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Q9UGT4

- SUSD2_HUMAN

UniProt

Q9UGT4 - SUSD2_HUMAN

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Protein

Sushi domain-containing protein 2

Gene

SUSD2

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

Functioni

May play a role in breast tumorigenesis.1 Publication

GO - Molecular functioni

  1. polysaccharide binding Source: InterPro
  2. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. immune response Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Sushi domain-containing protein 2
Gene namesi
Name:SUSD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:30667. SUSD2.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein Curated
Note: SUSD2 and LGALS1 co-localized in very specific, punctate regions along the cell membrane of breast cancer cells.1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134942464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 822795Sushi domain-containing protein 2PRO_0000249439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 44AlternatePROSITE-ProRule annotation
Disulfide bondi31 ↔ 35AlternatePROSITE-ProRule annotation
Disulfide bondi35 ↔ 62AlternatePROSITE-ProRule annotation
Disulfide bondi42 ↔ 55AlternatePROSITE-ProRule annotation
Disulfide bondi42 ↔ 44AlternatePROSITE-ProRule annotation
Disulfide bondi48 ↔ 54By similarity
Disulfide bondi55 ↔ 62AlternatePROSITE-ProRule annotation
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi522 – 5221N-linked (GlcNAc...)2 Publications
Disulfide bondi725 ↔ 765By similarity
Disulfide bondi751 ↔ 778By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9UGT4.
PaxDbiQ9UGT4.
PeptideAtlasiQ9UGT4.
PRIDEiQ9UGT4.

PTM databases

PhosphoSiteiQ9UGT4.

Expressioni

Tissue specificityi

Highly expressed in breast cancer, but shows a restricted expression pattern in normal tissues such as adipose, adrenal gland, kidney, lung, mammary gland, placenta, thyroid, trachea, and uterus.1 Publication

Gene expression databases

BgeeiQ9UGT4.
CleanExiHS_SUSD2.
GenevestigatoriQ9UGT4.

Organism-specific databases

HPAiHPA004117.

Interactioni

Subunit structurei

Interacts with LGALS1; leads to an increased amount of LGALS1 on the cell surface.1 Publication

Protein-protein interaction databases

BioGridi121109. 3 interactions.
IntActiQ9UGT4. 3 interactions.
MINTiMINT-4999571.
STRINGi9606.ENSP00000351075.

Structurei

3D structure databases

ProteinModelPortaliQ9UGT4.
SMRiQ9UGT4. Positions 24-92, 731-784.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 785758ExtracellularSequence AnalysisAdd
BLAST
Topological domaini807 – 82216CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei786 – 80621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6639SMBPROSITE-ProRule annotationAdd
BLAST
Domaini285 – 433149AMOPPROSITE-ProRule annotationAdd
BLAST
Domaini446 – 667222VWFDPROSITE-ProRule annotationAdd
BLAST
Domaini723 – 78058SushiPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AMOP domain.PROSITE-ProRule annotation
Contains 1 SMB (somatomedin-B) domain.Curated
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation
Contains 1 VWFD domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG299565.
GeneTreeiENSGT00730000110943.
HOGENOMiHOG000154448.
HOVERGENiHBG069278.
InParanoidiQ9UGT4.
OMAiAKWSYLY.
OrthoDBiEOG7FFMQX.
PhylomeDBiQ9UGT4.
TreeFamiTF321438.

Family and domain databases

InterProiIPR005533. AMOP.
IPR001212. Somatomedin_B_dom.
IPR000436. Sushi_SCR_CCP.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF03782. AMOP. 1 hit.
PF01033. Somatomedin_B. 1 hit.
PF00084. Sushi. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTiSM00723. AMOP. 1 hit.
SM00032. CCP. 1 hit.
SM00201. SO. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 1 hit.
PROSITEiPS50856. AMOP. 1 hit.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
PS50923. SUSHI. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UGT4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPALLPWAL LLLATALGPG PGPTADAQES CSMRCGALDG PCSCHPTCSG
60 70 80 90 100
LGTCCLDFRD FCLEILPYSG SMMGGKDFVV RHFKMSSPTD ASVICRFKDS
110 120 130 140 150
IQTLGHVDSS GQVHCVSPLL YESGRIPFTV SLDNGHSFPR AGTWLAVHPN
160 170 180 190 200
KVSMMEKSEL VNETRWQYYG TANTSGNLSL TWHVKSLPTQ TITIELWGYE
210 220 230 240 250
ETGMPYSQEW TAKWSYLYPL ATHIPNSGSF TFTPKPAPPS YQRWRVGALR
260 270 280 290 300
IIDSKNYAGQ KDVQALWTND HALAWHLSDD FREDPVAWAR TQCQAWEELE
310 320 330 340 350
DQLPNFLEEL PDCPCTLTQA RADSGRFFTD YGCDMEQGSV CTYHPGAVHC
360 370 380 390 400
VRSVQASLRY GSGQQCCYTA DGTQLLTADS SGGSTPDRGH DWGAPPFRTP
410 420 430 440 450
PRVPSMSHWL YDVLSFYYCC LWAPDCPRYM QRRPSNDCRN YRPPRLASAF
460 470 480 490 500
GDPHFVTFDG TNFTFNGRGE YVLLEAALTD LRVQARAQPG TMSNGTETRG
510 520 530 540 550
TGLTAVAVQE GNSDVVEVRL ANRTGGLEVL LNQEVLSFTE QSWMDLKGMF
560 570 580 590 600
LSVAAGDRVS IMLASGAGLE VSVQGPFLSV SVLLPEKFLT HTHGLLGTLN
610 620 630 640 650
NDPTDDFTLH SGRVLPPGTS PQELFLFGAN WTVHNASSLL TYDSWFLVHN
660 670 680 690 700
FLYQPKHDPT FEPLFPSETT LNPSLAQEAA KLCGDDHFCN FDVAATGSLS
710 720 730 740 750
TGTATRVAHQ LHQRRMQSLQ PVVSCGWLAP PPNGQKEGNR YLAGSTIYFH
760 770 780 790 800
CDNGYSLAGA ETSTCQADGT WSSPTPKCQP GRSYAVLLGI IFGGLAVVAA
810 820
VALVYVLLRR RKGNTHVWGA QP
Length:822
Mass (Da):90,208
Last modified:May 1, 2000 - v1
Checksum:i5B3E83862F045C90
GO

Sequence cautioni

The sequence BAB15481.1 differs from that shown. Reason: Frameshift at position 165.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti364 – 3641Q → R in BAB15481. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591R → Q.
Corresponds to variant rs17842275 [ dbSNP | Ensembl ].
VAR_027416
Natural varianti110 – 1101S → T.
Corresponds to variant rs9680526 [ dbSNP | Ensembl ].
VAR_027417
Natural varianti466 – 4661N → S.
Corresponds to variant rs8141797 [ dbSNP | Ensembl ].
VAR_027418

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z92546 Genomic DNA. Translation: CAB62953.1.
AK026431 mRNA. Translation: BAB15481.1. Frameshift.
BC033107 mRNA. Translation: AAH33107.1.
CCDSiCCDS13824.1.
RefSeqiNP_062547.1. NM_019601.3.
UniGeneiHs.131819.

Genome annotation databases

EnsembliENST00000358321; ENSP00000351075; ENSG00000099994.
GeneIDi56241.
KEGGihsa:56241.
UCSCiuc002zzn.1. human.

Polymorphism databases

DMDMi74735010.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z92546 Genomic DNA. Translation: CAB62953.1 .
AK026431 mRNA. Translation: BAB15481.1 . Frameshift.
BC033107 mRNA. Translation: AAH33107.1 .
CCDSi CCDS13824.1.
RefSeqi NP_062547.1. NM_019601.3.
UniGenei Hs.131819.

3D structure databases

ProteinModelPortali Q9UGT4.
SMRi Q9UGT4. Positions 24-92, 731-784.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121109. 3 interactions.
IntActi Q9UGT4. 3 interactions.
MINTi MINT-4999571.
STRINGi 9606.ENSP00000351075.

PTM databases

PhosphoSitei Q9UGT4.

Polymorphism databases

DMDMi 74735010.

Proteomic databases

MaxQBi Q9UGT4.
PaxDbi Q9UGT4.
PeptideAtlasi Q9UGT4.
PRIDEi Q9UGT4.

Protocols and materials databases

DNASUi 56241.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358321 ; ENSP00000351075 ; ENSG00000099994 .
GeneIDi 56241.
KEGGi hsa:56241.
UCSCi uc002zzn.1. human.

Organism-specific databases

CTDi 56241.
GeneCardsi GC22P024577.
HGNCi HGNC:30667. SUSD2.
HPAi HPA004117.
MIMi 615825. gene.
neXtProti NX_Q9UGT4.
PharmGKBi PA134942464.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG299565.
GeneTreei ENSGT00730000110943.
HOGENOMi HOG000154448.
HOVERGENi HBG069278.
InParanoidi Q9UGT4.
OMAi AKWSYLY.
OrthoDBi EOG7FFMQX.
PhylomeDBi Q9UGT4.
TreeFami TF321438.

Miscellaneous databases

GenomeRNAii 56241.
NextBioi 61848.
PROi Q9UGT4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGT4.
CleanExi HS_SUSD2.
Genevestigatori Q9UGT4.

Family and domain databases

InterProi IPR005533. AMOP.
IPR001212. Somatomedin_B_dom.
IPR000436. Sushi_SCR_CCP.
IPR001846. VWF_type-D.
[Graphical view ]
Pfami PF03782. AMOP. 1 hit.
PF01033. Somatomedin_B. 1 hit.
PF00084. Sushi. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view ]
SMARTi SM00723. AMOP. 1 hit.
SM00032. CCP. 1 hit.
SM00201. SO. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view ]
SUPFAMi SSF57535. SSF57535. 1 hit.
PROSITEi PS50856. AMOP. 1 hit.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
PS50923. SUSHI. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: Ileal mucosa.
  3. "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: Prostate.
  4. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-522.
    Tissue: Plasma.
  5. "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-522.
    Tissue: Liver.
  6. "Multiple functions of sushi domain containing 2 (SUSD2) in breast tumorigenesis."
    Watson A.P., Evans R.L., Egland K.A.
    Mol. Cancer Res. 11:74-85(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH LGALS1.

Entry informationi

Entry nameiSUSD2_HUMAN
AccessioniPrimary (citable) accession number: Q9UGT4
Secondary accession number(s): Q9H5Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 113 of the entry and version 1 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 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3