDBiQ96C92.
TreeFamiTF335840.

Miscellaneous databases

ChiTaRSiSDCCAG3. human.
GenomeRNAii10807.
NextBioi41051.
PROiQ96C92.

Gene expression databases

BgeeiQ96C92.
CleanExiHS_SDCCAG3.
ExpressionAtlasiQ96C92. baseline and differential.
GenevisibleiQ96C92. HS.

Family and domain databases

InterProiIPR026757. SDCCAG3.
[Graphical view]
PANTHERiPTHR31259. PTHR31259. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Lin L., Yu R., Cao L., Ke R., Li H., Zhou G., Shen C., Zhong G., Xiao W., Li M., Yang S.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS GLN-304 AND MET-379.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2), VARIANT ILE-428.
    Tissue: Skin.
  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] OF 80-435 (ISOFORMS 1/3), VARIANT GLY-176.
  7. "Characterization of human colon cancer antigens recognized by autologous antibodies."
    Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
    Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 221-412.
    Tissue: Colon carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis."
    Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.
    Oncogene 32:4602-4613(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPN13 AND GIT1, MUTAGENESIS OF PRO-190 AND GLU-194.
  12. "Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma-membrane recycling."
    McGough I.J., Steinberg F., Gallon M., Yatsu A., Ohbayashi N., Heesom K.J., Fukuda M., Cullen P.J.
    J. Cell Sci. 127:4940-4953(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VPS35, SUBCELLULAR LOCATION.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSDCG3_HUMAN
AccessioniPrimary (citable) accession number: Q96C92
Secondary accession number(s): A6NCP1
, O60525, Q5SXN1, Q5SXN2, Q5SXN3, Q5SXN4, Q5SXN8, Q6V704, Q9NVY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 11, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.