Full text data of NCKAP1L
NCKAP1L
(HEM1)
[Confidence: low (only semi-automatic identification from reviews)]
Nck-associated protein 1-like (Hematopoietic protein 1; Membrane-associated protein HEM-1)
Nck-associated protein 1-like (Hematopoietic protein 1; Membrane-associated protein HEM-1)
UniProt
P55160
ID NCKPL_HUMAN Reviewed; 1127 AA.
AC P55160; B4DUT5; Q52LW0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-DEC-2008, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Nck-associated protein 1-like;
DE AltName: Full=Hematopoietic protein 1;
DE AltName: Full=Membrane-associated protein HEM-1;
GN Name=NCKAP1L; Synonyms=HEM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=7643388; DOI=10.1006/jmbi.1995.0414;
RA Baumgartner S., Martin D., Chiquet-Ehrismann R., Sutton J., Desai A.,
RA Huang I., Kato K., Hromas R.;
RT "The HEM proteins: a novel family of tissue-specific transmembrane
RT proteins expressed from invertebrates through mammals with an
RT essential function in oogenesis.";
RL J. Mol. Biol. 251:41-49(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein;
CC Cytoplasmic side (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55160-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55160-2; Sequence=VSP_045191;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed only in cells of hematopoietic
CC origin.
CC -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35964.1; Type=Erroneous initiation;
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DR EMBL; M58285; AAA35964.1; ALT_INIT; mRNA.
DR EMBL; AK300783; BAG62447.1; -; mRNA.
DR EMBL; AC025570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96787.1; -; Genomic_DNA.
DR EMBL; BC093769; AAH93769.1; -; mRNA.
DR EMBL; BC093771; AAH93771.1; -; mRNA.
DR PIR; S36666; S36666.
DR RefSeq; NP_001171905.1; NM_001184976.1.
DR RefSeq; NP_005328.2; NM_005337.4.
DR UniGene; Hs.182014; -.
DR ProteinModelPortal; P55160; -.
DR MINT; MINT-1711041; -.
DR STRING; 9606.ENSP00000293373; -.
DR PhosphoSite; P55160; -.
DR DMDM; 218512111; -.
DR PaxDb; P55160; -.
DR PRIDE; P55160; -.
DR Ensembl; ENST00000293373; ENSP00000293373; ENSG00000123338.
DR Ensembl; ENST00000545638; ENSP00000445596; ENSG00000123338.
DR GeneID; 3071; -.
DR KEGG; hsa:3071; -.
DR UCSC; uc001sgc.4; human.
DR CTD; 3071; -.
DR GeneCards; GC12P054891; -.
DR HGNC; HGNC:4862; NCKAP1L.
DR HPA; HPA039490; -.
DR HPA; HPA040772; -.
DR MIM; 141180; gene.
DR neXtProt; NX_P55160; -.
DR PharmGKB; PA29239; -.
DR eggNOG; NOG287735; -.
DR HOGENOM; HOG000231880; -.
DR HOVERGEN; HBG006344; -.
DR InParanoid; P55160; -.
DR KO; K05750; -.
DR OMA; AFMALSF; -.
DR OrthoDB; EOG7TJ3H0; -.
DR GenomeRNAi; 3071; -.
DR NextBio; 12151; -.
DR PRO; PR:P55160; -.
DR ArrayExpress; P55160; -.
DR Bgee; P55160; -.
DR CleanEx; HS_NCKAP1L; -.
DR Genevestigator; P55160; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IMP:UniProtKB.
DR GO; GO:0030675; F:Rac GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IMP:UniProtKB.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IEP:UniProtKB.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; IMP:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR InterPro; IPR019137; Nck-associated_protein-1.
DR Pfam; PF09735; Nckap1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Membrane;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1127 Nck-associated protein 1-like.
FT /FTId=PRO_0000216175.
FT TRANSMEM 996 1016 Helical; (Potential).
FT VAR_SEQ 1 50 Missing (in isoform 2).
FT /FTId=VSP_045191.
FT VARIANT 391 391 T -> A (in dbSNP:rs7311877).
FT /FTId=VAR_059316.
FT VARIANT 402 402 S -> L (in dbSNP:rs2270581).
FT /FTId=VAR_049344.
FT CONFLICT 496 496 T -> H (in Ref. 1; AAA35964).
FT CONFLICT 768 769 NA -> KP (in Ref. 1; AAA35964).
FT CONFLICT 1060 1060 L -> V (in Ref. 1; AAA35964).
SQ SEQUENCE 1127 AA; 128153 MW; 9389BAB163BAEA45 CRC64;
MSLTSAYQHK LAEKLTILND RGQGVLIRMY NIKKTCSDPK SKPPFLLEKS MEPSLKYINK
KFPNIDVRNS TQHLGPVHRE KAEIIRFLTN YYQSFVDVME FRDHVYELLN TIDACQCHFD
INLNFDFTRS YLDLIVTYTS VILLLSRIED RRILIGMYNC AHEMLHGHGD PSFARLGQMV
LEYDHPLKKL TEEFGPHTKA VSGALLSLHF LFVRRNQGAE QWRSAQLLSL ISNPPAMINP
ANSDTMACEY LSVEVMERWI IIGFLLCHGC LNSNSQCQKL WKLCLQGSLY ITLIREDVLQ
VHKVTEDLFS SLKGYGKRVA DIKESKEHVI ANSGQFHCQR RQFLRMAVKE LETVLADEPG
LLGPKALFAF MALSFIRDEV TWLVRHTENV TKTKTPEDYA DSSIAELLFL LEGIRSLVRR
HIKVIQQYHL QYLARFDALV LSDIIQNLSV CPEEESIIMS SFVSILSSLN LKQVDNGEKF
EFSGLRLDWF RLQAYTSVAK APLHLHENPD LAKVMNLIVF HSRMLDSVEK LLVETSDLST
FCFHLRIFEK MFAMTLEESA MLRYAIAFPL ICAHFVHCTH EMCPEEYPHL KNHGLHHCNS
FLEELAKQTS NCVLEICAEQ RNLSEQLLPK HCATTISKAK NKKTRKQRQT PRKGEPERDK
PGAESHRKNR SIVTNMDKLH LNLTELALTM NHVYSFSVFE HTIFPSEYLS SHLEARLNRA
IVWLAGYNAT TQEIVRPSEL LAGVKAYIGF IQSLAQFLGA DASRVIRNAL LQQTQPLDSC
GEQTITTLYT NWYLESLLRQ ASSGTIILSP AMQAFVSLPR EGEQNFSAEE FSDISEMRAL
AELLGPYGMK FLSENLMWHV TSQIVELKKL VVENMDILVQ IRSNFSKPDL MASLLPQLTG
AENVLKRMTI IGVILSFRAM AQEGLREVFS SHCPFLMGPI ECLKEFVTPD TDIKVTLSIF
ELASAAGVGC DIDPALVAAI ANLKADTSSP EEEYKVACLL LIFLAVSLPL LATDPSSFYS
IEKDGYNNNI HCLTKAIIQV SAALFTLYNK NIETHLKEFL VVASVSLLQL GQETDKLKTR
NRESISLLMR LVVEESSFLT LDMLESCFPY VLLRNAYREV SRAFHLN
//
ID NCKPL_HUMAN Reviewed; 1127 AA.
AC P55160; B4DUT5; Q52LW0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-DEC-2008, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Nck-associated protein 1-like;
DE AltName: Full=Hematopoietic protein 1;
DE AltName: Full=Membrane-associated protein HEM-1;
GN Name=NCKAP1L; Synonyms=HEM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=7643388; DOI=10.1006/jmbi.1995.0414;
RA Baumgartner S., Martin D., Chiquet-Ehrismann R., Sutton J., Desai A.,
RA Huang I., Kato K., Hromas R.;
RT "The HEM proteins: a novel family of tissue-specific transmembrane
RT proteins expressed from invertebrates through mammals with an
RT essential function in oogenesis.";
RL J. Mol. Biol. 251:41-49(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein;
CC Cytoplasmic side (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55160-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55160-2; Sequence=VSP_045191;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed only in cells of hematopoietic
CC origin.
CC -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35964.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; M58285; AAA35964.1; ALT_INIT; mRNA.
DR EMBL; AK300783; BAG62447.1; -; mRNA.
DR EMBL; AC025570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96787.1; -; Genomic_DNA.
DR EMBL; BC093769; AAH93769.1; -; mRNA.
DR EMBL; BC093771; AAH93771.1; -; mRNA.
DR PIR; S36666; S36666.
DR RefSeq; NP_001171905.1; NM_001184976.1.
DR RefSeq; NP_005328.2; NM_005337.4.
DR UniGene; Hs.182014; -.
DR ProteinModelPortal; P55160; -.
DR MINT; MINT-1711041; -.
DR STRING; 9606.ENSP00000293373; -.
DR PhosphoSite; P55160; -.
DR DMDM; 218512111; -.
DR PaxDb; P55160; -.
DR PRIDE; P55160; -.
DR Ensembl; ENST00000293373; ENSP00000293373; ENSG00000123338.
DR Ensembl; ENST00000545638; ENSP00000445596; ENSG00000123338.
DR GeneID; 3071; -.
DR KEGG; hsa:3071; -.
DR UCSC; uc001sgc.4; human.
DR CTD; 3071; -.
DR GeneCards; GC12P054891; -.
DR HGNC; HGNC:4862; NCKAP1L.
DR HPA; HPA039490; -.
DR HPA; HPA040772; -.
DR MIM; 141180; gene.
DR neXtProt; NX_P55160; -.
DR PharmGKB; PA29239; -.
DR eggNOG; NOG287735; -.
DR HOGENOM; HOG000231880; -.
DR HOVERGEN; HBG006344; -.
DR InParanoid; P55160; -.
DR KO; K05750; -.
DR OMA; AFMALSF; -.
DR OrthoDB; EOG7TJ3H0; -.
DR GenomeRNAi; 3071; -.
DR NextBio; 12151; -.
DR PRO; PR:P55160; -.
DR ArrayExpress; P55160; -.
DR Bgee; P55160; -.
DR CleanEx; HS_NCKAP1L; -.
DR Genevestigator; P55160; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IMP:UniProtKB.
DR GO; GO:0030675; F:Rac GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IMP:UniProtKB.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IEP:UniProtKB.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
DR GO; GO:0042493; P:response to drug; IMP:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR InterPro; IPR019137; Nck-associated_protein-1.
DR Pfam; PF09735; Nckap1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Membrane;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1127 Nck-associated protein 1-like.
FT /FTId=PRO_0000216175.
FT TRANSMEM 996 1016 Helical; (Potential).
FT VAR_SEQ 1 50 Missing (in isoform 2).
FT /FTId=VSP_045191.
FT VARIANT 391 391 T -> A (in dbSNP:rs7311877).
FT /FTId=VAR_059316.
FT VARIANT 402 402 S -> L (in dbSNP:rs2270581).
FT /FTId=VAR_049344.
FT CONFLICT 496 496 T -> H (in Ref. 1; AAA35964).
FT CONFLICT 768 769 NA -> KP (in Ref. 1; AAA35964).
FT CONFLICT 1060 1060 L -> V (in Ref. 1; AAA35964).
SQ SEQUENCE 1127 AA; 128153 MW; 9389BAB163BAEA45 CRC64;
MSLTSAYQHK LAEKLTILND RGQGVLIRMY NIKKTCSDPK SKPPFLLEKS MEPSLKYINK
KFPNIDVRNS TQHLGPVHRE KAEIIRFLTN YYQSFVDVME FRDHVYELLN TIDACQCHFD
INLNFDFTRS YLDLIVTYTS VILLLSRIED RRILIGMYNC AHEMLHGHGD PSFARLGQMV
LEYDHPLKKL TEEFGPHTKA VSGALLSLHF LFVRRNQGAE QWRSAQLLSL ISNPPAMINP
ANSDTMACEY LSVEVMERWI IIGFLLCHGC LNSNSQCQKL WKLCLQGSLY ITLIREDVLQ
VHKVTEDLFS SLKGYGKRVA DIKESKEHVI ANSGQFHCQR RQFLRMAVKE LETVLADEPG
LLGPKALFAF MALSFIRDEV TWLVRHTENV TKTKTPEDYA DSSIAELLFL LEGIRSLVRR
HIKVIQQYHL QYLARFDALV LSDIIQNLSV CPEEESIIMS SFVSILSSLN LKQVDNGEKF
EFSGLRLDWF RLQAYTSVAK APLHLHENPD LAKVMNLIVF HSRMLDSVEK LLVETSDLST
FCFHLRIFEK MFAMTLEESA MLRYAIAFPL ICAHFVHCTH EMCPEEYPHL KNHGLHHCNS
FLEELAKQTS NCVLEICAEQ RNLSEQLLPK HCATTISKAK NKKTRKQRQT PRKGEPERDK
PGAESHRKNR SIVTNMDKLH LNLTELALTM NHVYSFSVFE HTIFPSEYLS SHLEARLNRA
IVWLAGYNAT TQEIVRPSEL LAGVKAYIGF IQSLAQFLGA DASRVIRNAL LQQTQPLDSC
GEQTITTLYT NWYLESLLRQ ASSGTIILSP AMQAFVSLPR EGEQNFSAEE FSDISEMRAL
AELLGPYGMK FLSENLMWHV TSQIVELKKL VVENMDILVQ IRSNFSKPDL MASLLPQLTG
AENVLKRMTI IGVILSFRAM AQEGLREVFS SHCPFLMGPI ECLKEFVTPD TDIKVTLSIF
ELASAAGVGC DIDPALVAAI ANLKADTSSP EEEYKVACLL LIFLAVSLPL LATDPSSFYS
IEKDGYNNNI HCLTKAIIQV SAALFTLYNK NIETHLKEFL VVASVSLLQL GQETDKLKTR
NRESISLLMR LVVEESSFLT LDMLESCFPY VLLRNAYREV SRAFHLN
//
MIM
141180
*RECORD*
*FIELD* NO
141180
*FIELD* TI
*141180 HEMATOPOIETIC PROTEIN HEM-1; HEM1
*FIELD* TX
CLONING
Hromas et al. (1991) obtained cDNAs 3.8 kb in length containing a long
read moreopen reading frame and showing hybridization exclusively to transcripts
from hematopoietic cells. The protein, which they called HEM1, contains
8 potential membrane domains and 2 possible cAMP/cGMP phosphorylation
sites.
MAPPING
By hybridization to flow-sorted chromosomes, Hromas et al. (1991) mapped
the HEM1 gene to chromosome 12. Using in situ hybridization, they
localized it to chromosome 12q13.1, a region of occasional
translocations in hematopoietic neoplasia and the site of a rare folic
acid fragile site.
ANIMAL MODEL
Using chemical mutagenesis and positional cloning, Park et al. (2008)
obtained mice with a mutation in exon 13 of the Hem1 gene, resulting in
a gln445-to-ter substitution. Mice lacking Hem1 had defective F-actin
(see 102610) polymerization and actin capping in lymphocytes and
neutrophils due to loss of the Rac (see 602048)-controlled actin
regulatory WAVE (WASF1; 605035) protein complex. T-cell development was
disrupted at the Cd4 (186940)/Cd8 (see 186910) double-negative to
Cd4/Cd8 double-positive stage, and T-cell activation and adhesion were
impaired. Hem1-deficient neutrophils failed to migrate in response to
chemotactic signals and were deficient in phagocytosing bacteria. Other
Rac-dependent functions, such as Th1 differentiation and Nfkb (see
164011)-dependent proinflammatory cytokine transcription, were
unimpaired, whereas production of Th17 cells (see 603149) was enhanced.
Park et al. (2008) concluded that HEM1 is essential for hematopoietic
cell development, function, and homeostasis by controlling a pathway
leading to cytoskeletal reorganization.
*FIELD* RF
1. Hromas, R.; Collins, S.; Raskind, W.; Deaven, L.; Kaushansky, K.
: Hem-1, a potential membrane protein, with expression restricted
to blood cells. Biochim. Biophys. Acta 1090: 241-244, 1991.
2. Park, H.; Staehling-Hampton, K.; Appleby, M. W.; Brunkow, M. E.;
Habib, T.; Zhang, Y.; Ramsdell, F.; Liggitt, H. D.; Freie, B.; Tsang,
M.; Carlson, G.; Friend, S.; Frevert, C.; Iritani, B. M.: A point
mutation in the murine Hem1 gene reveals an essential role for hematopoietic
protein 1 in lymphopoiesis and innate immunity. J. Exp. Med. 205:
2899-2913, 2008.
*FIELD* CN
Paul J. Converse - updated: 3/27/2009
*FIELD* CD
Victor A. McKusick: 1/26/1993
*FIELD* ED
mgross: 03/30/2009
mgross: 3/30/2009
terry: 3/27/2009
carol: 2/9/1993
carol: 1/26/1993
*RECORD*
*FIELD* NO
141180
*FIELD* TI
*141180 HEMATOPOIETIC PROTEIN HEM-1; HEM1
*FIELD* TX
CLONING
Hromas et al. (1991) obtained cDNAs 3.8 kb in length containing a long
read moreopen reading frame and showing hybridization exclusively to transcripts
from hematopoietic cells. The protein, which they called HEM1, contains
8 potential membrane domains and 2 possible cAMP/cGMP phosphorylation
sites.
MAPPING
By hybridization to flow-sorted chromosomes, Hromas et al. (1991) mapped
the HEM1 gene to chromosome 12. Using in situ hybridization, they
localized it to chromosome 12q13.1, a region of occasional
translocations in hematopoietic neoplasia and the site of a rare folic
acid fragile site.
ANIMAL MODEL
Using chemical mutagenesis and positional cloning, Park et al. (2008)
obtained mice with a mutation in exon 13 of the Hem1 gene, resulting in
a gln445-to-ter substitution. Mice lacking Hem1 had defective F-actin
(see 102610) polymerization and actin capping in lymphocytes and
neutrophils due to loss of the Rac (see 602048)-controlled actin
regulatory WAVE (WASF1; 605035) protein complex. T-cell development was
disrupted at the Cd4 (186940)/Cd8 (see 186910) double-negative to
Cd4/Cd8 double-positive stage, and T-cell activation and adhesion were
impaired. Hem1-deficient neutrophils failed to migrate in response to
chemotactic signals and were deficient in phagocytosing bacteria. Other
Rac-dependent functions, such as Th1 differentiation and Nfkb (see
164011)-dependent proinflammatory cytokine transcription, were
unimpaired, whereas production of Th17 cells (see 603149) was enhanced.
Park et al. (2008) concluded that HEM1 is essential for hematopoietic
cell development, function, and homeostasis by controlling a pathway
leading to cytoskeletal reorganization.
*FIELD* RF
1. Hromas, R.; Collins, S.; Raskind, W.; Deaven, L.; Kaushansky, K.
: Hem-1, a potential membrane protein, with expression restricted
to blood cells. Biochim. Biophys. Acta 1090: 241-244, 1991.
2. Park, H.; Staehling-Hampton, K.; Appleby, M. W.; Brunkow, M. E.;
Habib, T.; Zhang, Y.; Ramsdell, F.; Liggitt, H. D.; Freie, B.; Tsang,
M.; Carlson, G.; Friend, S.; Frevert, C.; Iritani, B. M.: A point
mutation in the murine Hem1 gene reveals an essential role for hematopoietic
protein 1 in lymphopoiesis and innate immunity. J. Exp. Med. 205:
2899-2913, 2008.
*FIELD* CN
Paul J. Converse - updated: 3/27/2009
*FIELD* CD
Victor A. McKusick: 1/26/1993
*FIELD* ED
mgross: 03/30/2009
mgross: 3/30/2009
terry: 3/27/2009
carol: 2/9/1993
carol: 1/26/1993