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Protein

Scavenger receptor class F member 2

Gene

SCARF2

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

Functioni

Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL) (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Scavenger receptor class F member 2
Alternative name(s):
SRECRP-1
Scavenger receptor expressed by endothelial cells 2 protein
Short name:
SREC-II
Gene namesi
Name:SCARF2
Synonyms:SREC2, SREPCR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:19869. SCARF2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 441398ExtracellularSequence analysisAdd
BLAST
Transmembranei442 – 46221HelicalSequence analysisAdd
BLAST
Topological domaini463 – 870408CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Van den Ende-Gupta syndrome (VDEGS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by craniofacial and skeletal abnormalities that include blepharophimosis, a flat and wide nasal bridge, narrow and beaked nose, hypoplastic maxilla with or without cleft palate and everted lower lip, prominent ears, down-slanting eyes, arachnodactyly, and camptodactyly. Patients present congenital joint contractures that improve without intervention, and normal growth and development. Intelligence is normal. Rarely, enlarged cerebella can be present. Some patients experience respiratory problems due to laryngeal abnormalities.
See also OMIM:600920
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti258 – 2581C → Y in VDEGS. 1 Publication
VAR_065302

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiSCARF2.
MIMi600920. phenotype.
Orphaneti2460. Van den Ende-Gupta syndrome.
PharmGKBiPA134908523.

Polymorphism and mutation databases

BioMutaiSCARF2.
DMDMi380865486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343Sequence analysisAdd
BLAST
Chaini44 – 870827Scavenger receptor class F member 2PRO_0000007739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 86PROSITE-ProRule annotation
Disulfide bondi80 ↔ 98PROSITE-ProRule annotation
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence analysis
Disulfide bondi100 ↔ 109PROSITE-ProRule annotation
Disulfide bondi126 ↔ 134PROSITE-ProRule annotation
Disulfide bondi128 ↔ 141PROSITE-ProRule annotation
Disulfide bondi143 ↔ 152PROSITE-ProRule annotation
Disulfide bondi156 ↔ 163PROSITE-ProRule annotation
Disulfide bondi158 ↔ 170PROSITE-ProRule annotation
Disulfide bondi172 ↔ 181PROSITE-ProRule annotation
Disulfide bondi185 ↔ 193PROSITE-ProRule annotation
Disulfide bondi187 ↔ 200PROSITE-ProRule annotation
Disulfide bondi202 ↔ 211PROSITE-ProRule annotation
Disulfide bondi215 ↔ 222PROSITE-ProRule annotation
Disulfide bondi217 ↔ 229PROSITE-ProRule annotation
Disulfide bondi231 ↔ 240PROSITE-ProRule annotation
Disulfide bondi244 ↔ 251PROSITE-ProRule annotation
Disulfide bondi246 ↔ 258PROSITE-ProRule annotation
Disulfide bondi260 ↔ 269PROSITE-ProRule annotation
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence analysis
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi376 ↔ 384PROSITE-ProRule annotation
Disulfide bondi379 ↔ 391PROSITE-ProRule annotation
Disulfide bondi393 ↔ 402PROSITE-ProRule annotation
Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence analysis
Modified residuei551 – 5511PhosphoserineBy similarity
Modified residuei613 – 6131PhosphoserineCombined sources
Modified residuei628 – 6281PhosphotyrosineBy similarity
Modified residuei651 – 6511PhosphoserineCombined sources
Modified residuei653 – 6531PhosphoserineCombined sources
Modified residuei710 – 7101PhosphoserineBy similarity
Modified residuei718 – 7181PhosphoserineCombined sources
Modified residuei742 – 7421PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ96GP6.
PaxDbiQ96GP6.
PRIDEiQ96GP6.

PTM databases

iPTMnetiQ96GP6.
PhosphoSiteiQ96GP6.
SwissPalmiQ96GP6.

Expressioni

Tissue specificityi

Predominantly expressed in endothelial cells. Expressed in heart, placenta, lung, kidney, spleen, small intestine and ovary.1 Publication

Gene expression databases

BgeeiQ96GP6.
CleanExiHS_SCARF2.
ExpressionAtlasiQ96GP6. baseline and differential.
GenevisibleiQ96GP6. HS.

Organism-specific databases

HPAiHPA035079.

Interactioni

Subunit structurei

Homophilic and heterophilic interaction via its extracellular domain. Interacts with SCARF1. The heterophilic interaction with SCARF1, which is stronger than the homophilic interaction with itself, is suppressed by the presence of SCARF1 ligand such as Ac-LDL (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1752088,EBI-389883

Protein-protein interaction databases

BioGridi124803. 4 interactions.
IntActiQ96GP6. 4 interactions.
MINTiMINT-7240909.
STRINGi9606.ENSP00000266214.

Structurei

3D structure databases

ProteinModelPortaliQ96GP6.
SMRiQ96GP6. Positions 69-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 11040EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini122 – 15332EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini148 – 18235EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini183 – 21230EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 24129EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini236 – 27035EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini372 – 40332EGF-like 7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi648 – 847200Pro-richAdd
BLAST

Sequence similaritiesi

Contains 7 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1218. Eukaryota.
ENOG410XQWV. LUCA.
HOGENOMiHOG000015093.
HOVERGENiHBG023166.
InParanoidiQ96GP6.
OrthoDBiEOG77HDD8.
PhylomeDBiQ96GP6.
TreeFamiTF332598.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR033327. Scarf2.
[Graphical view]
PANTHERiPTHR24043:SF5. PTHR24043:SF5. 1 hit.
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96GP6-1) [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
MEGAGPRGAG PARRRGAGGP PSPLLPSLLL LLLLWMLPDT VAPQELNPRG
60 70 80 90 100
RNVCRAPGSQ VPTCCAGWRQ QGDECGIAVC EGNSTCSENE VCVRPGECRC
110 120 130 140 150
RHGYFGANCD TKCPRQFWGP DCKELCSCHP HGQCEDVTGQ CTCHARRWGA
160 170 180 190 200
RCEHACQCQH GTCHPRSGAC RCEPGWWGAQ CASACYCSAT SRCDPQTGAC
210 220 230 240 250
LCHAGWWGRS CNNQCACNSS PCEQQSGRCQ CRERTFGARC DRYCQCFRGR
260 270 280 290 300
CHPVDGTCAC EPGYRGKYCR EPCPAGFYGL GCRRRCGQCK GQQPCTVAEG
310 320 330 340 350
RCLTCEPGWN GTKCDQPCAT GFYGEGCSHR CPPCRDGHAC NHVTGKCTRC
360 370 380 390 400
NAGWIGDRCE TKCSNGTYGE DCAFVCADCG SGHCDFQSGR CLCSPGVHGP
410 420 430 440 450
HCNVTCPPGL HGADCAQACS CHEDTCDPVT GACHLETNQR KGVMGAGALL
460 470 480 490 500
VLLVCLLLSL LGCCCACRGK DPTRRPRPRR ELSLGRKKAP HRLCGRFSRI
510 520 530 540 550
SMKLPRIPLR RQKLPKVVVA HHDLDNTLNC SFLEPPSGLE QPSPSWSSRA
560 570 580 590 600
SFSSFDTTDE GPVYCVPHEE APAESRDPEV PTVPAEAPAP SPVPLTTPAS
610 620 630 640 650
AEEAIPLPAS SDSERSASSV EGPGGALYAR VARREARPAR ARGEIGGLSL
660 670 680 690 700
SPSPERRKPP PPDPATKPKV SWIHGKHSAA AAGRAPSPPP PGSEAAPSPS
710 720 730 740 750
KRKRTPSDKS AHTVEHGSPR TRDPTPRPPG LPEEATALAA PSPPRARARA
760 770 780 790 800
APRPLGAHGR RRSPAKRAEA ASMLAADVRG KTRSLGRAEV ALGAQGPREK
810 820 830 840 850
PAPPQKAKRS VPPASPARAP PATETPGPEK AATDLPAPET PRKKTPIQKP
860 870
PRKKSREAAG ELGRAGAPTL
Length:870
Mass (Da):92,479
Last modified:March 21, 2012 - v4
Checksum:iDCB735A50E6E9D1F
GO
Isoform 2 (identifier: Q96GP6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-478: Missing.

Show »
Length:865
Mass (Da):91,816
Checksum:i93B4D1E48CF6B771
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti629 – 64113ARVAR…RPARA → PTTTWITHSTAAS in AAH00584 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti750 – 76819AAPRP…PAKRA → GRGPGLLEPTDAGGPPRSAP in BAC53753 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti750 – 76819AAPRP…PAKRA → GRGPGLLEPTDAGGPPRSAP in BAD93345 (Ref. 3) CuratedAdd
BLAST
Sequence conflicti750 – 76819AAPRP…PAKRA → GRGPGLLEPTDAGGPPRSAP in EAX02965 (PubMed:11181995).CuratedAdd
BLAST
Sequence conflicti750 – 76819AAPRP…PAKRA → GRGPGLLEPTDAGGPPRSAP in AAH00584 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti750 – 76819AAPRP…PAKRA → GRGPGLLEPTDAGGPPRSAP in AAH09326 (PubMed:15489334).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741P → S.1 Publication
Corresponds to variant rs361566 [ dbSNP | Ensembl ].
VAR_059274
Natural varianti258 – 2581C → Y in VDEGS. 1 Publication
VAR_065302
Natural varianti425 – 4251T → S.
Corresponds to variant rs2241230 [ dbSNP | Ensembl ].
VAR_055776
Natural varianti499 – 4991R → C in a breast cancer sample; somatic mutation. 1 Publication
VAR_035837
Natural varianti522 – 5221H → L.
Corresponds to variant rs12484828 [ dbSNP | Ensembl ].
VAR_055777
Natural varianti777 – 7771D → E.4 Publications
Corresponds to variant rs759611 [ dbSNP | Ensembl ].
VAR_015148
Natural varianti778 – 7781V → L.4 Publications
Corresponds to variant rs759612 [ dbSNP | Ensembl ].
VAR_015149
Natural varianti819 – 8191A → G.
Corresponds to variant rs874100 [ dbSNP | Ensembl ].
VAR_015150
Natural varianti837 – 8371A → G.
Corresponds to variant rs874101 [ dbSNP | Ensembl ].
VAR_015151

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei474 – 4785Missing in isoform 2. 3 PublicationsVSP_042462

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052951 mRNA. Translation: BAC53753.1.
AF522196 mRNA. Translation: AAN45861.1.
AB024433 mRNA. Translation: BAD93345.1.
AC007731 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX02965.1.
BC000584 mRNA. Translation: AAH00584.2.
BC009326 mRNA. Translation: AAH09326.2.
RefSeqiNP_699165.3. NM_153334.6.
NP_878315.2. NM_182895.4.
UniGeneiHs.474251.

Genome annotation databases

EnsembliENST00000622235; ENSP00000477564; ENSG00000244486.
GeneIDi91179.
KEGGihsa:91179.
UCSCiuc062bsr.1. human. [Q96GP6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052951 mRNA. Translation: BAC53753.1.
AF522196 mRNA. Translation: AAN45861.1.
AB024433 mRNA. Translation: BAD93345.1.
AC007731 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX02965.1.
BC000584 mRNA. Translation: AAH00584.2.
BC009326 mRNA. Translation: AAH09326.2.
RefSeqiNP_699165.3. NM_153334.6.
NP_878315.2. NM_182895.4.
UniGeneiHs.474251.

3D structure databases

ProteinModelPortaliQ96GP6.
SMRiQ96GP6. Positions 69-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124803. 4 interactions.
IntActiQ96GP6. 4 interactions.
MINTiMINT-7240909.
STRINGi9606.ENSP00000266214.

PTM databases

iPTMnetiQ96GP6.
PhosphoSiteiQ96GP6.
SwissPalmiQ96GP6.

Polymorphism and mutation databases

BioMutaiSCARF2.
DMDMi380865486.

Proteomic databases

EPDiQ96GP6.
PaxDbiQ96GP6.
PRIDEiQ96GP6.

Protocols and materials databases

DNASUi91179.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000622235; ENSP00000477564; ENSG00000244486.
GeneIDi91179.
KEGGihsa:91179.
UCSCiuc062bsr.1. human. [Q96GP6-1]

Organism-specific databases

CTDi91179.
GeneCardsiSCARF2.
H-InvDBHIX0213276.
HGNCiHGNC:19869. SCARF2.
HPAiHPA035079.
MalaCardsiSCARF2.
MIMi600920. phenotype.
613619. gene.
neXtProtiNX_Q96GP6.
Orphaneti2460. Van den Ende-Gupta syndrome.
PharmGKBiPA134908523.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1218. Eukaryota.
ENOG410XQWV. LUCA.
HOGENOMiHOG000015093.
HOVERGENiHBG023166.
InParanoidiQ96GP6.
OrthoDBiEOG77HDD8.
PhylomeDBiQ96GP6.
TreeFamiTF332598.

Miscellaneous databases

ChiTaRSiSCARF2. human.
GenomeRNAii91179.
PROiQ96GP6.
SOURCEiSearch...

Gene expression databases

BgeeiQ96GP6.
CleanExiHS_SCARF2.
ExpressionAtlasiQ96GP6. baseline and differential.
GenevisibleiQ96GP6. HS.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR033327. Scarf2.
[Graphical view]
PANTHERiPTHR24043:SF5. PTHR24043:SF5. 1 hit.
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of SRECRP (scavenger receptor expressed by endothelial cell related protein)."
    Adachi H., Tsujimoto M.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS SER-174; GLU-777 AND LEU-778.
  2. "SREC-II, a new member of the scavenger receptor type F family, trans-interacts with SREC-I through its extracellular domain."
    Ishii J., Adachi H., Aoki J., Koizumi H., Tomita S., Suzuki T., Tsujimoto M., Inoue K., Arai H.
    J. Biol. Chem. 277:39696-39702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Epithelium.
  3. "A novel human nurse cell receptor NSR1."
    Kitaura M., Iwagami S., Tsuruta Y., Suzuki R.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLU-777 AND LEU-778.
    Tissue: Vulva.
  4. "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].
  5. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-777 AND LEU-778.
  6. "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] OF 272-870 (ISOFORM 2), VARIANTS GLU-777 AND LEU-778.
    Tissue: Brain.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-653 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-613; SER-653 AND SER-742, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-499.
  11. Cited for: VARIANT VDEGS TYR-258.

Entry informationi

Entry nameiSREC2_HUMAN
AccessioniPrimary (citable) accession number: Q96GP6
Secondary accession number(s): E5RFB8
, Q58A83, Q8IXF3, Q9BW74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 21, 2012
Last modified: June 8, 2016
This is version 134 of the entry and version 4 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

Caution

The conflict at position 750-768 is due to frameshifts. The frameshifted sequence is found in mouse.Curated

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

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.