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P31948

- STIP1_HUMAN

UniProt

P31948 - STIP1_HUMAN

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Protein

Stress-induced-phosphoprotein 1

Gene

STIP1

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

Functioni

Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. response to stress Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-induced-phosphoprotein 1
Short name:
STI1
Alternative name(s):
Hsc70/Hsp90-organizing protein
Short name:
Hop
Renal carcinoma antigen NY-REN-11
Transformation-sensitive protein IEF SSP 3521
Gene namesi
Name:STIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:11387. STIP1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: ProtInc
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Stress-induced-phosphoprotein 1PRO_0000106372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei8 – 81N6-acetyllysine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei301 – 3011N6-acetyllysine1 Publication
Modified residuei312 – 3121N6-acetyllysine1 Publication
Modified residuei325 – 3251N6-acetyllysine1 Publication
Modified residuei344 – 3441N6-acetyllysine1 Publication
Modified residuei354 – 3541Phosphotyrosine1 Publication
Modified residuei446 – 4461N6-acetyllysine1 Publication
Modified residuei481 – 4811Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP31948.
PaxDbiP31948.
PRIDEiP31948.

2D gel databases

REPRODUCTION-2DPAGEIPI00013894.
UCD-2DPAGEP31948.

PTM databases

PhosphoSiteiP31948.

Expressioni

Gene expression databases

BgeeiP31948.
CleanExiHS_STIP1.
ExpressionAtlasiP31948. baseline and differential.
GenevestigatoriP31948.

Organism-specific databases

HPAiCAB017448.
HPA039291.
HPA044062.

Interactioni

Subunit structurei

Forms a complex with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84. Interacts with PACRG. Interacts with METTL21B. Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC117Q8IWD42EBI-1054052,EBI-3387963
CDC37L1Q7L3B62EBI-1054052,EBI-2841876
EGFRP005332EBI-1054052,EBI-297353

Protein-protein interaction databases

BioGridi116162. 63 interactions.
DIPiDIP-41085N.
IntActiP31948. 77 interactions.
MINTiMINT-132047.
STRINGi9606.ENSP00000305958.

Structurei

Secondary structure

1
543
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Helixi20 – 3314
Helixi38 – 5114
Helixi54 – 6714
Helixi72 – 8413
Helixi88 – 9912
Helixi106 – 11712
Helixi223 – 23715
Helixi241 – 25414
Helixi259 – 27214
Helixi275 – 29117
Helixi296 – 31217
Helixi316 – 32914
Helixi333 – 34816
Helixi359 – 37214
Helixi377 – 38711
Helixi394 – 40411
Turni405 – 4084
Helixi410 – 42314
Helixi428 – 44013
Helixi444 – 45714
Helixi459 – 4624
Helixi463 – 47513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELRX-ray1.90A223-352[»]
1ELWX-ray1.60A/B1-118[»]
2LNINMR-A356-477[»]
3ESKX-ray2.05A223-350[»]
3FWVX-ray2.20A/B223-349[»]
ProteinModelPortaliP31948.
SMRiP31948. Positions 2-118, 223-540.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati4 – 3734TPR 1Add
BLAST
Repeati38 – 7134TPR 2Add
BLAST
Repeati72 – 10534TPR 3Add
BLAST
Domaini130 – 16940STI1 1Add
BLAST
Repeati225 – 25834TPR 4Add
BLAST
Repeati259 – 29234TPR 5Add
BLAST
Repeati300 – 33334TPR 6Add
BLAST
Repeati360 – 39334TPR 7Add
BLAST
Repeati394 – 42734TPR 8Add
BLAST
Repeati428 – 46134TPR 9Add
BLAST
Domaini492 – 53140STI1 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 23918Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Domaini

The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.

Sequence similaritiesi

Contains 2 STI1 domains.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00750000117686.
HOGENOMiHOG000186562.
HOVERGENiHBG057820.
InParanoidiP31948.
KOiK09553.
OMAiCEKAIDV.
OrthoDBiEOG7BGHM5.
PhylomeDBiP31948.
TreeFamiTF300478.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 8 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P31948-1) [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
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK
60 70 80 90 100
KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK
110 120 130 140 150
HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP
160 170 180 190 200
TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP
210 220 230 240 250
PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK
260 270 280 290 300
AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
310 320 330 340 350
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE
360 370 380 390 400
RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR
410 420 430 440 450
AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV
460 470 480 490 500
YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS
510 520 530 540
DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR
Length:543
Mass (Da):62,639
Last modified:July 1, 1993 - v1
Checksum:i8E58ECA13825CB0E
GO
Isoform 2 (identifier: P31948-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MEQ → MESGSPMGEVEISRTIRTNGRGQRGYDWQCKRPIRVAEVRSSLHSWSLRW

Show »
Length:590
Mass (Da):68,080
Checksum:i76F4C7A16BFCBCA0
GO
Isoform 3 (identifier: P31948-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-97: Missing.

Show »
Length:519
Mass (Da):59,778
Checksum:i0D7C993B4B4E230E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841F → L in AAH39299. (PubMed:15489334)Curated
Sequence conflicti364 – 3641K → E in BAG59782. (PubMed:14702039)Curated
Sequence conflicti533 – 5331K → R in BAG59782. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 33MEQ → MESGSPMGEVEISRTIRTNG RGQRGYDWQCKRPIRVAEVR SSLHSWSLRW in isoform 2. 1 PublicationVSP_055034
Alternative sequencei74 – 9724Missing in isoform 3. 1 PublicationVSP_055035Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86752 mRNA. Translation: AAA58682.1.
BT020010 mRNA. Translation: AAV38813.1.
BT020011 mRNA. Translation: AAV38814.1.
CR536512 mRNA. Translation: CAG38750.1.
AK297319 mRNA. Translation: BAG59782.1.
AP005668 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74196.1.
CH471076 Genomic DNA. Translation: EAW74197.1.
BC002987 mRNA. Translation: AAH02987.1.
BC039299 mRNA. Translation: AAH39299.1.
CCDSiCCDS60827.1. [P31948-2]
CCDS60828.1. [P31948-3]
CCDS8058.1. [P31948-1]
PIRiA38093.
RefSeqiNP_001269581.1. NM_001282652.1. [P31948-2]
NP_001269582.1. NM_001282653.1. [P31948-3]
NP_006810.1. NM_006819.2. [P31948-1]
UniGeneiHs.337295.

Genome annotation databases

EnsembliENST00000305218; ENSP00000305958; ENSG00000168439. [P31948-1]
ENST00000358794; ENSP00000351646; ENSG00000168439. [P31948-2]
ENST00000538945; ENSP00000445957; ENSG00000168439. [P31948-3]
GeneIDi10963.
KEGGihsa:10963.
UCSCiuc001nyk.1. human. [P31948-1]

Polymorphism databases

DMDMi400042.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86752 mRNA. Translation: AAA58682.1 .
BT020010 mRNA. Translation: AAV38813.1 .
BT020011 mRNA. Translation: AAV38814.1 .
CR536512 mRNA. Translation: CAG38750.1 .
AK297319 mRNA. Translation: BAG59782.1 .
AP005668 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74196.1 .
CH471076 Genomic DNA. Translation: EAW74197.1 .
BC002987 mRNA. Translation: AAH02987.1 .
BC039299 mRNA. Translation: AAH39299.1 .
CCDSi CCDS60827.1. [P31948-2 ]
CCDS60828.1. [P31948-3 ]
CCDS8058.1. [P31948-1 ]
PIRi A38093.
RefSeqi NP_001269581.1. NM_001282652.1. [P31948-2 ]
NP_001269582.1. NM_001282653.1. [P31948-3 ]
NP_006810.1. NM_006819.2. [P31948-1 ]
UniGenei Hs.337295.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ELR X-ray 1.90 A 223-352 [» ]
1ELW X-ray 1.60 A/B 1-118 [» ]
2LNI NMR - A 356-477 [» ]
3ESK X-ray 2.05 A 223-350 [» ]
3FWV X-ray 2.20 A/B 223-349 [» ]
ProteinModelPortali P31948.
SMRi P31948. Positions 2-118, 223-540.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116162. 63 interactions.
DIPi DIP-41085N.
IntActi P31948. 77 interactions.
MINTi MINT-132047.
STRINGi 9606.ENSP00000305958.

PTM databases

PhosphoSitei P31948.

Polymorphism databases

DMDMi 400042.

2D gel databases

REPRODUCTION-2DPAGE IPI00013894.
UCD-2DPAGE P31948.

Proteomic databases

MaxQBi P31948.
PaxDbi P31948.
PRIDEi P31948.

Protocols and materials databases

DNASUi 10963.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305218 ; ENSP00000305958 ; ENSG00000168439 . [P31948-1 ]
ENST00000358794 ; ENSP00000351646 ; ENSG00000168439 . [P31948-2 ]
ENST00000538945 ; ENSP00000445957 ; ENSG00000168439 . [P31948-3 ]
GeneIDi 10963.
KEGGi hsa:10963.
UCSCi uc001nyk.1. human. [P31948-1 ]

Organism-specific databases

CTDi 10963.
GeneCardsi GC11P063953.
HGNCi HGNC:11387. STIP1.
HPAi CAB017448.
HPA039291.
HPA044062.
MIMi 605063. gene.
neXtProti NX_P31948.
PharmGKBi PA36196.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0457.
GeneTreei ENSGT00750000117686.
HOGENOMi HOG000186562.
HOVERGENi HBG057820.
InParanoidi P31948.
KOi K09553.
OMAi CEKAIDV.
OrthoDBi EOG7BGHM5.
PhylomeDBi P31948.
TreeFami TF300478.

Miscellaneous databases

ChiTaRSi STIP1. human.
EvolutionaryTracei P31948.
GeneWikii Hop_(protein).
GenomeRNAii 10963.
NextBioi 35473239.
PROi P31948.
SOURCEi Search...

Gene expression databases

Bgeei P31948.
CleanExi HS_STIP1.
ExpressionAtlasi P31948. baseline and differential.
Genevestigatori P31948.

Family and domain databases

Gene3Di 1.25.40.10. 3 hits.
InterProi IPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF00515. TPR_1. 8 hits.
PF13181. TPR_8. 1 hit.
[Graphical view ]
SMARTi SM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1."
    Honore B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.
    J. Biol. Chem. 267:8485-8491(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 3).
    Tissue: Brain.
  5. 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] (ISOFORMS 1 AND 2).
    Tissue: Lung and Testis.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND 534-543, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-44; 64-73; 79-87; 154-160; 253-272; 306-312; 352-364; 407-429; 454-462; 489-513 AND 534-543, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381.
    Tissue: Keratinocyte.
  11. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
    Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
    J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AA1.
  12. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  13. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
    Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
    J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACRG.
  14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-8; LYS-301; LYS-312; LYS-325; LYS-344 AND LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH METTL21B.
  23. "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine."
    Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I.
    Cell 101:199-210(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349.

Entry informationi

Entry nameiSTIP1_HUMAN
AccessioniPrimary (citable) accession number: P31948
Secondary accession number(s): B4DM70
, F5H0T1, G3XAD8, Q3ZCU9, Q5TZU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 159 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3