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Q9UQ13

- SHOC2_HUMAN

UniProt

Q9UQ13 - SHOC2_HUMAN

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Protein

Leucine-rich repeat protein SHOC-2

Gene

SHOC2

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

Functioni

Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes.2 Publications

GO - Molecular functioni

  1. protein phosphatase binding Source: UniProtKB
  2. protein phosphatase regulator activity Source: UniProtKB

GO - Biological processi

  1. fibroblast growth factor receptor signaling pathway Source: UniProtKB
  2. positive regulation of Ras protein signal transduction Source: UniProtKB
  3. Ras protein signal transduction Source: UniProtKB
  4. regulation of catalytic activity Source: GOC
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9UQ13.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat protein SHOC-2
Alternative name(s):
Protein soc-2 homolog
Protein sur-8 homolog
Gene namesi
Name:SHOC2
Synonyms:KIAA0862
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:15454. SHOC2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Translocates from cytoplasm to nucleus upon growth factor stimulation.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. protein phosphatase type 1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Noonan syndrome-like disorder with loose anagen hair (NSLH) [MIM:607721]: A syndrome characterized by Noonan dysmorphic features such as macrocephaly, high forehead, hypertelorism, palpebral ptosis, low-set and posteriorly rotated ears, short and webbed neck, pectus anomalies, in association with pluckable, sparse, thin and slow-growing hair.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → G in NSLH; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane. 1 Publication
VAR_060199

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi607721. phenotype.
Orphaneti2701. Noonan syndrome-like disorder with loose anagen hair.
PharmGKBiPA37960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582Leucine-rich repeat protein SHOC-2PRO_0000097737Add
BLAST

Proteomic databases

MaxQBiQ9UQ13.
PaxDbiQ9UQ13.
PeptideAtlasiQ9UQ13.
PRIDEiQ9UQ13.

PTM databases

PhosphoSiteiQ9UQ13.

Expressioni

Gene expression databases

BgeeiQ9UQ13.
CleanExiHS_SHOC2.
ExpressionAtlasiQ9UQ13. baseline and differential.
GenevestigatoriQ9UQ13.

Organism-specific databases

HPAiHPA009164.

Interactioni

Subunit structurei

Interacts with M-Ras/MRAS, and RAF1. Forms a multiprotein complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts with ERBB2IP; disrupts the interaction with RAF1 and Ras, leading to prevent activation of the Ras signaling pathway. Specifically binds K-Ras/KRAS, M-Ras/MRAS and N-Ras/NRAS but not H-Ras/HRAS.3 Publications

Protein-protein interaction databases

BioGridi113729. 12 interactions.
IntActiQ9UQ13. 7 interactions.
MINTiMINT-131517.
STRINGi9606.ENSP00000358464.

Structurei

3D structure databases

ProteinModelPortaliQ9UQ13.
SMRiQ9UQ13. Positions 73-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati101 – 12222LRR 1Add
BLAST
Repeati124 – 14522LRR 2Add
BLAST
Repeati147 – 16923LRR 3Add
BLAST
Repeati170 – 19122LRR 4Add
BLAST
Repeati193 – 21422LRR 5Add
BLAST
Repeati216 – 23722LRR 6Add
BLAST
Repeati239 – 26022LRR 7Add
BLAST
Repeati262 – 28322LRR 8Add
BLAST
Repeati285 – 30723LRR 9Add
BLAST
Repeati308 – 32922LRR 10Add
BLAST
Repeati332 – 35322LRR 11Add
BLAST
Repeati356 – 37722LRR 12Add
BLAST
Repeati380 – 40021LRR 13Add
BLAST
Repeati403 – 42422LRR 14Add
BLAST
Repeati426 – 44823LRR 15Add
BLAST
Repeati449 – 47022LRR 16Add
BLAST
Repeati472 – 49423LRR 17Add
BLAST
Repeati495 – 51622LRR 18Add
BLAST
Repeati518 – 54023LRR 19Add
BLAST
Repeati542 – 56322LRR 20Add
BLAST

Sequence similaritiesi

Belongs to the SHOC2 family.Curated
Contains 20 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118833.
HOGENOMiHOG000116557.
HOVERGENiHBG055661.
InParanoidiQ9UQ13.
OMAiHGIGNLR.
OrthoDBiEOG773XFV.
PhylomeDBiQ9UQ13.
TreeFamiTF315742.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF12799. LRR_4. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 4 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 17 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UQ13) [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
MSSSLGKEKD SKEKDPKVPS AKEREKEAKA SGGFGKESKE KEPKTKGKDA
60 70 80 90 100
KDGKKDSSAA QPGVAFSVDN TIKRPNPAPG TRKKSSNAEV IKELNKCREE
110 120 130 140 150
NSMRLDLSKR SIHILPSSIK ELTQLTELYL YSNKLQSLPA EVGCLVNLMT
160 170 180 190 200
LALSENSLTS LPDSLDNLKK LRMLDLRHNK LREIPSVVYR LDSLTTLYLR
210 220 230 240 250
FNRITTVEKD IKNLSKLSML SIRENKIKQL PAEIGELCNL ITLDVAHNQL
260 270 280 290 300
EHLPKEIGNC TQITNLDLQH NELLDLPDTI GNLSSLSRLG LRYNRLSAIP
310 320 330 340 350
RSLAKCSALE ELNLENNNIS TLPESLLSSL VKLNSLTLAR NCFQLYPVGG
360 370 380 390 400
PSQFSTIYSL NMEHNRINKI PFGIFSRAKV LSKLNMKDNQ LTSLPLDFGT
410 420 430 440 450
WTSMVELNLA TNQLTKIPED VSGLVSLEVL ILSNNLLKKL PHGLGNLRKL
460 470 480 490 500
RELDLEENKL ESLPNEIAYL KDLQKLVLTN NQLTTLPRGI GHLTNLTHLG
510 520 530 540 550
LGENLLTHLP EEIGTLENLE ELYLNDNPNL HSLPFELALC SKLSIMSIEN
560 570 580
CPLSHLPPQI VAGGPSFIIQ FLKMQGPYRA MV
Length:582
Mass (Da):64,888
Last modified:June 20, 2001 - v2
Checksum:iF3F828646642A855
GO
Isoform 2 (identifier: Q9UQ13-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-279: Missing.

Note: No experimental confirmation available.

Show »
Length:536
Mass (Da):59,743
Checksum:i7F662A1A4580F3B7
GO

Sequence cautioni

The sequence BAA74885.2 differs from that shown. Reason: Erroneous initiation.
The sequence BAG52235.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAH72813.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti475 – 4751K → E in BAF85522. (PubMed:14702039)Curated
Sequence conflicti535 – 5351F → L in BAA74885. (PubMed:10048485)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → G in NSLH; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane. 1 Publication
VAR_060199

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei234 – 27946Missing in isoform 2. 1 PublicationVSP_038188Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068920 mRNA. Translation: AAC39856.1.
AF054828 mRNA. Translation: AAC25698.1.
AB020669 mRNA. Translation: BAA74885.2. Different initiation.
AK090820 mRNA. Translation: BAG52235.1. Different initiation.
AK292833 mRNA. Translation: BAF85522.1.
AL158163 Genomic DNA. Translation: CAH72812.1.
AL158163 Genomic DNA. Translation: CAH72813.1. Sequence problems.
CH471066 Genomic DNA. Translation: EAW49548.1.
BC050445 mRNA. Translation: AAH50445.1.
CCDSiCCDS58095.1. [Q9UQ13-2]
CCDS7568.1. [Q9UQ13-1]
RefSeqiNP_001255968.1. NM_001269039.1. [Q9UQ13-2]
NP_031399.2. NM_007373.3. [Q9UQ13-1]
UniGeneiHs.104315.

Genome annotation databases

EnsembliENST00000265277; ENSP00000265277; ENSG00000108061. [Q9UQ13-2]
ENST00000369452; ENSP00000358464; ENSG00000108061. [Q9UQ13-1]
GeneIDi8036.
KEGGihsa:8036.
UCSCiuc001kzl.4. human. [Q9UQ13-1]
uc001kzn.3. human. [Q9UQ13-2]

Polymorphism databases

DMDMi14423936.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

The matchmaker - Issue 121 of September 2010

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068920 mRNA. Translation: AAC39856.1 .
AF054828 mRNA. Translation: AAC25698.1 .
AB020669 mRNA. Translation: BAA74885.2 . Different initiation.
AK090820 mRNA. Translation: BAG52235.1 . Different initiation.
AK292833 mRNA. Translation: BAF85522.1 .
AL158163 Genomic DNA. Translation: CAH72812.1 .
AL158163 Genomic DNA. Translation: CAH72813.1 . Sequence problems.
CH471066 Genomic DNA. Translation: EAW49548.1 .
BC050445 mRNA. Translation: AAH50445.1 .
CCDSi CCDS58095.1. [Q9UQ13-2 ]
CCDS7568.1. [Q9UQ13-1 ]
RefSeqi NP_001255968.1. NM_001269039.1. [Q9UQ13-2 ]
NP_031399.2. NM_007373.3. [Q9UQ13-1 ]
UniGenei Hs.104315.

3D structure databases

ProteinModelPortali Q9UQ13.
SMRi Q9UQ13. Positions 73-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113729. 12 interactions.
IntActi Q9UQ13. 7 interactions.
MINTi MINT-131517.
STRINGi 9606.ENSP00000358464.

PTM databases

PhosphoSitei Q9UQ13.

Polymorphism databases

DMDMi 14423936.

Proteomic databases

MaxQBi Q9UQ13.
PaxDbi Q9UQ13.
PeptideAtlasi Q9UQ13.
PRIDEi Q9UQ13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265277 ; ENSP00000265277 ; ENSG00000108061 . [Q9UQ13-2 ]
ENST00000369452 ; ENSP00000358464 ; ENSG00000108061 . [Q9UQ13-1 ]
GeneIDi 8036.
KEGGi hsa:8036.
UCSCi uc001kzl.4. human. [Q9UQ13-1 ]
uc001kzn.3. human. [Q9UQ13-2 ]

Organism-specific databases

CTDi 8036.
GeneCardsi GC10P112679.
HGNCi HGNC:15454. SHOC2.
HPAi HPA009164.
MIMi 602775. gene.
607721. phenotype.
neXtProti NX_Q9UQ13.
Orphaneti 2701. Noonan syndrome-like disorder with loose anagen hair.
PharmGKBi PA37960.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00760000118833.
HOGENOMi HOG000116557.
HOVERGENi HBG055661.
InParanoidi Q9UQ13.
OMAi HGIGNLR.
OrthoDBi EOG773XFV.
PhylomeDBi Q9UQ13.
TreeFami TF315742.

Enzyme and pathway databases

SignaLinki Q9UQ13.

Miscellaneous databases

ChiTaRSi SHOC2. human.
GeneWikii SHOC2.
GenomeRNAii 8036.
NextBioi 30623.
PROi Q9UQ13.
SOURCEi Search...

Gene expression databases

Bgeei Q9UQ13.
CleanExi HS_SHOC2.
ExpressionAtlasi Q9UQ13. baseline and differential.
Genevestigatori Q9UQ13.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view ]
Pfami PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 4 hits.
[Graphical view ]
SMARTi SM00369. LRR_TYP. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 17 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "SUR-8, a conserved Ras-binding protein with leucine-rich repeats, positively regulates Ras-mediated signaling in C. elegans."
    Sieburth D.S., Sun Q., Han M.
    Cell 94:119-130(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH KRAS AND NRAS.
  2. "Soc-2 encodes a leucine-rich repeat protein implicated in fibroblast growth factor receptor signaling."
    Selfors L.M., Schutzman J.L., Borland C.Z., Stern M.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:6903-6908(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-582 (ISOFORM 2).
    Tissue: Amygdala and Trachea.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
    Tissue: Testis.
  8. "The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf."
    Li W., Han M., Guan K.-L.
    Genes Dev. 14:895-900(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Erbin inhibits RAF activation by disrupting the sur-8-Ras-Raf complex."
    Dai P., Xiong W.C., Mei L.
    J. Biol. Chem. 281:927-933(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB2IP.
  10. "A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic subunit of PP1 functions as an M-Ras effector to modulate Raf activity."
    Rodriguez-Viciana P., Oses-Prieto J., Burlingame A., Fried M., McCormick F.
    Mol. Cell 22:217-230(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MRAS AND RAF1, IDENTIFICATION IN A COMPLEX WITH PP1CA; PPP1CB; PPP1CC; RAF1 AND MRAS.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: VARIANT NSLH GLY-2, CHARACTERIZATION OF VARIANT NSLH GLY-2, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSHOC2_HUMAN
AccessioniPrimary (citable) accession number: Q9UQ13
Secondary accession number(s): A8K9W8
, B3KR23, O76063, Q5VZS8, Q5VZS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: October 29, 2014
This is version 132 of the entry and version 2 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 10
    Human chromosome 10: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3