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Protein

SH2 domain-containing protein 4A

Gene

SH2D4A

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

Functioni

Inhibits estrogen-induced cell proliferation by competing with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG and repressing estrogen-induced proliferation. May play a role in T-cell development and function.2 Publications

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

GO - Biological processi

  • negative regulation of phosphatase activity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9H788.

Names & Taxonomyi

Protein namesi
Recommended name:
SH2 domain-containing protein 4A
Alternative name(s):
Protein SH(2)A
Protein phosphatase 1 regulatory subunit 38
Gene namesi
Name:SH2D4A
Synonyms:PPP1R38, SH2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:26102. SH2D4A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134891945.

Polymorphism and mutation databases

BioMutaiSH2D4A.
DMDMi74725117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454SH2 domain-containing protein 4APRO_0000233133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei124 – 1241PhosphoserineCombined sources
Modified residuei261 – 2611PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H788.
MaxQBiQ9H788.
PaxDbiQ9H788.
PeptideAtlasiQ9H788.
PRIDEiQ9H788.

PTM databases

iPTMnetiQ9H788.
PhosphoSiteiQ9H788.

Expressioni

Tissue specificityi

Ubiquitously expressed. Aberrantly expressed in some cancers.1 Publication

Gene expression databases

BgeeiQ9H788.
CleanExiHS_SH2D4A.
ExpressionAtlasiQ9H788. baseline and differential.
GenevisibleiQ9H788. HS.

Organism-specific databases

HPAiHPA001871.
HPA001919.

Interactioni

Subunit structurei

Interacts with ESR1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ALAS1P131963EBI-747035,EBI-3905054
CASKO149363EBI-747035,EBI-1215506
CCDC172P0C7W63EBI-747035,EBI-2548868
CDR2Q018503EBI-10308083,EBI-1181367
CEP70Q8NHQ13EBI-10308083,EBI-739624
CEP76Q8TAP63EBI-747035,EBI-742887
DBNLQ9UJU66EBI-747035,EBI-751783
FSD2A1L4K13EBI-747035,EBI-5661036
GOLGA2Q083793EBI-10308083,EBI-618309
HCLS1P143174EBI-747035,EBI-750369
HMBOX1Q6NT763EBI-747035,EBI-2549423
IKZF1Q134223EBI-747035,EBI-745305
KRT40Q6A1623EBI-747035,EBI-10171697
LDOC1O957513EBI-747035,EBI-740738
LZTS2Q9BRK43EBI-747035,EBI-741037
MAGEA11P433642EBI-747035,EBI-739552
MAGEA6P433603EBI-747035,EBI-1045155
MTUS2Q5JR593EBI-10308083,EBI-742948
NECAB2H3BTW23EBI-747035,EBI-10172876
NINLQ9Y2I63EBI-747035,EBI-719716
NUTM1Q86Y263EBI-747035,EBI-10178410
PDE4DIPQ5VU433EBI-747035,EBI-1105124
PNMA1Q8ND903EBI-747035,EBI-302345
PPP1CAP621362EBI-747035,EBI-357253
PPP1CBP621406EBI-747035,EBI-352350
PSTPIP1O435863EBI-747035,EBI-1050964
RINT1Q6NUQ13EBI-747035,EBI-726876
SH3GL1Q6FGM03EBI-747035,EBI-10173690
SH3GL1Q999613EBI-747035,EBI-697911
SKAP1Q86WV13EBI-10308083,EBI-2477305
SORBS2O948753EBI-10308083,EBI-311323
SORBS3O605043EBI-747035,EBI-741237
SPAG5Q96R063EBI-747035,EBI-413317
STAM2O758863EBI-747035,EBI-373258
STX11O755583EBI-747035,EBI-714135
TACC1O754103EBI-747035,EBI-624237
TFIP11Q9UBB93EBI-10308083,EBI-1105213
TRAF2Q129333EBI-747035,EBI-355744
TRIM23P364063EBI-10308083,EBI-740098
TRIM27P143733EBI-747035,EBI-719493
UBXN11Q5T1243EBI-747035,EBI-746004
USHBP1Q8N6Y03EBI-10308083,EBI-739895
VPS52Q8N1B43EBI-747035,EBI-2799833
ZBTB16Q055163EBI-10308083,EBI-711925

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121977. 58 interactions.
IntActiQ9H788. 48 interactions.
MINTiMINT-1474891.
STRINGi9606.ENSP00000265807.

Structurei

3D structure databases

ProteinModelPortaliQ9H788.
SMRiQ9H788. Positions 347-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini347 – 44094SH2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi172 – 1776Poly-Ser

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiENOG410IEFY. Eukaryota.
ENOG410XPPJ. LUCA.
GeneTreeiENSGT00570000079047.
HOGENOMiHOG000031527.
HOVERGENiHBG057918.
InParanoidiQ9H788.
KOiK17577.
OMAiPYDVLCN.
OrthoDBiEOG71P2BD.
PhylomeDBiQ9H788.
TreeFamiTF336893.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9H788-1) [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
MLKQILSEMY IDPDLLAELS EEQKQILFFK MREEQIRRWK EREAAMERKE
60 70 80 90 100
SLPVKPRPKK ENGKSVHWKL GADKEVWVWV MGEHHLDKPY DVLCNEIIAE
110 120 130 140 150
RARLKAEQEA EEPRKTHSEE FTNSLKTKSQ YHDLQAPDNQ QTKDIWKKVA
160 170 180 190 200
EKEELEQGSR PAPTLEEEKI RSLSSSSRNI QQMLADSINR MKAYAFHQKK
210 220 230 240 250
ESMKKKQDEE INQIEEERTK QICKSWKEDS EWQASLRKSK AADEKRRSLA
260 270 280 290 300
KQAREDYKRL SLGAQKGRGG ERLQSPLRVP QKPERPPLPP KPQFLNSGAY
310 320 330 340 350
PQKPLRNQGV VRTLSSSAQE DIIRWFKEEQ LPLRAGYQKT SDTIAPWFHG
360 370 380 390 400
ILTLKKANEL LLSTGMPGSF LIRVSERIKG YALSYLSEDG CKHFLIDASA
410 420 430 440 450
DAYSFLGVDQ LQHATLADLV EYHKEEPITS LGKELLLYPC GQQDQLPDYL

ELFE
Length:454
Mass (Da):52,727
Last modified:March 1, 2001 - v1
Checksum:i2FC21D4E07FDA922
GO
Isoform 2 (identifier: Q9H788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MLKQILSEMYIDPDLLAELSEEQKQILFFKMREEQIRRWKEREAAMERKESLPVKPRPKK → MWRVIEPPCPGAPST

Note: No experimental confirmation available.
Show »
Length:409
Mass (Da):46,978
Checksum:iE7EE9D96502188B4
GO

Sequence cautioni

The sequence AAH67117.1 differs from that shown. Reason: Frameshift at position 392. Curated
The sequence AAO41715.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO41715.1 differs from that shown. Reason: Erroneous termination at position 455. Translated as stop.Curated
The sequence BAB14935.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951N → T in BAB14935 (PubMed:14702039).Curated
Sequence conflicti179 – 1791N → T in AAO41715 (PubMed:12476414).Curated
Sequence conflicti238 – 2381K → R in AAO41715 (PubMed:12476414).Curated
Sequence conflicti253 – 2531A → V in AAO41715 (PubMed:12476414).Curated
Sequence conflicti291 – 2911K → E in BAB14935 (PubMed:14702039).Curated
Sequence conflicti346 – 3461P → S in AAO41715 (PubMed:12476414).Curated
Sequence conflicti440 – 4401C → R in BAB14935 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091E → G.1 Publication
Corresponds to variant rs35647122 [ dbSNP | Ensembl ].
VAR_051350
Natural varianti216 – 2161E → G.1 Publication
Corresponds to variant rs4921637 [ dbSNP | Ensembl ].
VAR_026055
Natural varianti263 – 2631G → A.1 Publication
Corresponds to variant rs877386 [ dbSNP | Ensembl ].
VAR_026056
Natural varianti275 – 2751S → N.1 Publication
Corresponds to variant rs34608771 [ dbSNP | Ensembl ].
VAR_051351

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060MLKQI…PRPKK → MWRVIEPPCPGAPST in isoform 2. 1 PublicationVSP_042784Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024620 mRNA. Translation: BAB14935.1. Different initiation.
AK024799 mRNA. Translation: BAB15010.1.
AK293301 mRNA. Translation: BAG56822.1.
AC068880 Genomic DNA. No translation available.
BC014525 mRNA. Translation: AAH14525.2.
BC067117 mRNA. Translation: AAH67117.1. Frameshift.
BC082982 mRNA. Translation: AAH82982.1.
AY190323 mRNA. Translation: AAO41715.1. Sequence problems.
CCDSiCCDS55206.1. [Q9H788-2]
CCDS6009.1. [Q9H788-1]
RefSeqiNP_001167630.1. NM_001174159.1. [Q9H788-1]
NP_001167631.1. NM_001174160.1. [Q9H788-2]
NP_071354.2. NM_022071.3. [Q9H788-1]
UniGeneiHs.303208.

Genome annotation databases

EnsembliENST00000265807; ENSP00000265807; ENSG00000104611. [Q9H788-1]
ENST00000518040; ENSP00000429482; ENSG00000104611. [Q9H788-2]
ENST00000519207; ENSP00000428684; ENSG00000104611. [Q9H788-1]
GeneIDi63898.
KEGGihsa:63898.
UCSCiuc003wzb.4. human. [Q9H788-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024620 mRNA. Translation: BAB14935.1. Different initiation.
AK024799 mRNA. Translation: BAB15010.1.
AK293301 mRNA. Translation: BAG56822.1.
AC068880 Genomic DNA. No translation available.
BC014525 mRNA. Translation: AAH14525.2.
BC067117 mRNA. Translation: AAH67117.1. Frameshift.
BC082982 mRNA. Translation: AAH82982.1.
AY190323 mRNA. Translation: AAO41715.1. Sequence problems.
CCDSiCCDS55206.1. [Q9H788-2]
CCDS6009.1. [Q9H788-1]
RefSeqiNP_001167630.1. NM_001174159.1. [Q9H788-1]
NP_001167631.1. NM_001174160.1. [Q9H788-2]
NP_071354.2. NM_022071.3. [Q9H788-1]
UniGeneiHs.303208.

3D structure databases

ProteinModelPortaliQ9H788.
SMRiQ9H788. Positions 347-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121977. 58 interactions.
IntActiQ9H788. 48 interactions.
MINTiMINT-1474891.
STRINGi9606.ENSP00000265807.

PTM databases

iPTMnetiQ9H788.
PhosphoSiteiQ9H788.

Polymorphism and mutation databases

BioMutaiSH2D4A.
DMDMi74725117.

Proteomic databases

EPDiQ9H788.
MaxQBiQ9H788.
PaxDbiQ9H788.
PeptideAtlasiQ9H788.
PRIDEiQ9H788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265807; ENSP00000265807; ENSG00000104611. [Q9H788-1]
ENST00000518040; ENSP00000429482; ENSG00000104611. [Q9H788-2]
ENST00000519207; ENSP00000428684; ENSG00000104611. [Q9H788-1]
GeneIDi63898.
KEGGihsa:63898.
UCSCiuc003wzb.4. human. [Q9H788-1]

Organism-specific databases

CTDi63898.
GeneCardsiSH2D4A.
HGNCiHGNC:26102. SH2D4A.
HPAiHPA001871.
HPA001919.
MIMi614968. gene.
neXtProtiNX_Q9H788.
PharmGKBiPA134891945.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEFY. Eukaryota.
ENOG410XPPJ. LUCA.
GeneTreeiENSGT00570000079047.
HOGENOMiHOG000031527.
HOVERGENiHBG057918.
InParanoidiQ9H788.
KOiK17577.
OMAiPYDVLCN.
OrthoDBiEOG71P2BD.
PhylomeDBiQ9H788.
TreeFamiTF336893.

Enzyme and pathway databases

SignaLinkiQ9H788.

Miscellaneous databases

ChiTaRSiSH2D4A. human.
GeneWikiiSH2D4A.
GenomeRNAii63898.
PROiQ9H788.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H788.
CleanExiHS_SH2D4A.
ExpressionAtlasiQ9H788. baseline and differential.
GenevisibleiQ9H788. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2), VARIANTS GLY-209; GLY-216 AND ALA-263.
    Tissue: Adipose tissue.
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1), VARIANT ASN-275.
    Tissue: Ovary, Prostate and Uterus.
  4. "A novel member of SH(2) signaling protein family: cloning and characterization of SH(2)A gene."
    Dai S., Zhao Y., Ding Q.
    Zhonghua Yi Xue Yi Chuan Xue Za Zhi 19:458-462(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-454 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  5. "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.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Genetic analysis of SH2D4A, a novel adapter protein related to T cell-specific adapter and adapter protein in lymphocytes of unknown function, reveals a redundant function in T cells."
    Lapinski P.E., Oliver J.A., Kamen L.A., Hughes E.D., Saunders T.L., King P.D.
    J. Immunol. 181:2019-2027(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC pathway."
    Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.
    BMB Rep. 42:516-522(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1.
  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-261 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSH24A_HUMAN
AccessioniPrimary (citable) accession number: Q9H788
Secondary accession number(s): B4DDR1
, Q5XKC1, Q6NXE9, Q86YM2, Q96C88, Q9H7F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 125 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 8
    Human chromosome 8: 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.